Two fairly known examples of the effect of certain weather conditions on the body are dry hands due to decreased air humidity around us (more commonly in the winter, as described here), and flaring of arthritis immediately before or after it rains (as described here and here).
I was wondering if there are more examples of this kind, when what I am specifically looking for are bodily reactions through which one might be able to forecast or know something about the weather (i.e. if you have arthritis, you might be able to know it is going to rain sometime soon according to what you feel in your legs; if your hands are dry and chapped, you know that the air is drier than usual).
On having metal in your body (surgical implants, weather pains, and more)
I’ve found any discussion on surgical hardware sorely lacking. For years I assumed I was looking in the wrong places. At this point, I don’t think a solid discussion is out there. I’m near positive it doesn’t all exist in a comprehensive manner, which I’m hoping to ameliorate. My feeling is what may be obvious to the surgeons is not, at all, obvious to the recipients of surgeries. And, as we’ll see, there are certain things nobody is sure of, including the surgeons. Hopefully we can answer these questions.
When you place a foreign object in your body, there is a lot to discuss. Here is what we’re going to hit, in order. (You can click the section to be taken directly to it. Although, I recommend reading in order.)
This was an extraordinarily hard post to write. I’m not sure anything else I’ve worked on has ended up so mentally expansive. Unlike the majority of my writing, which comes solely from my own head, on this I had to enlist the help of quite a few different people, from quite a few different disciplines. I either talked to people directly, or indirectly used knowledge from areas such as:
- Exercise Science
I know I have a good amount of readers who are engineers, doctors, researchers, and some just all around smart people. If you feel I’ve missed something, please let me know and I will correct it. I’ve tried to strike a balance between accuracy and explaining things in a way all the everyday people with metal in their body can understand.
As the index above suggests, there is a lot in this beyond just having a foreign object in your body. Going through this reminded me of some particulars about how the body adapts, along with exposing me to things I didn’t know. I never thought I’d be reading documents from NASA about pressurized suits and boiling blood, then finding applications in that for everyday people.
I hope this is clear, that you learn something, and can put the information to use. Please share it if you find it helpful.
When hardware goes awry
“However, one would think stress concentrations must be of significance in orthopedic surgery, especially when the surgeon fits a stiff metal prosthesis to a relatively flexible bone.”
I work with a lot of people whose injury histories are longer than their life story. Obviously, this is usually older people. But I’ve trained one younger guy, 25 when I met him, who I too often think about.
Dan had a traumatic injury where he ended up needing quite a bit of surgical hardware in his body. At one point he had a metal rod and four metal screws in his leg. (He also had reconstructive ACL surgery, skin grafts, a bone graft, and more. Guy basically had a boulder fall on his legs.) By the time he got to me, some of the hardware had been removed, but a good amount remained.
After many months, I had to accept I wasn’t getting anywhere with Dan. His body wasn’t responding, and things just seemed off with him. He had been having a ton of issues exactly where one screw was located. Dan decided to get an X-Ray done on his mom’s, a veterinarian, machine. There was a ton of lysis (bone dissolution) going on right around the screw. Dan’s surgeon kept trying to avoid going back in, but this convinced them otherwise. (Don’t ask why Dan had to perform his own X-Ray.)
Turns out, the screw had broken in half, inside his bone. His bone was in a sense dying, and he had metal floating around within it. No wonder he had so many issues in that area.
He got the screw removed and within a few weeks was doing exponentially better.
Dan is one of those people who I like to say, “You have a body which hates foreign objects.” Some people go decades with all types of materials in them, never having a problem. Google “shrapnel in body” and you’ll come across loads of stories of soldiers going years and years with hundreds of bomb remnants inside them. Meanwhile, Dan had been progressively removing one thing after the other. His bones in particular did not agree with things. (We have to also acknowledge the possibility he had a surgeon who didn’t get things right.)
The hiccup with Dan was knowing the screw was broken. When Dan initially complained, nothing was unusual in his X-Rays. The screw was somehow broken in a way it wasn’t visible on radiographs. (Or someone missed it.) The bone dissolution also wasn’t apparent yet. This is one of the ways hardware really plays with people. You may have issues in the bone(s) but it doesn’t show up radiographically for months. It takes time until you can see the bone decaying on an X-Ray. (This interim period was one in which Dan tried things like mirror therapy. Along with too many painkillers.) 
Why hardware, and the material, matters
When it comes to placing screws in the body, we usually go with one of three options:
(Biabsorbable starts out similar to plastic. They then dissolve- absorb- within the body over time.)
Rather than detail the pros and cons of these devices, I’m going to borrow the following table from the paper Complications Associated With Use of Anterior Cruciate Ligament Fixation Devices. I will be focusing on the leg and often using reconstructive ACL surgery as a reference. (This is the surgery I’ve had.) The principles extend to the entire body though.
So, if you’re someone who is going to be having a lot of follow up imaging done, someone like Dan, metal may be a problem as it can cause issues. Whereas plastic is friendlier radiologically. Although, if a plastic screw moves around, plastic doesn’t show up on an X-Ray. It can be tough to know if it’s moved. If for some reason you wanted to get it removed, you’re looking at potential exploratory surgery.
Quick tangent, I’m not so sure plastic is completely unobservable on an X-Ray. You may not be able to see the actual screw, but if you look at my X-Rays, you can see where the screw is. Notice the tunneling?
Look at the tibial plateu on the right leg. (Left side in image.)
On the other hand, if you’re someone who needs a strong material to help hold your leg up, like Dan, what’s better, metal or plastic? What’s stronger? Metal, of course.
This is why we use metal to fixate broken bones. The purpose of the internal fixation is not just to hold the bones in place, it’s to do this and allow a person to move around more than they would when casted up, hopefully speeding up the rehabilitative process.  However, in the interim period of the bone healing, you need to insure it’s together. Plastic will not get the job done.
Looking at the table, we can see metal is actually so strong it can damage the graft used in anterior cruciate ligament reconstructions.
Stronger isn’t always better
Think of a rubber band being pinned on a wall, and pulling on the rubber. Now think about whether we use steel or plastic to pin the rubber band. Which material is more likely to tear the rubber band? The steel. If we pull on a plastic pin, the plastic has some give to it. Whereas steel is going to have much less. The steel pin is more likely to tear through the rubber than the plastic.
The steel is almost assuredly sharper too. When you pin a badge on a shirt, you’d rather have metal than plastic. The metal pushes through the material more easily.
An ACL graft isn’t quite fixated like this analogy suggests. Rather than the screw be inserted through the graft, the screw is often inserted more along the graft. It “interferes” with the graft. It’s an “interference screw.” Making things quite snug, so the graft stays put.
ACL tunnel with screw about to be inserted along graft. (Graft is behind screw in image.)
The analogy still holds though. If you are screwing damn near into rubber, what is more likely to tear the rubber, steel or plastic? The steel, because it’s so much harder and stronger. When pushing plastic in against the graft, there is going to be a bit more give.
Stressing vs Straining bone
“However, one would think stress concentrations must be of significance in orthopedic surgery, especially when the surgeon fits a stiff metal prosthesis to a relatively flexible bone.”
I bolded flexible bone because it’s important we remember bone does bend. All materials bend, we can’t always see it, but they do.
In something like reconstructive ACL surgery, and in many surgeries, the purpose of the screw is not to perform supportive work for the bones. The purpose of the material is to hold the graft in place until the bones can do it on their own. That’s all. In contrast to a broken bone fixation where the purpose is to help support the bone, the purpose of a screw fixation with a graft is to help the bone hold the graft in place. Eventually, the bone will remodel and secure the graft, but it needs help and time before that happens.
The fact a screw can help hold a graft in place is all well and good, but we’re still leaving a screw in the body. We’ve already discussed how a screw can damage the graft, but what about a screw’s impact on the loading of the bone? If you put too big a screw into a piece of wood, or you screw too violently, the wood cracks. The screw is often fine. The metal is stronger and stiffer than the wood.
Even if the screw doesn’t crack the wood on insertion, if you place too high a load on the wood, the wood will crack. Again, the screw may end up fine. The breaking point for the wood is much lower than the breaking point for the, say, steel. Furthermore, the wood may crack right around the screw.
Notice the vertical cracks above and below the screw.
One way to not break is to bend more. Like a ziploc bag. Rather than tear, it first stretches. The plastic will deform quickly, but it can take a lot more before it fractures. However, when a really stiff object is placed where another object would like to bend, the object can’t deform like it would prefer. Less ability to deform = greater tendency to crack.
This is especially true with bone. In the book Bone in Clinical Orthopedics, there is a fascinating discussion regarding how bone adapts. We tend to think of bone adapting to stress, the amount of force we place on it. This book makes the argument it’s not stress it’s strain -the amount of bone deformation. (Something like a ziploc bag can’t take a lot of stress before it deforms, but it can handle quite a bit of strain.)
If we think back to Dan, we gain a better understanding of why he’s had so many issues with hardware. I mentioned he also had a metal rod in him. One aspect of the rod is to help handle the force of his body, instead of his bone, while his bone heals. (It’s also to help the bone stay in place while it handles load. Rather than move around like a fractured bone would.)
An example. (From tetongravity.com)
However, with such a stiff material, the amount his bone can strain -deform- may be minimized. In Dan, it was. You could see his bone dying because it wasn’t being strained where the rod was. Above the rod and below the rod, his bone had become more dense, but between the rod it was becoming more porous. (Had more holes in it -less dense.)
When he had the rod removed, he immediately laid down a bunch of new bone. It appears without cyclically straining bone, it literally dies. As people die they move less, but the converse is also true. When you move less, parts of you begin to die. 
Say we have a piece of wood, and we put a screw in it. Then we place this piece of wood on top of the ground.
Next, we place a force on top of the wood, pushing into the ground:
The ground is then going to oppose that force:
While all this is going on, the screw is going to receive these forces as well:
And it too will have an opposing action:
Let’s take a step back for a moment. The first important surgical implication of all this is the fact the wood needs to receive this force from the screw. Not just when the wood is loaded, but upon immediate insertion of the screw. The wood needs to make room for the screw.
The implication is the wood will widen. You may not be able to eye ball it, but it happens. Here’s an exaggerated version (the yellow box represents where the wood originally was):
If you’re someone who has a screw in your body, you may have noticed your bones are a little differently shaped than they used to be. Bone expands like the wood.
For me, I swear my distal femur and proximal tibia, the bones making up the knee joint, have expanded. In all likelihood, they have. Nobody else would be able to tell or feel it, it’s not visually obvious, but I can feel it. These areas have been power drilled once by having a tunnel put through them -again, radially stressing the bone- and two by having hardware placed inside them.
The dashed lines represent where the femur and tibia were before being drilled through.
In ACL surgery, you drill tunnels through the bones for the graft to be placed in, then you screw that graft in the tunnel. It’s going to take time for that tunnel to close. In the meantime, through the drilling, we have removed a chunk of bone, yet are still going to be placing a lot, if not the same amount, of stress and strain on the bone. That is, we’ve taken some bone away yet want a person to get walking pretty quickly after surgery. The bone takes a good couple of months to come back, whereas we want someone walking within a couple of weeks or so. (Depending the surgery and other factors.)
So, on the remaining bone, we may actually be placing more stress and strain. Less bone but same amount of forces = greater amount of forces on remaining bone. It’s conceivable the remaining bone, that which hasn’t been drilled, hypertrophies to some extent as well, helping to handle the loads and strains placed on it.
In a couple of different ways, it makes sense why your bones look and feel different after a surgery.
While it can feel and look weird, I don’t think this is anything to worry about. Joints widening in response to traumatic events is pretty common. I’ve dislocated my fingers in response they’ve widened, a “periosteal reaction,” and it’s never been a problem.
Right side thicker than left.
I’ve actually also dislocated my right elbow, which is now larger than my left, and that also has never been an issue. During my football playing days, these types of things were quite common amongst my teammates and I, and I see it with clients regularly. I think this is a positive adaptation more than anything else.
As someone with a screw in their body, what I’ve been most concerned about is that opposing force of the screw.
Is it strong enough to cause the wood (bone) issues? Like a fracture? Again, like this:
There are two ways to think about this. First, we’re not made of wood. We’re made of bone. Which, as we’ll see, is a great thing.
Strengths of different materials
When it comes to deforming a material, you push or pull on it. When you push you compress when you pull you tension.
Although, this isn’t always true. Depending on where you push or pull, you may compress and tension at the same time. If we take a beam and push down on it at the center:
Then we’re actually compressing one end of the beam and tensioning the other at the same time:
Point being, we need to worry about the tensile and compressive strengths of the material(s) we put in our body. This is important because these two strengths are often different. Just because you can tension something a certain amount does not mean you can compress it an equal amount.
If you need to stack things, brick is great. But if you need to prevent tension, brick is terrible.
What about the materials we’re most concerned with? For metal, we’re going to use the most common, steel. For plastic, according to the ACL paper I linked above, PEEK and PET are the most commonly used plastic screws. Finally, our most important material, our bones.
These numbers are not the easiest to find. Amazingly (to me), none of this is addressed in any paper I can find on using materials inside the body. The ACL paper I linked was great…but mentioned none of this. (There may be a decent reason for this, which I’ll get to.) So, I kind of had to hodge podge these numbers.
For PET plastic, according to its Wikipedia page, the tensile strength is 55-75 MPa. (MegaPascals. I’m going to keep all the units in this form.) We’ll call it 65. According to this page, its compressive strength is 80. However, according to plastics international, the numbers are more like 80 and 100 respectively. We’ll go with the higher numbers for now.
For PEEK plastic, the tensile strength is
95 its compressive strength is
117, according to plastics international.
For steel, the numbers seem to be
475 tensile 250 compressive.
For bone, the numbers jump around quite a bit. This is due to the fact the strength of bone can vary between people, different people will have different densities, and other factors such as different bones in different areas of the body are going to have different strengths. Think a leg bone versus a finger bone. Wikipedia lists the tensile and compressive strengths at
170 respectively. From other sources, this seems right in the neighborhood. (Some sources are higher some are lower.)
- Plastic (using PEEK) = 95 tensile 117 compressive.
- Steel =475 tensile 250 compressive.
- Bone = 112 tensile 170 compressive.
Getting the numbers to be perfectly precise is not the point here. The point is:
Take a really thick book, like a textbook. Open the book at the halfway point. Place a really strong material inside the pages. Like a metal screw. Now close the book.
Because the strength of the material is so much stronger than the strength of the book’s materials, the book deforms. Even if you place some force on top of the book, that steel is going to push back significantly:
Take a weaker material though. Like a pen.
The book doesn’t deform nearly as much. Metal on left plastic on right:
Depending on the material, the book may not deform at all. It’s all relative with this.
With steel, we’re placing a really, really strong material inside the book (bone). With plastic, our bones aren’t going to deform as much. The plastic is what will deform, as our bones are much stronger than a textbook.
Entering volume into the equation
I mentioned there were two ways to look at this. One, what we just went over, is the strengths of the materials. The second aspect is the volumes of materials. When we’re screwing a steel screw into our bone, our bones are bringing a lot more soldiers to the fight. In ACL reconstruction, we’re inserting a relatively small screw into a relatively large tibial plateau.
So, even though the steel screw’s material is so much stronger than our bones, our bones can make up for things by having a lot more of itself.
Thinking back to Dan though, the opposite occurred. So much metal was brought to the fight that his bone was deforming more than it usually would in certain areas, and less than it normally would in other areas. It’s tough to have hard rules here. The type of surgery, amount of metal, material, orientation of fixation, bone density, all come into play.
I’ve talked to a decent amount of people about this. An orthopedic surgeon, veterinarian surgeon, engineers, people with some carpentry / woodworking experience, in all cases nobody thinks something like the ACL interference screw is going to present a bone loading issue. The size of the screw is a big factor, but so is the incredible ability of our bones to adapt.
In a pig, the radius and ulna are both weight bearing bones. There are documented accounts where if the ulna is removed, the radius will accommodate. All the way to the point where the strain on the osteotomized (bone removed) side will not be different than the opposite side. To be clear, one bone remodels enough to take the place of two bones!
In humans, there are circumstances, such as in bone grafts, where the fibula is removed, causing the tibia to have to increase its load and strain bearing.
In a study showing the awe-inspiring ability of the body to adapt and survive, the fibulas were removed from kids who needed a humeral reconstruction due to cancer. That is, take a fibula from the leg and place it in the arm to make a new humerus. Look at what happened to their tibias in response:
From the paper: Tibia Adaptation after Fibula Harvesting: An in Vivo Quantitative Study.
Notice the tibia on the left (right side of body) progressively increase in size in (B) and (C).
In these cases, the cross-sectional area for the side of the tibia without a fibula, ended up matching exactly that of the side of the tibia and fibula. That is, the tibia on one side became, on its own, the size of the tibia and fibula combined on the other side. The adaptations were that specific.
We’re talking removing an entire bone here. If bone can adapt to this, I doubt a little screw, or most implants, present a problem in this regard. Insuring the bone is able to be strained, but still held in place, like a broken bone fixation, seems to be much more the concern. You want the fracture to have a stable healing environment, but if the bone isn’t strained, we have issues. Too little strain is more a concern than too much.
Reconstructive ACL simulation
I actually took the time to get some bones, power drill a tunnel, screw some metal into the bone, then hammer it. (If you want to cause some discomfort, ask the guy at Home Depot how strong of a power drill you should buy to drill through bone.) I’m not sure how clear this will be, but I can tell you doing this gave me a better appreciation for how unlikely a screw is to be a concern in this regard. 
That bone in the video is not going to be as resilient as live bone because, well, it’s dead. I weakened the bone around the screw placement pretty significantly due how I drilled. (Had some trouble getting the right size.) And, that bone hasn’t been given anytime to remodel accordingly. Because the surrounding bone is going to be loaded a little more -if nothing else there is a little less bone now, due to the screw taking up that room- the bone is going to remodel accordingly. It’s going to get a bit stronger.
Through a myriad of perspectives, this doesn’t seem like something worth worrying about.
That doesn’t mean you’re in the clear (screw migration)
We have to keep in mind here, everything I’ve gone over is considering ideal circumstances. Going back to our book analogy, what if we place the screw not in the middle, but much closer to the top of the book?
We don’t have nearly as much material to offset the strength of the screw. Despite too little strain being more a concern than too much, that picture above makes me very nervous.
We already do this with many screw placements due to necessity, such as where a bone is broken or where you’re fixating a graft. (You wouldn’t fix an ACL graft at the mid-shin.) Also, say your surgeon is having an off day and accidentally screws too high or too low. We start getting to where the level of concern may grow.
Another thing to consider is screw migration. A screw moving around on someone is a common enough occurrence. The screw may start off where there is enough bone to offset it, but it may migrate to where a stress riser occurs. That is, the stress from the screw moves to a point where there’s not enough bone to counteract.
Why will a screw move?
Notice anything funky about the screws in this X-Ray?
This is one of the biggest issues with internal fixations: When you compound the strength of bone, with its ability to remodel, on top of having something like a 200 pound person walking, on top of thousands of cycles, even in something like steel, the material can start to deform and bend. It may even break.
This is what happened to Dan. Over time, the material can only handle so much. It literally will fatigue. Especially when you account for the fact bone can remodel -break a bit apart then get put back together- where as metal cannot.
If you google some X-Rays of screws and plates (internal fixations), you’ll quickly find quite a few examples of a screw looking not straight. This is fairly common.
A screw may move because of this, or it may end up moving due to the nature of the surgery. You know how screws have threading?
There’s no guarantee a person’s bone is going to catch that threading. In something like reconstructive ACL surgery, the screw is going to be placed not only against bone, but against tendon (the graft).
The other aspect of a screw is it’s conical-like shape.
Because of this, not all of the screw is even going to be touching bone.
Let’s look at the tibia from the side. We’ll have our tibial tunnel, the graft (green), and our interference screw:
Look at the distal aspect of the screw:
Due to the anatomy of a screw, when we place it inside the tunnel, some of it isn’t going to be touching anything.
In both circumstances, the screw touching tendon and the screw touching nothing, it’s tough for bone to catch the screw completely. So, what can happen then is, as the bone remodels, it can push the screw around. Some of the bone may remodel faster than the other, some may touch one part of the screw sooner, etc.
And this is again, assuming perfect screw placement. In reality, a surgeon isn’t always going to get things as snugly as they want. If you have a slightly loose screw that you start placing an entire human bodyweight on, it’s going to move around. What happens to a slightly loose screw that gets banged around on? It can become an even more loose screw.
This is where a metal screw’s strength can be an advantage. The threading of a metal screw is going to be more likely to nicely slice into bone, causing a stronger fixation. (However, notice in the picture how it can lacerate the graft!) With plastic, the bone is going to be better able to push the threading away, due to plastic’s lesser strength.
This is where the timelines during the rehabilitative process is crucial. The body needs time to remodel in accordance with the graft. You simply cannot rush this aspect. Doing so only increases your odds of ripping the graft, causing the screw to migrate, or imprudently loading your bones (risk of fracture), as they haven’t had time to adapt to their new loading pattern.
Regardless of the material or how carefully things are done though, this is where things simply suck. Whether the screw moves around or not is in some sense a crap shoot. And knowing whether the screw has moved, as well as finding the screw, is often quite hard. Remember Dan?
There are a few things I think one can be on the lookout for, to know whether the screw is moving or causing problems.
- For someone like Dan, laying down his symptoms were fine. But as soon as he placed a load on his bones, he had issues. If you’re someone where immediately upon standing you’re having problems, that’s a decent sign something is up with the hardware. (We’re talking a significant amount of time post-op though. This isn’t a day after surgery.) Opposed to if you’re someone who only has issues during certain activities. Where in that case it may be something else going on.
- If the symptoms are quite localized, that’s another good sign it’s the hardware causing the problem.
- If you’re able to feel where the screw is, has it moved? Is it changing positions?
Unfortunately, beyond an arthroscope, not a whole lot can be known for sure here. Radiology can’t pick up plastic, and even with metal there’s no guarantee you can see it. Despite Dan having metal and X-Rays, nobody knew the screw was broken until they went inside him. And his surgeon had to dig through his bone to find the screw’s remnants.
Not to mention, just because a piece of hardware has moved doesn’t mean you need to get it removed. Reminder: See all those soldiers with shrapnel in their body for years.
Only you can know if a piece of hardware is causing you enough issues that the costs of another surgery outweigh the issues you’re having.
If and why the weather influences things like metal implants or achy joints turns out to be quite a hard question to answer.
Part of the issue with this is how variable and individualistic pain can be. Just think about cold weather in general. So many people have so many different responses to it. Some love it, some hate it, some will move to other states to avoid it, some vacation in it. Psychologically, it’s impossible to say, “People have this response.”
I don’t like using the psychological explanation as a sufficient answer though. One could easily say “So and so has issues with metal implants and cold weather due to some previous experience, existing beliefs, blah blah.” One of the great aspects of pain science is its recognition pain is comprised of various elements. The psychological aspect here, I believe, is just one aspect to take into account.
We cannot ignore the body does have some common responses to cold weather, low pressure, and the fact materials like metal have different thermal properties than the body. Understanding these responses can, I think, give us a framework for how to respond should an issue come up.
Some primers on thermal effects
When things gain or lose heat, they respectively expand or contract. Metal, plastic, etc. It can get bigger or smaller in response to the temperature. We call this “thermal expansion.”
The body isn’t as clear cut, but it does provide some typical responses. One of those is, when it’s cold, a shuttling of blood from the limbs to the core. When you get cold, you never think “Man, my stomach is freezing!” But you often think “My hands / feet / toes / ears are killing me!” This is because as it gets colder, different parts of the skin are different temperatures.
The body constricts itself distally for the tradeoff of keeping things like the vital organs warmer. If you have to lose something, it’s better survival wise to lose a hand than it is a liver. Thermal expansion is still a factor, but the body is just more clever about it.
Have you ever wondered why metal seems to always feel cold? For instance, you take a thermos out of a refrigerator compared to a different material. Both materials have been in the same fridge, why does one feel so much colder?
This is where the body is a little tricky. When you touch metal what you are feeling isn’t actually the temperature, because the metal and every other material in that fridge are the same temperature. (Assuming they’ve all been in there a while.) What’s different is how quickly the material takes the heat from your grabbing hand. Your skin in sensing a loss of heat from your body, not how cold something actually is. We call this “thermal conductivity,” or the ability to grab heat, and metal is quite good at it.
Some good TV has come from this phenomenon:
This is why when you get out of a hot shower you may suddenly feel cold as hell, despite your house not being cold. Were you cold before the shower? No. But when you get out of a hot shower, your body has some more heat to give away. You suddenly feel cold because your body is sensing a huge sense of heat loss. Your body is literally giving heat to the room which has lesser heat. (It’s not colder, it’s technically less heated.) Things tend to even out like this.
Now let’s think about someone with a big metal rod in their leg.
Notice the direction the metal is placed in relative to the leg. It’s not on top, it’s not below, it’s coming at the body from the side. The “transverse plane.” This happens to be the direction our bones most dislike. It’s the direction our bones are weakest in. 
If we get colder, we know we’re likely to start constricting the limb. At the same time, our body is generating heat in an attempt to get warm / maintain current temperature. Due to this, our body is going to be particularly sensitive to something attempting to take that heat.
The body is constricting itself against a material which is grabbing heat from us, a material which is potentially expanding due to increased heat, a material which is much stronger than our constricting skin. Furthermore, this material may be expanding against a brittle material, our bones, in the direction our bones most dislike, especially considering that specific area of bone may be weakened (due to trauma or the fixation). All in an environment where our skin / body / brain is extra sensitive to heat loss, as well as an environment where most people tend to not feel great period. (Cold, damp, overcast, etc.)
This is why I think it’s been so hard to give people an explanation for “Why does my surgically repaired leg ache when it’s cold out?” It’s likely not just one factor. But a confluence of them.
“But what about the size of the metal relative to the size of our leg? Shouldn’t our leg, being bigger than the metal rod, be able to offset this?” (Generate enough heat.)
This is where the properties of metal come even more into play. Because our body has so much water in it, it’s actually hard to heat it up. When it comes to everyday materials, water is the hardest to heat up. It has a great “heat capacity.” That is, it can withstand a ton of heat. (This is one reason it’s so hard for humans to overheat. We’re made of so much water. We do great in the heat we don’t do nearly as well in cold weather.) Despite this, metal is so dense, about eight times that of most human tissue, it can make up for it’s relatively poor heat capacity by being so damn heavy. 
Meaning a relatively small metal rod in a relatively large leg, can still hold a ton of heat. Meaning it can take a lot of heat from our body. Meaning when you go outside, you may feel that metal for a while, because it can take heat from your body for a while.
This is where the location of the metal matters as well. If some of the metal is only covered by the skin, or it’s just not very deep in the body, then you have relatively thin skin being pushed against relatively thick metal. The metal is going to be able to take heat for quite a bit of time against that thin skin.
Just like a splinter feels odd / uncomfortable / painful under the skin, so too can metal. Particularly when the weather is certain conditions.
Next time it’s a bit cold out, just touch something made of metal. Like a pole. You will immediately feel how much colder the steel is relative to your body -how quickly it’s taking your heat. Just think if you then pressed that metal against your body perpetually. It wouldn’t feel great.
Now, say that metal is in your forearm. Or somewhere pretty far from your core. You then couple this all with the fact the body is constricting things distally. Meaning the body is being pulled against the steel / titanium / metal even more, and more than usual. It makes sense for people’s pain description in these scenarios to be customarily “aching” or “I can feel the cold metal under my skin.” The metal is constantly pushing outward on the contracting limb. If someone were to constantly push on any part of your body, it would begin to ache after a while.
Contrast this with warmer temperatures. The body isn’t constricting against the material like in the cold it’s, if anything, expanding.
This is a perk of plastic. It’s more malleable than metal, doesn’t conduct heat to the same degree, and isn’t going to present the same level of issues with the weather. The plastic is going to be better able to go with the flow, sort of speak.
The meat of this post is about surgical hardware being inserted in the body. And because the weather is so often a remark from those with hardware in them, it was fitting to spend some time on it. Even without hardware in the body though, it’s customary for people to say the weather influences their joints, or makes them aware of an old injury. (An old injury which may have accompanied hardware at some point.) So, I think it’s fitting to continue some more on weather here.
The research on weather and joint pain is a bit all over the place. One thing that seems to have some consistency though is when it comes to arthritis, it’s not the temperature that’s a problem, it’s the barometric pressure. Anecdotally, metal is more an issue in colder weather generalized joint pain is more an issue in lower pressure, and maybe colder weather.
Pressure in this instance is a metric of how much the earth’s air is pushing against our body. When the air doesn’t push as much, our bodies push against the air more.
This is one reason astronauts wear space suits. In space, there’s no atmospheric pressure against the body. The “pressurized” suit artificially generates this pressure. Without, the body would expand significantly, although NASA tells me it wouldn’t explode. Our skin is strong enough to hold things together. For NASA, the bodily expansion isn’t the biggest factor. Our blood boiling due to such low pressure is the more pressing concern.
Same idea when we get in airplanes. A cabin is “pressurized” because the further away from the earth’s center you get, the less air above you there is to push on you. This is why some of you may notice your feet swell when you fly. Less pressure on you = more pressure in your body = things swell.
Simple experiment to show this:
The best theory I’ve seen out there is when the pressure is lower, our joints expand. When you take an already inflamed / pissed off joint, like an arthritic one, and you have it expand more, some pain may result.
There is an important subtlety here though. It’s not that the joint expands like I’ve seen others state. It’s more the fluids (gas and liquid) within the joint expands. The joint is made of all types of things. Bone, fluids, ligaments, etc. If general expansion were an issue, we’d expect people to also have issues in the heat -things expand in heat too- which you basically never hear of. In the heat though, fluid can actually move more easily. Similar to magma from a volcano. As it cools, it doesn’t move as easily as when it’s on fire.
What I believe happens here is any expansion of a joint in the heat, and the problems that could cause, are offset by the easier flow of fluid through the joint.
Plus, when it comes to our environment, higher temperatures tend to go with higher pressures. So, if we increase the temperature -potential joint expansion- we usually increase the pressure -joint is constricted- offsetting one another.
In the cooler seasons, air molecules don’t move as quickly. If you remember back to elementary science, the Earth has different atmospheres, changing as you get further from the surface. The lowest level, the one humans primarily hang out in, adjusts its height based on the time of year. In the summer, it’s lower (closer to the Earth’s surface) in the winter, it’s higher.
When it’s lower, the pressure on us is higher, meaning the density of the atmosphere is higher (same amount of molecules in lesser amount of space), meaning the temperature is higher. When the atmosphere is higher, the pressure on us is lower, the density of the atmosphere is lower, the temperature of the atmosphere is lower.
This is where the distinction between weather and climate comes in. Much like a cold day here and there, or even a cold winter here and there (weather), doesn’t mean the earth isn’t warming on a longer scale (climate), just because the pressure is higher in the summer doesn’t mean there won’t be some days where it’s lower.
As a general rule though, lower pressure tends to accompany lower temperatures, which is the combination you most often hear influencing how people’s joints feel. However, there may be the occasional time where it’s decently warm out and you still have some issues. (The pressure dropped.) I live in San Diego and see this all the time. It’s 75 out, but suddenly someone doesn’t feel great. Or the occasional time where the temperature hasn’t changed much, but there was a good drop in pressure.
So, when someone asks you about the weather affecting how you feel, your memory goes immediately to “cold weather” because in your mind that’s much more often a negative influence on you. But it’s not so much “cold” weather as it is lower pressure. Particularly sudden drops, which can occur during any season, and in various geographies. That said, when it’s cold and the pressure is low, that’s probably when things feel the worst, so we think about that most, as how bad things get is a big part of our memories. 
Much like people handle temperature differently, people handle pressure differently. Some athletes respond very well to altitude training (increased red blood cell production), whereas others don’t get much out of it.
When the pressure lowers, some are going to have a negative effect where others are not. Some may boost blood circulation helping to remove the excess joint fluid, while others may not. Some are going to already have a higher starting pressure within their joint or body, like high blood pressure or excess fluid, where others won’t. Some are going to have a more sensitive nervous system. Some are going to hate cold weather which makes everything feel worse. You get the idea.
There is a recent review on weather influencing osteoarthritis pain. It goes through how, essentially, none of the research on this topic has been satisfactory. The best study is amazingly 50 years old, but has had follow up studies which conflict its results. Part of this can be explained by the fact no other study was as rigorous. This 50 year old study was the only one strictly climate controlled. So, despite its age and other issues, what did this study find?
That it wasn’t one variable, such as low pressure, which increased people’s pain, but it was the mixture of low pressure and high humidity.
I still want to point out though, air pressure seems to be more of the consistent factor. However, I think this makes sense and fits in with the reasoning I’ve been going through.
Humidity is a measure of how much water vapor is in the air. Or how wet the air is.
When we sweat, we’re trying to get hot water out of our body and into the air. If there’s not much water vapor already in the air, this works great. The air has room to receive our heat / vapor. If there’s already a lot of water vapor in the air -high humidity- this system starts to falter.
This is why you feel like you’re sweating so much more when it’s humid. It’s not so much that you’re really sweating a ton more, it’s that you’re sitting in your own sweat more. Rather than go in the air, the moisture stays on you.
And this isn’t only a hot weather thing. Evaporation occurs even in cooler temperatures. It’s not as much, and it’s not as visual, but it’s happening.
Bringing our lower pressure scenario back into the mix: In low pressure we have potential to have increased fluid expansion. If we combine this with a scenario in which we have decreased ability to get rid of fluids, high humidity, we have an even better likelihood for something like too much fluid in our joints. That is, some discomfort.
Practical applications for surgical implants, cold weather, arthritis, low pressure, and more
Picking surgical hardware
If it hasn’t been made clear yet, plastic is a sure fire better choice for ACL reconstructions. The lesser chance of lacerating the graft, the fact plastic is more malleable, doesn’t conduct heat like metal (no issues with weather), are big wins for this surgery. If your surgeon plans on using metal, unless he has an extremely persuasive argument, you may have a good sign to go with another surgeon.
My assumption here is most surgeries involving fixating tendon are best with plastic. I believe the reason some surgeons go with metal is because metal is easier to screw than plastic. It drills more easily and is less likely to strip.
I didn’t go into this, but bioabsorbables look to be one of those great on paper, not so great in application ideas. Quite a few problems can arise.
For things like internal bone fixations, metal is the clear winner. The type of metal depends on the strength needed. Titanium is great as it has some more flexibility. It stresses and strains more similarly to bone than does steel. But, it’s not always strong enough.
Giving the hardware the best chance for success
Knowing the healing timelines of your various surgery are a huge help. Using ACL surgery as an example, the fact bone is being drilled through and needs to adapt tells one to go easy on it for 6-8 weeks, as that’s when bone heals.
Furthermore, depending on the graft, sometimes the bone has to heal to a tendon, rather than bone to bone. In the ACL world, it’s customary to add a month on top of the 6-8 weeks to insure the graft is secure. Where again, you’re careful how much you load the bones, along with how much range of motion you put the graft through.
Regardless of the procedure, there’s no point in pushing these types of things. Even if you have a broken bone put back together by steel, the bone itself is not back together. Biology needs time, and by rushing things all you do is increase your odds of complications.
In Bone in Clinical Orthopedics, a study is referenced stating upon inserting a screw, the ability of bone to store energy was reduced by 70%. Now, eight weeks later, the bone remodeled and this was alleviated. 
I referenced the incredible study showing how the tibia can adapt to be the size of the tibia and fibula, if the fibula is removed. In that study though, some of these adaptations were taking upwards of 3.5 years! The study was done on kids where part of this time involved chemotherapy, and we’re talking removing an entire bone, but it was also done on kids who have a faster ability to adapt. Point being sometimes adapting takes a long, long time. Give the body the time it needs.
At the same time, remember, in order to remodel, the bone does need to be strained. The “I’ll just do nothing for a few months” approach is just as bad as the “I’m going to come back faster than anyone else” approach. Strike a balance.
If you’re someone like Dan, where you’re having such intense issues due to hardware, the resolution is clear. Get the hardware removed. Although, even in Dan, this wasn’t so cut and dry. One reason his surgeons were apprehensive about removal was they wanted to give the bone as much time as possible to remodel. Removing the hardware meant a potential increased chance of the bone not staying together.
In other cases, you have to weigh how much the hardware is affecting things against going through another surgery. There are routine surgeries for surgeons. There are no routine surgeries for patients.
I referenced shrapnel at one point. The reason so many soldiers have tens, if not hundreds, of pieces of metal floating around in their body is not that a surgeon can’t remove a great deal of it. It’s the costs of doing that type of surgery don’t outweigh the effects of the shrapnel. If you merely have some discomfort every now and then, it’s probably best to just deal with it.
If you do get hardware removed, you now have to give your body the same level of respect to adapt as you hopefully did when the hardware was inserted. The body went through a bunch to adapt to how things were stressed and strained with hardware in it. It has to do that all over again without the hardware.
I referenced a study where a screw changed the energy storage capacity of bone by 70%, but the bone adapted after a couple of months. When removing this same screw, the bone’s ability to store energy was again reduced by 70%.
Athletes really need to take note here. If you’re getting some hardware removed due to some discomfort, you have to acknowledge you are going to significantly alter your offseason due to needing to give your body two months to adapt. For many, that’s the majority of the offseason.
Metal implants and cold weather
Quick review: The things we’re looking to counteract here are 1) A constriction of the distal aspects of the body 2) The sensitivity of the skin in losing heat to the metal.
What we can do: Get ourselves warmer. Whether it’s extra layers or moving to get more blood flowing, the warmer we feel the less likely our body is going to be constricting the limbs. Thereby hopefully lessening how much the metal is being pressed against. (Again, assuming the metal is touching the skin. Some metal implants are completely encased in bone.) Also, the warmer our brain thinks we are, the less annoyed it will be to losing heat. In fact, you can get yourself to the point where it welcomes it.
Next, perhaps we can put an extra layer on the specific site of the implant. Something like an ACE bandage wrapped around the implant site. This way we give that specific area of skin some extra help in not losing heat.
Low pressure / high humidity and achey joints
Quick review: We’re looking to combat the expansion of the joints due to excess fluid accumulation.
What we can do: Compress the joint / site of achiness. This way we artificially increase the pressure on the joint. This is what a spacesuit does. Here is how I like to wrap the knee:
In terms of how tight to wrap, think of it like a blood pressure cuff. The tighter it is, the more pressure on the area. The more fluid you have or achy you are, the tighter you may want to wrap. Where you can then lessen the tautness after you get some relief.
You can also compress things more globally. Like leggings or tights. It’s common for people to feel achey when they first wake up. So, wearing something like this to bed could work.
Next, we want to get moving quite a bit here, helping to get any excess fluid into circulation and out of the site of discomfort.
This is counterintuitive to some. They may wake up, feel achy, and go “Eh, I’ll take it easy today.” The days where this happens is actually when you want to move more. Moving less will only make matters worse. 
There is also room for some nutritional considerations. When we eat carbohydrates we store more water. If you’re someone who eats a good amount of carbohydrates, there is potential for lowering your carb intake, leading to less water / bloating, which may help.
Bringing us to the final, somewhat obvious recommendation with all this. The better in shape you are, the less overweight you are, the better much of this will be. Being overweight is hard enough on the body already. Being in shape tends to help blood circulation and lessen inflammation. Etc. Etc. All that great stuff that comes with being in shape.
If you found this helpful, please consider a donation-
Thanks to Dan, who is also a med-school student, for the inspiration on this, as well as his thoughts. My all around knowledgable Dad for his thoughts on the bone simulation. Tim, a surgeon, for answering many questions and drawing surgical pictures in the gym for me. My new roommate, whom I had no idea was a mechanical engineer until he saw me walk in the house with a power drill. Warren, a former structural engineer. My brother, who is studying physics / computer science / mathematics. And my girlfriend for filming and listening to me try to explain this in layman’s terms, which was the primary goal.
-The book Bone in Clinical Orthopedics. This was lent to me by an orthopedist. It’s a graduate level text for orthopedic surgeons in training. This isn’t quick reading, but if you have some anatomy background, I think you’ll be good. I made my way through this and Structures: Or Why Things Don’t Fall Down at the same time. Where the “Bone” book falls short on explaining mechanical concepts the “Structure” book really clarifies. For instance, stress and strain was a blip in “Bone,” whereas it was covered continuously all throughout “Structure.”
-A solid, albeit still lacking, article on weather and joint pain, from WebMD:
-That Veritasium video again:
-A shorter video, with some different info, regarding thermal conductivity and our perceptions:
-These discussions on Reddit were helpful regarding metal feeling cold:
-This site, http://www.itis.ethz.ch/itis-for-health/tissue-properties/database/database-summary/ , amazingly has an extensive list of tissues in the human body, and their corresponding densities, heat capacities, thermal conductivities, and more. The fact this exists is incredible.
-A word of caution, when looking at various values and comparing, make sure the units are the same. (www.engineeringtoolbox.com has a lot of the values.) They are often not. I used a couple different unit conversion sites.
 I think about Dan all the time because he is a reminder to me that localized abnormalities CAN cause pain. There has been this surge of pain science, all obsessing over our psychology’s influence on pain. In the pain science world, Dan was a classic case of a guy who is post surgery, having unusual pain, hmm…something has to be going on at his brain, right? Terms such as smudging, catastrophizing, sensitization, all that good stuff. Dan even did mirror therapy at one point, something typically reserved for phantom limb pain. The fact of the matter is the dude has a broken piece of metal floating around in his decaying bone, and that’s why he had pain. His brain was pissed because his leg was pissed.
 Humans have learned the hard way the worst thing to do after any injury is immobilization. You may significantly modify how you move, how much you move, how intensely you move…but you better be moving.
 This distinction between stressing and straining bone has some significant implications. How many people exercise by means of the pool, a reclining bike, or the elliptical? Now think about what’s happening to the bones in these scenarios. Sure, the bones are having to endure some stress, but is it enough stress that the bone strains?
There are actually solid examples of high level cyclists with bone density issues. While it’s obvious in these activities -cycling and such- there is not as much strain as something like walking, more intense weightlifting, etc. it isn’t obvious the level of strain is so low, or nonexistent, that people may lose bone.
The unfortunate irony here is those who are most worried about bone density tend to be those who are most prone to using the pool, bike, or elliptical! I’m going to be succinct on this for now: If you want to improve your ability to be on land, work on your ability to be on land. Don’t work in a buoyed state, a seated state, or a gliding over the ground state. Get your feet on the ground. Your body needs some level of impact.
 I went to Home Depot and bought:
- 20 volt power drill.
- Drill bit kit. (Standard cannulated bits. You don’t need anything stronger than this.)
- You will need something sharp. A regular bit did not get the job done for me.
I also went to a butcher and got some soup bones.
- Drilled a pilot hole with a 2.4mm bit, at a 45 degree angle.
- Moved to a larger, spiked drill bit to get a tunnel.
- I then used a blank drill bit to enlarge the tunnel. (The spike bit wasn’t big enough.)
- Placed the graft into the tunnel.
- Screwed the screw, which should be 1mm smaller than the tunnel, into the tunnel. The screw can be smaller than the tunnel because once you place the graft (rubber band) in, the screw will end up being quite snug. (I had a lot of trouble with this part due to not having the right sized bit to drill the screw in. I ended up rubber hammering the screw in -I was losing daylight- which ended up fine.)
While I had to deviate, and no this isn’t an exact simulation, I followed the procedure for an ACL reconstruction quite closely. I followed guidelines such as these, and watched a good amount of videos, to organize all the above.
I wasn’t sure what was going to come of this. But I can tell you I’m really glad I did it. It really helps you grasp what this, or whatever surgery, entails. An engineering acquaintance remarked I should have tried to simulate this with software to be more precise. While I get the mentality, doing this with your own hands gives you a different level of understanding. Feeling how strong bone is cannot be replaced. This is one reason virtual anatomy and robotic surgery has faded out. It doesn’t reproduce all the senses. I’ve talked to actual surgeons about this. There is an element of feel you don’t get with a robot. Sometimes you don’t recognize how amazing your senses are until you try to do something without one of them.
Last piece of advice: The same engineering acquaintance mentioned to use some oil to clean the bits afterwards, to avoid corroding the bits from the bone remnants and whatnot. Advice I’d adhere to.
- Compressive 170 MPa
- Tensile 112 MPa
- Transverse (shear) 51.6 MPa
Why is bone so weak in the transverse plane? Much like wood, you don’t want to load against the grain. Think of the grain of bone as:
Anything that hits at a 90 degree angle to those grains and the bone can’t resist it well. This is one reason banging your shin on something hurts so damn much.
q = sensible heat stored in the material (J, Btu)
V = volume of substance (m 3 , ft 3 )
ρ = density of substance (kg/m 3 , lb/ft 3 )
m = mass of substance (kg, lb)
cp = specific heat capacity of the substance (J/kg o C, Btu/lb o F)
dt = temperature change ( o C, o F)
Keeping other variables constant, steel has a
-density 1,000 kg/m^3 (rough average from here.)
The point here is merely to show how much steel’s density can make up for the body’s much greater heat capacity (remember, different than storage).
 I do want to point out this was a study done in rabbits. That said, bone is one of the few instances where animal research and human research seem to relate very, very well.
 Fun fact: NASA actually uses exercise as a means of getting astronauts ready for spacewalks. It’s literally part of the protocol before leaving the space vehicle and entering their suits, where the pressure is much lower. The rationale being it increase the speed at which certain substances (nitrogen) are removed from the blood, insuring the astronaut is better and more quickly prepared for a lower pressure environment.
Fun fact two: There is some research out there suggesting women are more likely to give birth after the pressure lowers. See: Spontaneous delivery is related to barometric pressure.
Wearable sensors have evolved from body-worn fitness tracking devices to multifunctional, highly integrated, compact, and versatile sensors, which can be mounted onto the desired locations of our clothes or body to continuously monitor our body signals, and better interact and communicate with our surrounding environment or equipment. Here, we discuss the latest advances in textile-based and skin-like wearable sensors with a focus on three areas, including (i) personalised health monitoring to facilitate recording physiological signals, body motions, and analysis of body fluids, (ii) smart gloves and prosthetics to realise the sensation of touch and pain, and (iii) assistive technologies to enable disabled people to operate the surrounding motorised equipment using their active organs. We also discuss areas for future research in this emerging field.
Know the Symptoms of an Asthma Attack
An asthma attack is the episode in which bands of muscle surrounding the airways are triggered to tighten. This tightening is called bronchospasm. During the attack, the lining of the airways becomes swollen or inflamed and the cells lining the airways produce more and thicker mucus than normal.
All of these factors -- bronchospasm, inflammation, and mucus production -- cause symptoms such as difficulty breathing, wheezing, coughing, shortness of breath, and difficulty performing normal daily activities. Other symptoms of an asthma attack include:
- Severe wheezing when breathing both in and out
- Coughing that won't stop
- Very rapid breathing or pressure
- Tightened neck and chest muscles, called retractions
- Difficulty talking
- Feelings of anxiety or panic
- Pale, sweaty face
- Blue lips or fingernails
The severity of an asthma attack can escalate rapidly, so it's important to treat these asthma symptoms immediately once you recognize them.
Without immediate treatment, such as with your asthma inhaler or bronchodilator, your breathing will become more labored. If you use a peak flow meter at this time, the reading will probably be less than 50%. Many asthma action plans suggest interventions starting at 80% of normal.
As your lungs continue to tighten, you will be unable to use the peak flow meter at all. Gradually, your lungs will tighten so there is not enough air movement to produce wheezing. You need to be transported to a hospital immediately. Unfortunately, some people interpret the disappearance of wheezing as a sign of improvement and fail to get prompt emergency care.
If you do not receive adequate asthma treatment, you may eventually be unable to speak and will develop a bluish coloring around your lips. This color change, known as cyanosis, means you have less and less oxygen in your blood. Without aggressive treatment for this asthma emergency, you may lose consciousness and eventually die.
If you are experiencing an asthma attack, follow the "Red Zone" or emergency instructions in your asthma action plan immediately. These symptoms occur in life-threatening asthma attacks. You need medical attention right away.
For more detail, see WebMD’s article Asthma Attack Symptoms.
Health Solutions From Our Sponsors
Ackerman, J.P., T. Riggins, and M.M. Black. "A Review of the Effects of Prenatal Cocaine Exposure Among School-Aged Children." Pediatrics 125.3 Mar. 2010: 554-565.
American Psychiatric Association. Diagnostic and Statistical Manual of Mental Disorders, Fifth Edition. Arlington, Virginia: American Psychiatric Association, 2013.
American Psychiatric Association. Diagnostic and Statistical Manual of Mental Disorders, Fourth Edition, Treatment Revision. Washington, D.C.: American Psychiatric Association, 2000.
American Psychiatric Association. Practice Guideline and Resources for Treatment of Patients with Substance Use Disorders, Second Edition. Arlington, Virginia: American Psychiatric Association, 2006.
Barbosa de Carvalho, H., and S.D. Seibel. "Crack Cocaine Use and Its Relationship With Violence and HIV." Clinics (Sao Paulo) 64.9 Sept. 2009: 857-866.
Bhuvaneswar, C.G., G. Chang, L.A. Epstein, and T.A. Stern. "Cocaine and Opioid Use During Pregnancy: Prevalence and Management." Primary Care Companion for the Journal of Clinical Psychiatry 10.1 (2008): 59-65.
Brodie, J.D., B.G. Case, E. Figueroa, et al. "Randomized, Double-Blind, Placebo-Controlled Trial of Vigabatrin for the Treatment of Cocaine Dependence in Mexican Parolees." American Journal of Psychiatry 166 (2009): 1269-1277.
Chermack, S.T., R.L. Murray, M.A. Walton, B.A. Booth, J. Wryobeck, and F.C. Blow. "Partner Aggression Among Men and Women in Substance Use Disorder Treatment: Correlates of Psychological and Physical Aggression and Injury." Drug and Alcohol Dependence 98.1-2 Nov. 2008: 35-44.
Committee on Drugs, American Academy of Pediatrics. "Neonatal Drug Withdrawal." Pediatrics 101.6 June 1998: 1079-1088.
Compton, W.M., Y.F. Thomas, F.S. Stinson, and B.F. Grant. "Prevalence, Correlates, Disability and Comorbidity of DSM-IV Drug Abuse and Dependence in the United States." Archives of General Psychiatry 64.5 (2007): 566-576.
Drug Enforcement Administration (DEA). DEA History Book, 1876-1990. Washington, D.C.: U.S. Department of Justice, 1991.
Etheridge, R.M., J.C. Smith, J.L. Rounds-Bryant, and R.L. Hubbard. "Drug Abuse Treatment and Comprehensive Services for Adolescents." Journal of Adolescent Research 16 (2001): 563-589.
Gates, S., L.A. Smith, and D.R. Foxcroft. "Auricular acupuncture for cocaine dependence." Cochrane Database Systematic Review 2006.
Guerrero, E., and C.M. Andrews. "Cultural competence in outpatient substance abuse treatment: Measurement and relationship to wait time and retention." Drug and Alcohol Dependence 119 (1-2) Dec. 2011: 13-22.
Heard, K., R. Palmer, and N.R. Zahniser. "Mechanisms of acute cocaine toxicity." Open Pharmacology Journal 2008.
Hsue, P.Y., C.L. Salinas, A.F. Bolder, et al. "Acute Aortic Dissection Related to Crack Cocaine." Circulation 105 (2002): 1592.
Johnson, B.A., N. Ait-Daoud, X.Q. Wang, et al. "Topiramate for the treatment of cocaine addiction: a randomized clinical trial." Journal of the American Medical Association Psychiatry 70.12 Dec. 2013: 1338-1346.
Kumar, S., A. Kumari, and S. Muraka. "Lifestyle Factors in Deteriorating Male Reproductive Health." Indian Journal of Experimental Biology 47.8 Aug. 2009: 615-624.
Lam, W.K., J.D. Cance, A.N. Eke, et al. "Children of African-American Mothers Who Use Crack Cocaine: Parenting Influences on Youth Substance Use." Journal of Pediatric Psychology 32.8 (2007): 877-887.
Margolin, A., H.D. Kleber, S.K. Avants, et al. "Acupuncture for the treatment of cocaine addiction: a randomized controlled trial." Journal of the American Medical Association 287.1 (2002): 55.
Martin, P., B.A. Weinberg, and B.K. Bealer. Healing Addiction: An Integrated Pharmacopsychosocial Approach to Treatment. Hoboken, New Jersey: Wiley-Interscience National Institute on Drug Abuse, January 2007.
Moeller, F.G., et al. "Citalopram combined with behavioral therapy reduces cocaine use: a double-blind, placebo-controlled trial." American Journal of Drug and Alcohol Abuse 33.3 (2007): 367.
Morton, W.A. "Cocaine and Psychiatric Symptoms." Journal of Clinical Psychiatry, Primary Care Companion 1.4 Aug. 1999: 109-113.
O'Brien, M.S., and J.C. Anthony. "Risk of Becoming Cocaine Dependent: Epidemiological Estimates for the United States, 2000-2001." Neuropsychopharmacology 30.5 May 2005: 1006-1018.
Office of National Drug Control Policy. Apr. 6, 2005.
Richardson, G.A., L. Goldschmidt, and C. Larkby. "Effects of Prenatal Cocaine Exposure on Growth: A Longitudinal Analysis." Pediatrics 120.4 Oct. 2007: e1017-e1027.
Singer, L.T., L.J. Eisengart, S. Minnes, et al. "Prenatal Cocaine Exposure and Infant Cognition." Infant Behavioral Development 28.4 Dec. 2005: 431-444.
United States. National Institute on Drug Abuse. "Cocaine." July 2018. <https://www.drugabuse.gov>.
United States. National Institute on Drug Abuse. Preventing Drug Abuse among Children and Adolescents: A Research-Based Guide for Parents, Educators, and Community Leaders, Second Edition. Bethesda, Maryland: National Institutes of Health, 2003.
Top Cocaine and Crack Abuse Related Articles
What Causes Abdominal Pain?
High Blood Pressure (Hypertension)
High blood pressure (hypertension) is a disease in which pressure within the arteries of the body is elevated. About 75 million people in the US have hypertension (1 in 3 adults), and only half of them are able to manage it. Many people do not know that they have high blood pressure because it often has no has no warning signs or symptoms.
Systolic and diastolic are the two readings in which blood pressure is measured. The American College of Cardiology released new guidelines for high blood pressure in 2017. The guidelines now state that blood normal blood pressure is 120/80 mmHg. If either one of those numbers is higher, you have high blood pressure.
The American Academy of Cardiology defines high blood pressure slightly differently. The AAC considers 130/80 mm Hg. or greater (either number) stage 1 hypertension. Stage 2 hypertension is considered 140/90 mm Hg. or greater.
If you have high blood pressure you are at risk of developing life threatening diseases like stroke and heart attack.
Sensing weather conditions through bodily reactions (e.g. dry hands, arthritic pains) - Biology
первый в мире пиратский ресурс, который открыл публичный и массовый доступ к десяткам миллионов научных статей
Если бы не было Sci-Hub – не смог бы вообще написать диссертацию. Направление – материаловедение. Исследования, связанные со структурообразованием в алюминиевых сплавах.
Мы ведем борьбу с информационным неравенством во всем мире. Научные знания должны стать доступны для всех людей независимо от их материального положения, социального статуса, страны проживания и других факторов.
Миссия проекта – устранение абсолютно всех барьеров, препятствующих максимально широкому распространению знаний в современном обществе!
Мы выступаем за немедленную отмену интеллектуальной собственности и копирайта для научно-образовательной информации.
Законы о копирайте делают юридически нелегальной работу электронных библиотек и закрывают доступ к знаниям большинству людей, в то же время позволяя отдельным индивидам извлекать из этой ситуации огромные прибыли, создавая и поддерживая не только информационное, но и экономическое неравенство.
Проект Sci-Hub поддерживает движение Открытого доступа в науке. Научные статьи должны публиковаться в открытом – то есть бесплатном для чтения – доступе.
Открытый доступ – новая и прогрессивная модель научной коммуникации, за которой будущее. Мы выступаем против заработка, полученного путем ограничения доступа к информации.
Sensing weather conditions through bodily reactions (e.g. dry hands, arthritic pains) - Biology
Food Allergy, Intolerance and Sensitivity
- A Food Allergy is a severe, immediate and acute immune response to eating a particular food type, resulting from an IgE mediated reaction. It is sometimes referred to as an IgE-mediated Food Allergy or Hypersensitivity.
- Food Intolerance is a broad term to describe a variety of slower acting and chronic symptoms to eating a particular food type. The responses can include metabolic, pharamcological, toxicological and non-IgE mediated immune reactions.
- Swelling of soft tissues of face and tongue
- Breathlessness, wheezing, difficulty breathing or swallowing
- Itching of mouth, throat, eyes and skin
- Sore throat
- Rhinorrhea (sudden onset of runny nose), sneezing, sinusitis (nasal congestion)
- Anaphylactic Shock
- Tree nut
- Wheat (or other Gluten-containing grains)
- House Dustmite
- Cat, Dog or Horse Epithelium
- Pollen (e.g. stinging nettle, hazel, birch, grass, mugwort etc.)
- Fungi (e.g. Aspergillus fumigatus, Alternaria alternata, Cladosporium Herbarum)
- Metabolic food reactions - on account of genetic or acquired errors in the metabolism of nutrients. Consumption of these foods can result in inadequate digestion or absorption of these food types, resulting in excessive bacterial fermentation and 'rotting' of the foods in the digestive tract. Examples include Lactose Intolerance and Fructose Intolerance. Lactose Intolerance is relatively common.
- Non-IgE-mediated Immune system reactions to food and also certain chemical compounds found in foods. These include the reaction of the Immunoglobulins/Antibodies IgA and IgG, as well as White Blood Cells, to food. These immune modulated reactions to food are much slower acting than IgE (which is regarded as a 'true allergy'). This is perhaps one of the most common types of Food Intolerance.
- Pharmacological reactions may involve physiological responses to certain chemical compounds contained in the foods (not immune system mediated). Symptoms may include headaches, dizziness, fatigue etc. Excessive consumption of certain food types regularly, depending on what they are, may well result in too high an intake of certain types of constituent chemical compounds. Only a few examples are examined below.
- Excessive tyramine intake in cheese or wine
- Excessive salicylate intake when many salicylate-rich foods are eaten in combination., particularly those who are particularly sensitive to high salicylate levels. Salicylates are a natural plant immune hormone and preservative. A Salicylate Food Guide and general information web site is available here. They are particularly rich in dried fruits, jam, honey, coconut oil, black pepper and much more. They are also created synthetically and can be found in certain medicines, perfumes and preservatives.
- Food additives, e.g. preservatives, natural or artificial colours, flavourings etc. This category constitutes a large category and may include preservatives such as Sodium Metabisulphite, Nitrites etc. or thickeners and flavourings such as free glutamate. Artifical sweetners such as Aspartame also cause problems. Other problematic chemicals include Caffeine, Benzoates and Tartrazine.
- Excessive Histamine intake from foods that are naturally rich in histamine, certain fermented foods (released by yeast), those that encourage the release of histamine or those that develop a build-up of histamine in their flesh as they age (e.g. certain fish when not stored properly - Tuna, Mackerel, Bluefish, Mahi-Mahi and Herring). A list of histamine rich foods can be viewed here and here.
Food intolerance is harder to identify on account of its slower acting nature and often cause downstream problems, localised gastointestinal inflammation and a drain on one's energy reserves if not regulated and treated properly.
Below are some useful information web sites on food allergies and intolerances.
In a general sense, a Food Allergy can be classed as an immediate immune system response, specifically the Immunoglubin IgE, to consuming a certain food protein, even in tiny amounts. A Food Allergy response can occur within seconds or minutes of consuming the item. It can even occur as the food touches the lips or tongue, before the food has actually entered the oesophagus.
IgE is one of the body's primary immune defences against real or perceived threats or 'invaders'. In this instance, the food proteins in question are confused with the very similar viral DNA proteins. The immune system detects these food types as antigens or allergens, and the immune system produces large amounts of IgE antibodies, which attach themselves to specialised white blood cells, which secrete histamine (the chief inflammatory agent) and cytotoxic and inflammatory chemicals.
Whilst this predisposition toward misinterpretation may sometimes be of genetic origin or of infant immunity adaptation, there are many other factors involved in the immune system developing this characteristic. In 2008, The Food Allergy & Anaphylaxis Network estimated that 4% of the US population suffered from food allergies.
In extreme cases, it can be life threatening (i.e. anaphylactic shock), the severity of the body's IgE immune response being sufficient to hypotension (blood pressure drop), loss of consciousness and possibly death. In such cases, an Adrenaline (Epinephrine) is used by Ambulance or Accident and Emergency staff as an injection to control the allergic reaction. However, in the vast majority of cases, a mild version of one or more of the other symptoms is experienced immediately after coming into contact with the food, the allergic reaction just subsides with time.
Another term for Food Allergy is Rapid-Onset Food Allergy. Whilst the term Food Allergy is used to describe IgE-mediated immune system response to a certain food type, it could imply to some that this is the only type of adverse immune response possible to certain non-contaminated food types. There are slower acting, chronic responses to eating certain food types that can develop anywhere from 30 minutes to 48 hours after eating, involving other types of immune system response, but these are generally referred to as Food Intolerance
The other 10% of food allergies (the less common ones) involves the proteins of certain food sources. One example is a rice allergy. This tends to be more common in East and South East Asia where rice forms a large piet of the staple diet of the average person. Celery allergies tend to be more common in Central European populations.
There may be some cross-sensitivity with foods, for example, those allergic to crustaceans or oysters may tend to also be allergic to squid.
Food allergies can operate through airborne matter from problem foods, and through the skin (touching the food type with your hands or lips), and not just through the actual ingestion of the foods. This may affect workers in food processing industries who may suffer from skin disease, asthma, rhinitis and conjunctivitis.
In general the more concentrated the protein fraction of the food is, the more noticeable the allergic reaction and symptoms will be. For example, consuming reasonable quantities of wheat bran or rice bran will likely produce more of an allergic reaction in individuals who suffer from these allergies than their usual flour or wholegrain counterpart, as the protein concentration is higher. However, there is not always a logical pattern to follow. To a large extent, it may depend on the brand or source of the food substance, and also its possible level of contamination with other grains. A similar pattern may be noticed with supplements, some working well with the body, others doing nothing and others still provoking a mild immune system-type response - for the same active ingredient (differing in quality, preparation and other additives etc.)
For example, I myself experience an immediate allergic reaction upon eating a porridge made with NOW Foods Rice Bran (immediate onset of a sore throat which lasts several hours). I can feel the 'sour' nature of the protein in my mouth and feel an instant IgE reaction with the porridge in my mouth. There is no swelling of any kind, just a continual sore throat. However, I do not experience any such reaction when taking a protein supplement rich in Rice Protein and Rice Bran, Thorne Research's MediClear. MediClear was also kinesiologically tested on me and found at that point in time to be what the body wanted. It is unlikely that a food stuff that caused a Food Allergy response would test positively using this method. I have tried a few brands of wholegrain rice and rice milk, which are less concentrated sources of rice protein/gluten, and does not experience any noticeable allergy symptoms with these.
Another example is Coconut. I have found that I had a similar reaction to dessicated Coconut, with a sore throat coming on within minutes. However, I do not observe these symptoms with Coconut oil, which contains no protein (possibly contain some faint traces of Coconut protein).
Similarly, I experience a similar sour sensation when tasting porridge made from The Oatmeal of Alford (Kiln Fried, Stone Ground) and immediate onset of a sore throat upon eating that lasts for several hours, similar to the above (i.e. an IgE-mediated food allergy response). However, I experience significantly reduced symptoms with porridge made from other brands of oats (e.g. Organic Quaker Oats, E.Flahavan & Sons Porridge Oats, Jordan Organic Oats) or even with a more concentrated Oat protein/gluten source such as Mornflake Oatbran. Gluten-Free Oats (or in other words, Oats free of any Wheat, Barley or Rye contamination - but still containing the glutens naturally found in Oats) still produced an allergic reaction.
Similarly, those who suffer from a milk allergy will likely experience less of a reaction from goat's milk than cow's milk, as the protein fraction is lower.
There may be possible minor food intolerance issues associated with these foods I have cited as examples, but that is a different story (which could be down to general digestive inefficiency and/or IgG type reactions). Of course, the fact that I am experiencing a sore throat with the aforementioned proteins in certain forms is a general indicator to avoid those forms, and perhaps also related forms that may still be causing immune system responses but that which are not noticeable, but still not really desirable from a physiological perspective.
Those with severe IgE-mediated allergies should consider wearing a Medic Alert bracelet, pendant or tag with details of their allergies, and perhaps blood type and any other relevant information.
Hazelnut is a food type that is sometimes identified in IgG blood testing as being a food that one reacts to. However, some commentators argue that this is a reaction, but not an allergic one (despite the test result). The Hazelnut protein is irritating to the tongue and it titillates the palate in small doses. This is why Hazelnuts are often used by Chocolatiers as opposed to other nuts. I have always wondered why Hazelnuts were used as they were never his favourite nut particularly.
One could however interpret this behaviour of hazelnuts as being reflecive of Oral Allergy Syndrome, that is a cluster of allergies (including IgE) in the mouth (typically burning sensation or itching of lips, mouth and/or pharynx) to eating certain fruits, nuts and vegetables, typically noted in hayfever sufferers who have cross-reaction with compounds in these foods that appears similar to birch pollen. These foods can include: apples, hazelnuts, peaches, cherries, almonds, pears, carrots, and celery. The symptoms are arguably somewhat different to those the majority of people who eat hazelnuts without itchy lips etc. It is more of a mild (physical) irritation to the tongue as opposed to an immune system-mediated response that affects more parts of the head and throat.
Food Intolerance, or non-IgE mediated Food Hypersensitivity, is a term used to describe a number of different possible, chronic, slow acting symptoms and processes that result from the consumption of a certain food type, a reaction occurring anything between 30 minutes or up to 48 hours after the food is consumed. The amount of a food substance required to trigger this response may vary, but is usually much larger than that required to trigger a food allergy response as described above.
- Reactions to naturally occuring toxins in foods that can be broken down by most individuals but not successfully by susceptible individuals. Examples include lectins found in cereals, beans and vegetables of the nightshade family (e.g. potatoes). Lectins are highly resistant, carbohydrate-binding proteins. In susceptible individuals, they bind to the villi inside the GI tract and damage the gut lining. Once in the bloodstream, they can bind to cell membranes, arteries and veins, organs and glands, and can result in autoimmune disorders or degenerative diseases. Lectins also break down to form polyamines which can lower NK cell counts directly in the bloodstream and indirectly in the GI tract by altering the flora balance.
- Reactions to contaminated foods. These include bacterial food poisoning from contaminated or degraded food, i.e. from the toxins produced by these bacteria that subsequently contaminate the food, even after the bacteria themselves are killed by cooking, e.g. staphylotoxins from staphylococcus species bacteria other sources of toxins may include various toxins released from teflon frying pans or pots when heated excessively or other forms of excessive chemical contamination. These however in the context of Food Intolerances are those contaminated foods that affect predisposed individuals much more than healthy individuals with no predisposition. Chemical sensitivities, mainly lymphocyte mediated, may occur in certain individuals, but these are generally categorised as Chemical Sensitivities rather than Food Allergies, and are often triggered by viral episodes or toxicity build up (c/f the Nitric Oxide pathway.
- Irritable Bowel Syndrome (IBS) Symptoms - Abdominal pain, stomach distension (bloating), excessive wind, and bowel dysfunction (alternating between constipation and loose stools). IBS may well be a consequence of Food Intolerance.
- Itchy Skin or Eczema
- Sinusitis - Nasal congestion
- Joint pain
- Irritable bowel syndrome (IBS)
- Inflammatory bowel disease (IBD), such as Crohn's Disease and Ulcerative Colitis
- Other auto-immune disorders
- Chronic constipation
- Chronic hepatitis C infection
- NSAID (Non-steroidal anti-inflammatory drugs) intolerance
- Respiratory complaints, e.g. including asthma, rhinitis (runny nose) and headache
- Functional dyspepsia (indigestion)
- eosinophilic esophagitis (inflammation of esophagus)
- ENT (ear, nose and throat) illnesses
- IgE-mediated (classic food allergy)
- IgE and/or non-IgE-mediated, including Eosinophilic (white blood cell) reactions
- Non-IgE -mediated, e.g. IgA, IgG and IgM reactions
Symptoms of Food Intolerance include the following.
Fatigue in the context of CFS means more than one's usual level of fatigue, hours or days after consuming certain foods. Other individuals may sense the fatigue or general malaise a few hours after eating it or so.
If one is eating the foods in question every day or every other day, then it one may not notice the dips so much as one may well be in a constant low ebb - abstaining from the offending foods may result in a decrease in one's day to day level of fatigue.
Symptoms may vary in severity between individuals and be dependent on the volumes of the foods in question, and the concentrations of the ingredients that cause intolerance contained in them. Symptoms may persist for up to 3 days or so (in some cases up to 2 weeks) after cutting out all foods that are the main causes of intolerance (if this is possible - see below). Many of the symptoms may go unnoticed by the patient, or if they are noticed, may simply be accepted as part of one's physiological make-up and not attributed to being caused by one's diet.
Because of the slow nature of the reaction to the food, it is clearly more difficult to determine the precise offending food that is causing this response, if indeed one believes that a food source may be the problem, which may not be immediately obvious to a doctor or a patient. IgE-mediated Food allergies are generally much easier to identify on account of their rapid onset, immediately after consuming the particular food type.
The reaction to the consumption of these foods tends to arrive between 3 hours after first consuming the food and up to 3 days afterwards. According to Allergy UK, up to 45% of the UK population is affected by food intolerance.
Other terms for Food Intolerance, or Non-IgE-Mediated Food Hypersensitivity, include Non-Allergic Food Hypersensitivity, Pseudo-Allergic Reactions, Slow-Onset Food Allergies. Clearly some of these terms are slightly misleading as some imply that slow acting immune responses are not 'true allergies' and other terms for Food Intolerance imply that all the types of Food Intolerance are 'allergies' or immune system related, which is not true either. Food Intolerance is a little like CFS, it is useful for describing symptoms, but not very useful when it comes to correctly describing the causes or mechanisms of those symptoms.
Food Intolerance is still not taken very seriously by medical professions in the UK:
'In the UK, scepticism about food intolerance as a specific condition influenced doctors' (GPs') perceptions of patients and of the patients' underlying problems. However, rather than risk damaging the doctor-patient relationship, when GPs chose, despite their scepticism, and tempered by an element of awareness of the limitations of modern medicine, to negotiate mutually acceptable ground with patients and with patients' beliefs. That as a result, whether due to a placebo effect, secondary benefit, or as a biophysical result of excluding a food from the diet, the GPs acknowledged benefit, both personal and therapeutic.'
Non-IgE Mediated Immune System Response to Food
The term Food Allergy is used to denote fast acting, IgE-mediated immune system reactions to food only, rather than embracing the entirety of different adverse immune system responses to food, the fast acting and more acute, and the slower acting and more chronic. All Non-IgE Mediated Immune System Responses to Food, being slower acting, are classed as being Food Intolerances, a term which includes other types of slow reaction included a lack of necessary enzymes and toxicological responses etc.
Of course, IgE and non-IgE immune responses can occur within the same patient to the same food type, but at slightly different times, i.e. the IgE symptoms being noticed immediately upon ingestion and the non-IgE symptoms being noticed slightly later.
Some of the latter two groups are hereditary (genetic) in nature, others are merely conditioned or acquired.
Non-IgE-mediated Immune System Responses to certain Food Types could be classed as Non-IgE-mediated 'Food Allergies'. Some commentators use the term 'Delayed-Onset Food Allergies' to describe Food Intolerance as a whole, although this is misleading as it associates non-immune system modulated Food Intolerance reactions (e.g. inadequate enzyme production) with Non-IgE-Mediated Immune System Responses to Food. Some may complain about the use of the term 'Allergy' as it should primarly refer to IgE reactions, as per Wikipedia's definition of Allergy below.
However, there is a certain amount of leniency in defining what is an 'Allergy', as per the 3 groups of Allergy referenced above. I therefore stick to the term 'Non-IgE Mediated Immune System Response to Food' which is what we are actually talking about here - where there can be no room for confusion. Secondary Immune System Response to Food could also be another possible term, although perhaps less formal and precise than the above.
It is primarly the non-IgE mediated immune responses that we shall examine in this section, specifically IgA and IgG. The severity of the different immunological reactions to food differ between foods, and between individuals, as well as how they combine with other Food Intolerance and other factors.
Non-IgE Mediated Immune System Responses do not occur in isolation to other types of Food Intolerance and can occur concurrently with Metabolic, Pharmacological and Toxin-Mediated Reactions to Food. Their combined action may provide the broad spectrum of symptoms that we experience as Food Intolerance. And indeed, they can also exacerbate a downward spiral of General Digestive Enzyme and Stomach Acid Deficiencies and indeed the other types of Food Intolerance.
The foods that cause Non-IgE Mediated Immune System Responses in susceptible individuals tend to from the same food groups as those that provoke IgE mediated food allergies (Classic or True Food Allergies) as listed above. The reactions are based on the misrecognition of certain types of protein as viral DNA proteins, the same as Classic Food Allergies.
'Food antigens contact the immune system throughout the intestinal tract via the gut associated lymphoid system (GALT), where interactions between antigen presenting cells and T cells direct the type of immune response mounted. Unresponsiveness of the immune system to dietary antigens is termed "oral tolerance" and is believed to involve the deletion or switching off of reactive antigen-specific T cells and the production of regulatory T cells (T reg) that quell inflammatory responses to benign antigens.'
Immunoglobulin G (IgG) is a monomeric immunoglobulin. Each IgG has two antigen binding sites. It is the most abundant immunoglobulin and is equally distributed in tissues liquids and blood, constituting 75% of serum immunogloblulins in humans. IgG molecules are synthesised and secreted by plasma B cells. IgG forms part of the body's secondary immune system, the primary being mediated mainly by IgM.
Typically IgG-mediated reactions are much more common than IgE mediated reactions, but are much less well researched and understood. Most occurrences are very mild and go undetected or relatively symptomless (which is a matter of perception in many individuals with a less than perfect diet and lifestyle). Many may choose to ignore the presence of some of the milder IgG reactions, and pay attention and make dietary changes accordingly when they are found to have more severe IgG reactions to certain food types. However, milder IgG reactions may be indicative of other types of immunological reactions to these foods or other foods, and indeed may over time drain one's energy reserves and put a strain on the immune system and body in general. Most commonly, IgG antibodies/immunoglobulins are detected in the blood, through an IgG blood test. IgG-mediated immune reactions to food tend to occur in some of the food types that we consume most regularly, but as a species are not perhaps best physiologically adapted to (e.g. most commonly grains and milk). IgG antibodies are found in those individuls who do not have (significant) food intolerances (who do not notice any symptoms).
Of course the foods that create these Non-IgE-Mediated Immunological Food Intolerance reactions do so in their protein form, which is the non-digested or semi-digested form, in the digestive tract, and what is absorbed into the bloodstream is (hopefully) only amino acids (assuming that Leaky Gut Syndrome (LGS) is not present. LGS can be caused by a number of possible factors, including excessive Candida albicans growth, which can further fuel Non-IgE Mediated Immunological Responses to Food. In addition, LGS is one potential downstream consequence of too much immune system regulated inflammation in the digestive tract, caused by excessive Eosinophil hyperactivity and inflammatory cytokines being released by them. This is one feature of severe cases of Celiac Disease (Gliadin Protein Intolerance). LGS is examined in more detail on the Digestive Disorders page.
Therefore one would assume that the majority of IgG antibodies would be present in the digestive tract rather than in the blood, although in more severe cases, the levels may well rise higher in the blood. Some commentators have criticised IgG blood tests as they often come back negative when the actual picture in the body as a whole, and also the digestive tract, tells a different story. Nevertheless, IgG blood tests can still be a useful tool in diagnosing Non-IgE-Mediated Immunological Food Intolerances.
YorkTest states that Food Intolerance can be detected by measuring IgG antibodies in th blood, in their Foodscan 113 Food Intolerance Test report, which is a test for IgG antibody reaction to 113 food types. It is presented as a Food Intolerance Test, but it is really just tested one aspect of Food Intolerance - which is still useful, but it is more of an introductory type test into Food Intolerance. YorkTest also state that Food Sensitivity can also arise from mechanisms that do not involve the immune system, such as enzyme deficiencies (e.g. lactose intolerance) or chemical sensitivies such as reaction sto food additives (e.g. tartrazine (E102) and sunset yellow (E110). YorkTest use the terms Food Intolerance and Food Sensitivity interchangeably, the latter being arguably a more ambiguous term.
Immunoglobulin A (IgA) is an antibody that plays a critical role in the immunity of mucosal membranes. IgA in the mucosal linings are larger in number than all other types of antibodies combined. Between 3g and 5g is secreted into the intestinal lumen every day. There are two subclasses of IgA, IgA1 and IgA2, and can exist in a dimeric form, known as secretory IgA (sIgA). The secretory part protects the immunoglobulin from being degraded by proteolytic enzymes, e.g. in the digestive tract, so it can survive in the intestines and protect against harmful microbes. http://en.wikipedia.org/wiki/IgA
IgA antibodies/immunoglobulins are produced mainly in the digestive tract. They are the digestive tract's main immunological defense. They are secreted by the intestinal walls into the intestinal lumen (the hollow centre of the intestines) and mix in with the Chyme and Stool, which passes through the GI tract, slowly being digested, before being expelled from the body via the anus. IgA antibodies cannot be readily reabsorbed from the digestive tract. The purpose of these antibodies is to combine with any detected protein threats, interpreted to be of viral origin, in order to neutralise them and prevent them being absorbed from the GI tract into the bloodstream. This may well result in some of the IBS type symptoms as unabsorbed proteins are fermented by bacteria in the colon. Antibodies operate in a kind of lock and key manner, matching the exact type of protein they are created to bind with.
The immune cells of the digestive tract comprise the largest body of immune cells in the body. The GI tract has an enormous surface area and is arguably one of the main possible mode of entry into the body by foreign pathogens, perhaps even more so than the lungs. The GI tract comprises probably the majority of the body's immune system, in relative terms. Without IgA antibodies being released into the digestive tract, one would be highly susceptible to gastro-intestinal viruses and other forms of infection, e.g. bacterial, fungal etc. Certain individuals in tests have been shown to produce very few IgA antibodies, which is of course an immune system deficiency.
However in Food Intolerance patients, the level of IgA antibodies tends to be elevated, that is only the IgA antibodies that correspond to certain food types. It is thought that measuring IgA antibodies in the stool is a useful measure of Immunologically-Mediated Food Intolerance, and can show us what IgA antibodies are present in too high a concentration in the stool, thus indicating this type of Food Intolerance response before signs and symptoms are evident in the blood with overactivity and overproduction of other antibody types (to the particular food types).
Whilst anti-Gliadin antibodies are found in the blood samples of approximately 12% of the general US public, the studies of Kenneth Fine, M.D., of Enterolab, have shown that perhaps up to 30% of a group of 'otherwise normal people' from the US and Overseas have detectable levels of these antibodies in their stool samples. This figure rises to as high as 50% in patients suffering adverse symptoms or from high risk populations (those with higher incidences of Gliadin sensitivities). This would seem to confirm the above hypothesis regarding IgA levels in the stool vs the blood, and backing up the idea that the stool is the most sensible place to look for IgA antibodies.
If one has an non-IgE-mediated immune system sensitivity or response to certain food types, e.g. Gliadin or Dairy, and one eliminates these food sources from one's diet, i.e. one goes on a Gluten-free or Milk-free diet (and does not consume any hidden sources of Gliadin), then the production of the IgA antibodies corresponding to these food types does not go down immediately to lower levels. Of course, without these particular food sources in the GI tract, they have nothing to attack (often besides the digestive tract itself), but the body still produces them as it is 'expecting' them. Research shows that these antibodies continue to be produced in the digestive tract (and possibly elsewhere) for up to 1-2 years after a person has ceased consuming the corresponding food items. The levels of the corresponding antibodies in the blood tend to drop off more rapidly, in 3-6 months typically. Controlled reintroduction may be one method of adjusting to these proteins without the production of these corresponding antibodies, as may low dose immunotherapy. However, if one starts to eat these food sources in copious quantities in a non-systematic and uncontrolled manner, then the levels of the antibodies are likely to increase to their former levels very rapidly. It may vary according to the individual of course, and a 'Gluten challenge' may not necessarily guarantee immediate increase in relevant antibody levels for detection if Gluten is reintroduced heavily for 1-2 weeks.
Enterolab have stated in an email correspondence with me that the body generates IgA antibodies if one is intolerant or sensitive to a particular food (food intolerance and sensitivity being used interchangeably here also) but that the body will generate either IgE or IgG antibodies/immunoglobulins if one is allergic to a particular food, depending on the food and severity of the response. Arguably it is probably both for a Classic Food Allergy. Whether one chooses to classify IgG-Mediated Immune System Response then as an Allergy, a Group 3 Allergy or Food Intolerance is perhaps a matter of classification. However, Enterolab stress the difference in causation between IgA and IgE reactions.
Coeliac or Celiac Disease
Celiac Disease, a.k.a. Celiac Sprue or Coeliac Disease, is classified as an autoimmune disorder, and is essentially an adverse immune system response to Gluten (i.e. Gliadin/Gluten Intolerance). It can affect genetically predisposed individuals of all ages, from middle infancy onwards. Celiac Disease is the result of a combination of the action of Anti-Gliadin Antibodies (AGAs) against the presence of ingested Gliadin , but more importantly the production of Anti-Tissue Transglutaminase Antibodies (anti-tTG antibodies). Whilst non-Celiac sufferers can have AGAs, i.e. Gliadin/Gluten Intolerance, they do not have measurable levels of anti-tTG antibodies, which are a genetic-based response in Celiac sufferers to the ingestion of Gliadin. Celiac Disease is therefore a specific type of Gliadin(Gluten)-intolerance.
Approximately 0.5-1% of the population of the USA suffer from Celiac Disease. There are a number of genes that are involved in controlling the excessive immune response to Gliadin (Gluten), that may lend an individual predisposed or more likely to develop such a condition, and according to the studies of Kenneth Fine, M.D., of Enterolab, is found in approximately 60% of Americans. There may be other, currently undefined genes, that control whether such a toxic reaction occurs and if and to what extent damage will occur to the intestines and other tissues or not. Research suggests that as many as 30% of Americans may be Gluten sensitive, with 1 in 225 having the sensivity as severe to cause the intestinal damage associated with Celiac Disease. Please seee the Genetic Testing section below for more discussion of the Celiac genes present in the US population.
Transglutaminase is family of enzymes that catalyse the formation of a covalent bond between a free amine group (e.g. from lysine groups found in a protein or peptide) and the gamma-carboamid group (e.g. from glutamine groups found in another protein or peptide). The bonds formed by transglutaminase are highly resistant to proteolytic degradation. Tranglutaminase enzymes are generally found in the intestines and also in the tissues. It is referred to as 'meat glue' in the food processing industry. They play an important part in blood clotting.
One subclass of Transglutaminase is known as Tissue-Transglutaminasen (TG2 or tTG). It is classed as an 'auto-antigen'. It's natural affinity to binding with Gliadin, and the resulting protein crosslinking stimulates the immune B-cell responses that eventually result in the production of the problematic overproduction of the ATA IgA and IgG antibodies (examined below).
Whilst associated with Celiac Disease, high levels of Tissue Transglutaminase enzymes are found in sufferers of Huntingdon's and Parkinson's Disease. A study by Griffin M, Casadio R, Bergamini CM. 'Transglutaminases: nature's biological glues'. Biochem J 2002368:377-96 suggests that tTG plays an important role in inflammation, degenerative diseases and tumor biology.
In Celiac Disease, antiendomysial antibodies (EMAs) are produced. These mainly consist of Anti-Transglutaminse Antibodies (ATAs) against the enzyme Transglutaminase and Tissue-Transglutaminase. ATAs are types of IgA and IgG antibodies, and their relative proportions in Celiac Disease sufferers depends on the phenotypes involved. Please note that these EMAs are different to Anti-Gliadin Antibodies (AGAs), consisting of IgA and IgG antibodies, that attack Gliadin directly. IgA antibodies can be found in the stool and also the blood to a lesser extent, and the presence of anti-tTG antibodies in high numbers can predict the onset of Celiac Disease. anti-tTG antibody production can also be stimulated by the presence of the Rotavirus protein VP7. A Rotavirus is a genus of double-stranded RNA virus from the Retroviridae family and is known to cause diahrrea.
'For tTG autoimmunity (CD), T-cells are generated against wheat gliadin and similar gluten proteins of the trib Triticeae. The T-cells are defined by the ability to react to HLA-DQ8 and DQ2.5 restricted antigens and gliadin is one of the antigens. Gliadin is a favored dietary substrate for transglutaminase because of many enzyme reaction sites on gliadin. In disease, transglutaminase reacts with gliadin forming a linkage. In forming this bond transglutaminase becomes linked to T-cell epitopes on gliadin. B-cells with surface IgM that react to transglutaminase can present it with bound gliadin peptides to T-cells which stimulate B-cell maturation and proliferation to plasma cells making IgA or IgM.'
According to Dr Kenneth Fine of Enterolab, 'the main perpetrator of the immune response to gluten is not antibody but T lymphocytes (T cells) producing tissue-damaging chemicals called cytokines and chemokines. How much antibody is produced at the stimulus of T cells differs in different people. Furthermore, some people simply do not or cannot make alot of intestinal IgA antibody even though gluten may be stimulating a severe T cell-mediated immune response. Unlike antibody levels, the numeric value of malabsorption test results are an indicator of severity of intestinal damage.'
Enterolab stated in an email correspondence to me that cytokines and chemokines can cause damage to the intestinal villi. This is observed in IgA deficient individuals. In addition, cytokines and chemokines can circulate anywhere in the body to cause oxidative damage elsewhere, which is why systematic and multisystem symptoms (of inflammation) are observed in gluten sensitivity (whether AGA and/or ATA derived).
'The release of IL15 [Interleukin 15 - a cytokine] is a major factor in coeliac disease as IL15 has been found to attract intraepithelial lymphocytes (IEL) that characterize Marsh grade 1 and 2 coeliac disease. Lymphocytes attracted by IL-15 are composed of markers enriched on natural killer cells versus normal helper T-cells. One hypothesis is that IL-15 induces the highly inflammatory Th1 response that activates T-helper cells (DQ2 restricted gliadin specific) that then orchestrate the destructive response, but the reason why inflammatory cells develop prior to gliadin specific helper cells is not known. The IRP response differs from typical responses that stimulate IL15 release, such as viral infection. In addition, other cytokines such as IL12 and IL2, which are typically associated with T-helper cell stimulation, are not involved. In these two ways the innate peptide activation of T-cells in celiac disease is strange. IL-15 appears to induce increases in MICA and NKG2D that may increase brush-border cell killing.'
- Anti-Tissue Transglutaminase (anti-tTG)
Antibodies to epidermal transglutaminase (a.k.a. eGT or Keratinocyte transglutaminase) are the antibodies believed to cause Dermatitis Herpetiformis (Duhring's Disease), the chronic blistering skin condition, characterised by extremely itchy blisters filled with a watery fluid, found in some Celiac Disease sufferers. It is a less common type of eczema, and not to be confused with eczema that can result from other causes, e.g. dry skin for prolonged periods, stress, allergic response to animal danders, ingestion of too many spices etc.
ATAs are found most frequently in certain autoimmune diseases, e.g. juvenile diabetes, and in almost all cases of Celiac Disease. The above estimate of 0.5% to 1% of the US population being Celiac Disease sufferers is based upon the statistic of 1% of the population having pathogenic levels of ATA. ATAs are
The antibodies implicated in Celiac Disease, i.e. IgA and IgG, are discussed at the link below.
There may be no detectable symptoms of the IgA ATA immune response to Gliadin, with symptoms typically becoming noticeable when the immune reaction over time has begun to damage the intestines, with resulting Food Intolerance type symptoms. These symptoms derive from the resulting malabsorption or improper digestion of dietary nutrients (i.e. metabolic food intolerance - discussed below), and can include abdominal pain or bloating, diarrhea, constipation, wind or nauseous feeling (with or without vomiting). Fine postulates that acid reflux and heartburn may also be a possible symptom. Other symptoms could include fatigue, joint pains, mouth ulcers, bone pain, abnormal menses and even temporary infertility. It is the downstream effects of the IgA ATA immune response to Gliadin and the damage it causes to the intestinal villi and the resulting symptoms that is generally referred to as Celiac Disease.
Kenneth Fine has suggested that the intestinal damage caused by Celiac Disease (or otherwise elevated Anti-tTG antibodies) is responsible for a significant increased risk of cancer of lymphoma of the small intestine. Indeed, he believes there is a strong correlation between autoimmune disease development and the continued consumption of Gliadin in Gluten sensitive individuals.
Fine also suggests that 'Non-celiac gluten sensitivity syndromes are no less severe than ones accompanied by villous atrophy, in terms of symptoms they may cause, accompanying autoimmune diseases in other parts of the body, and resultant disability.'
In an email correspondence to me, Enterolab have stated that Dr Fine has found that anti-casein antibodies can actually cause some of the same damage and symptoms (of villous atrophy) as anti-Gliadin antibodies (AGAs), which are often more harmful than the effects of the anti-tTG antibodies produced in reaction to the fusion of tTG and Gliadin.
Enterolab also stated that Dr Fine uses the the 'Gluten-Sensitive' to describe those that produce IgA antibodies in reaction to Gluten, i.e. Anti-Gliadin Antibodies (AGAs). Some of the people who produce AGAs also produce anti-tTG antibodies. As mentioned above, the damage to the intestinal villi does come immediately, but lags behind anti-tTG antibody production and may not be detectable (using conventional methods) until the damage has been done. Clearly one does not need to have intestinal damage present in order to be considered 'Gluten-Sensitive', but the more damage that is present, the more likely one is to be diagnosed with Celiac Disease and classified as a Celiac. By this logic, some Celiac patients or those who exhibit the same symptoms may not necessarily be producing significant anti-tTG antibodies, but much of the damage may be caused by Anti-Casein Antibodies and anti-Gliadin antibodies etc. (i.e. Milk and Gliadin/Gluten Sensitivity).
In the UK, the National Institute for Health and Clinical Excellence (NICE), whilst immersed in controversy over some of its arguably inappropriate recommendions for CFS treatment, does actually recommend the screening for Celiac Disease in patients with newly diagnosed CFS (Clinical Guideline 53) and IBS (Clinical Guideline 61).
Bloating is a result of the gas production caused by bacteria consuming undigested food sources, mainly carbohydrates, which puts pressure on the intestinal wall or insufficient stomach acid or enzymes causing food to remain longer than it should in the stomach.
The regular consumption of foods that cannot be fully digested may in turn encourage the growth of dysbiotic or pathogenic bacteria, and harmful yeasts such as Candida albicans, which can in turn cause further problems. Please see the Bacterial page for more information.
The different types of Metabolic Food Intolerances are examined below.
Lactose is the main type of sugar found in milk, constituting 2-8% by weight. It is also found to a lesser extent other milk products. Fermented forms of milk, including natural bio-live yoghurt and kefir have a somewhat reduced lactose content as the probiotic bacteria have consumed part of the lactose to multiply. Protein-rich, hard cheeses contain virtually no lactose.
Lactose is a disaccharide, consisting of galactose and glucose fragments. Infant mammals, including humans, are nursed on their mother's milk which is rich in the carbohydrate lactose. Their intestinal villi secrete the enzyme Lactase (a.k.a. Beta-D-galactosidase) in order to digest it, which cleaves the lactose into two units, the simple sugars glucose and galactose. Lactose must be broken down into smaller units prior to absorption into the blood stream and cannot be directly absorbed in the form of Lactose.
Because lactose is chiefly found in a mother's milk, most mammals experience a natural decrease in Lactase after weaning age.
Approximately 75% of adults worldwide show some decrease in Lactase activity during adulthood. Lactase activity decrease varies according to population, from as little as 5% in Northern Europe, up to 71% in Southern Europe, and up to 90%+ in some parts of Africa and Asia. Lactose Intolerance usually therefore tends to occur in affected individuals after the age of two.
- Northern & Western Europeans - 15% affected
- Asian, African, native American and Mediterranean populations - 70-90% affected.
- Soy sauce
- Fermented soy bean and rice paste (e.g. miso)
- Malted foods or drinks
- Powdered cheese
- Hydrolysed vegetable protein (HVP)
- Hydrolysed plant protein (HPP)
- Texturised protein
- Autolysed plant protein
- Protein extract
- Torula Yeast (a.k.a. Vitex)
- Senomyx additives
- Casein Hydrolysate
- Hydrolysed whey protein isolate
- Hydrolysed soy protein isolate
- Yeast extract (e.g. marmite or vegimite)
- Odourless Wind - carbon dioxide produced by the bacterial fermentation of carbohydrates (sugars)
- Pungent Wind - the result of the bacterial fermentation of nitrogen compounds found in proteins and amino acids and also the bacterial fermentation of sulphur containing compounds, usually found in sulphur-rich foods (which are useful for aiding detoxification but consuming more than can be digested and absorbed will result in this kind of Hydrogen Sulphide (H2S) smelling wind).
- Damp, Moist or Greasy Wind - the result of an excess of undigested fats or oils, known as fecal fats or lipids, in the stool. In normal circumstances, there should be very little fat or lipid content in the stool.
- Hot Wind - from the consumption of excess or supplemental dietary fibre
- Maize (Zea mays L. ssp. may, a.k.a. Corn) gluten - contains Zein (a Prolamin) and Glutelin-2 (a Glutelin).
- Oat (Avena sativa) gluten - contains Avenin (a Prolamin) and Oat Glutelin. Avenin is a minor protein of Oats. Approximately 80% of the storage protein of oats is Avenalin, a Globulin, which is atypical for grains. Oats contain more soluble fibre than any other grain.
- Rice (Oryza sativa) gluten - contains Rice Prolamin and Rice Glutelin, but not the same as Gliadin or Glutenin. Many manufacturers' rice packets often consisted of enriched rice, which is rice coated with a vitamin rich outer layer, usually Corn/Maize starch, but may possibly contain some wheat starch.
- Potato flour (farina)
- Millet flour
- Arrowroot flour
- Maize Flour
- Rice Flour
- Gram (Chickpea) Flour
- Buckwheat Flour
- Sago flour
- Tapoica flour
- Digestive Enzyme supplements (e.g. Tyler Similase, Renew Life DigestMore Ultra, Vital Nutrients Pancreatin and Ox Bile Extract etc.) - these will help where the stomach and pancreas do not produce sufficient quantities of a particular class of enzyme, e.g. proteases etc. Digestive Enzyme supplements nearly always contain Lactase, which will also help with the digestion of Lactose in those who are Lactose intolerant and anyone else with slightly lower levels of enzymes in general, if they choose to eat/drink dairy products.
- Betaine HCl is a stomach acid supplement and can help with the digestion of proteins in the stomach (e.g. Vital Nutrients Betaine HCl).
- Probiotic Bacteria - a long term programme of probiotic supplementation and correction of dysbiotic problems associated with deficient numbers of specific probiotic bacteria, excessive commensal bacteria and/or the presence of pathogenic bacteria, fungus, yeast or parasites to restore the correct Flora balance to the small and large intestine, to aid digestion, help suppress future commensal or pathogenic overgrowth as well as help stimulate T Helper 3 cells which regulate the intestinal immune system response to perceived 'threats' - which when not working correctly would invariably include various food types, even previously innocuous ones. Probiotic supplementation may be undertaken in conjunction with an Anti-Candida Diet, live fermented foods (assuming nutritional yeast (Saccharomyces cerevisiae) overgrowth is not an issue) as well as antimicrobial herbs to reduce the numbers of commensal and pathogenic anaerobic organisms. Please see the Bacterial page for more information.
- Increasing one's Fibre intake (subject to sensible precautions and assuming the digestive tract is able to tolerate fibre (i.e. no incidence of Crohn's Disease which is itself an inflammatory, autoimmune disease often caused by food intolerance.) This will help to remove Mucoid plaque which can clog up the intestinal walls and increase the likelihood of general, broad spectrum food intolerance and IBS symptoms. Please see the Mucoid Plaque page for more information.
- Herbs to promote efficient peristalsis, but not too many as to cause loose stools.
- Mineral and vitamin supplements to improve Methylation and to correct any nutrient deficiencies the body might have, e.g. Magnesium, P5P, B12 etc. Please see the Nutritional Deficiencies page for more information.
- damage to brain tissue, as it presses against the skull or as one part of the brain pushes into another
- pressure on blood vessels, reducing their ability to supply the brain cells with oxygen and essential nutrients
- a loss of consciousness
- convulsions or seizures
- repeated vomiting
- slurred speech
- weakness or numbness in the arms, legs, hands, or feet
- loss of coordination
- dilated pupils
- inability to wake up from sleep
- severe headache
- weakness and numbness in hands, feet, arms or legs
- changes in mood
- memory problems
- inability to remember what happened before or after the incident (tiredness) and lethargy
- getting lost easily
- persistent headaches
- persistent pain in the neck
- slowness in thinking, speaking, reading or acting
- moodiness, for example, suddenly feeling sad or angry for no apparent reason
- sleep pattern changes, such as sleeping more or less than usual, or having trouble sleeping
- light headedness, dizziness
- becoming more easily distracted
- increased sensitivity to light or sounds
- loss of sense of smell or taste
- nausea , or ringing in the ears
- changes in sleeping patterns
- irritability and crying
- loss of balance
- loss of newly acquired skills, such as toilet training
- changes in playing behavior changes
- refusal to eat
- loss of interest in favorite activities or toys
- unsteady walking
- Sedation: This can help prevent agitation and excess muscle activity and contribute to pain relief. Examples include profanol.
- Pain relief: Opioids may be used.
- Diuretics: These increase urine output and reduce the amount of fluid in tissue. These are administered intravenously. Mannitol is the most commonly used diuretic for TBI patients.
- Anti-seizure medication: A person who has experienced moderate to severe TBI may have seizures for up to a week after the incident. Medication may help prevent further brain damage that may result from a seizure.
- Coma-inducing medications: During a coma, a person needs less oxygen. Sometimes, a coma may be deliberately induced coma if the blood vessels are unable to supply adequate amounts of food and oxygen to the brain.
- Removing a hematoma: Internal bleeding can cause partly or fully clotted blood to pool in some part of the brain, worsening the pressure on the brain tissue. Emergency surgery can remove a hematoma from between the skull and the brain, reducing pressure inside the skull and preventing further brain damage.
- Repairing a skull fracture: Any part of the skull that is fractured and pressing into the brain will need to be surgically repaired. Skull fractures that are not pressing into the brain normally heal on their own. The main concern with a skull fracture is that forces strong enough to cause it may have caused further, underlying damage.
- Creating an opening in the skull: This can relieve the pressure inside the skull if other interventions have not worked.
- Avoid activities that could cause another blow or jolt to the head.
- Follow the instructions of healthcare professionals.
- Do not take drugs that the physician has not approved.
- Do not return to normal activities, including driving and sports participation, until the doctor agrees.
- Get plenty of rest.
- Falls: Responsible for 47 percent of reported cases, notably in children aged up to 14 years and adults aged over 65 years
- Motor vehicle accidents: These accounted for 14 percent of cases, especially in the 15 to 19-year age group.
- Being struck by or colliding with an object: 15 percent of TBIs resulted from a collision with either a moving or stationery object.
- focus, reason, and process information
- communicate verbally and nonverbally
- judge situations
- remember things in the short term
- solve problems
- organize their thoughts and ideas
- tinnitus, or ringing in the ears
- difficulty recognizing objects
- clumsiness, due to poor hand-eye coordination
- double vision and blind spots
- sensing bad smells or a bitter taste
- your mouth ulcer has lasted three weeks
- you keep getting mouth ulcers
- your mouth ulcer becomes more painful or red – this could be a sign of a bacterial infection, which may need treatment with antibiotics
- not taking your medication as directed
- damage to the thyroid gland, such as a punch to the throat
- a very rapid heartbeat (over 140 beats a minute)
- fever (a temperature higher than 38C/100.4F) , with diarrhoea and vomiting
- jaundice – a yellow tinge to your skin and eyes
- severe agitation and confusion
- hallucinations – seeing or hearing things that are not real – being unable to tell the difference between reality and your imagination
- chest pain
- muscle weakness
Humans are of course the only animal to consume milk after weaning age, and in particular the milk of other animals, namely the milk of the domesticated cow (Bos primigenius). And indeed the only animal to expose other animal's milk to high temperatures before consumption (pasturisation), which may modify the protein structure. If milk was so vital to an adult's diet, grown men would continue to breast feed from their mothers into their old age, presumably?
The most common of the type of Metabolic Food Intolerance is Lactose Intolerance, i.e. a 'deficiency' in the Lactase enzyme. Calling it a deficiency in this context is not quite correct and is looking at the glass half empty rather than half full. Having low levels of the lactose enzyme as an adult mammal or indeed human is normal and 'natural', whereas having the capability to produce an increased number of Lactase enzymes in the GI tract is a form of adaptation. This may be for genetic reasons because of the population group one derives from geographically (phenotype adaptation) and/or for historical reasons (depending on one's exposure to the said carbohydrate type during one's early childhood).
If the intestinal tract does not produce enough Lactase in response to the amount of Lactose consumed (i.e. being 'Lactose Intolerant' or simply consuming too much milk and dairy), then the remaining Lactose will work its way down the intestinal tract and be consumed/fermented/rotted by bacteria, that switch to lactose metabolism, producing hydrogen, carbon dioxide and methane. This fuelling of the dysbiotic and pathogenic micro-organisms in the colon can result in their multiplication, especially if consumed regularly. This creates a variety of unpleasant symptoms, including IBS.
Lactose Intolerance affects approximately 10% of the population of Northern Europe, cow's milk is staple food source for virtually all children and regular food source for most adults in this region.
Lactose intolerance may be caused or worsened also by Celiac Disease, which shortens the intestinal villi that are responsible for producing Lactase.
Fructose Malaborption and Fructose Intolerance
Fructose is a monosaccharide sugar, also known as a fruit sugar. Fructose is either found in the Fructose form or bound to Glucose as Sucrose (a.k.a. sugar), as a disaccharide, in various food types. Fructose is found in fruit, honey, corn syrup, HFCS, maple syrup and to a lesser extent in vegetables. The highest Fructose containing fruits, with the exception of dried fruits that are more concentrated forms of fruit, include mango, papaya and apple. Please see the chart below for Fructose levels in fruits.
Fructose Malabsorption is caused by a deficiency in the two carrier proteins. GLUT2 and GLUT5, that transport Fructose out of the Small Intestine and into the blood stream.
If one consumes an excess amount of Frucose (or Sucrose) or has a deficiency in the production of the carrier proteins for Fructose, then some Fructose will remain in the digestive tract, and similarly to Lactose Intolerance, will be fermented by bacteria. Excess fructose in the colon may also cause diarrhea if in sufficient quantity, on account of the water that is attracted and/or retained in the digestive tract by osmosis. Fructose Malabsorption (as opposed to excessive Fructose consumption) results in the exclusion of Fructose from anabolic and metabolic activities.
Acetate, Propionate and Butyrate - types of Short-Chain Fatty Acids - are produced in the colon by the bacterial fermentation of dietary fibre, which helps to keep down the stool pH to suppress dysbiotic and pathogenic microogranism overgrowth. However, greatly elevated levels of these SCFAs is an indicator of Fructose Malabsorption. Unabsorbed fructose osmotically reduces the absorption of water and is metabolised by the normal colonic bacteria to SCFAs and the gases Hydrogen, Carbon Dioxide and Methane. These SCFAs and gases are absorbed into the bloodstream, and thus elevated SCFA levels can be observed in the blood plasma.
Fructose-6-Phosphate (F6P) is produced from Fructose, and is utilised in the Glycolysis pathway, to produce Pyruvate from Glucose. Excessive Fructose intake leads to high F6P levels in the cells. If the Fructose availability far exceeds the Glucose supply, then metabolic issues arise as the control mechanisms that apply to Glucose are essentially bypassed or lifted. Excessive fructose intake tends to inhibit Glycolysis and Gluconeogensis, albeit in a slightly different manner to Hereditary Fructose Intolerance (HFI), discussed below.
Symptoms of Fructose Malabsorption include bloating, diarrhoea or constipation, flatulence, stomach pain (on account of muscle spasms) and other symptoms.
Fructose is metabolised differently from other types of sugar. Glucose is the main sugar used by the brain and muscles in respiration, and its uptake is dependent on the insulin hormone. Whilst all cells can metabolise Fructose to some degree, in balance with the mechanisms that control the balance between Glucose and Fructose levels, it is the liver and kidneys that produce most of their energy from the metabolism of Fructose (through enzymatic phosphorylation by ATP), and thus Fructose is responsible for much of the (liver) heat production in the body. The liver utilises fructose extremely rapidly and bypasses the phosphofructokinase regulatory step of glycolysis, and breaks Fructose down into Fructose-1-Phosphate, and converts it onwards to Glucose. Muscle usage of fructose relies on it being broken down into Fructose-6-Phosphate and being converted in Glucose.
Some studies suggest that as many as 1 in 3 people may suffer from sugar sensitivity, most commonly to Fructose. As well as the different lines of causation in Fructose Malabsorption and Intolerance described below, the immune system may additionally be implicated. Antibodies may form against one or more of the enzymes, substrates or products implicated in Fructose metabolism, further impairing Fructose metabolism and the adverse reaction to Fructose consumption. Strictly speaking, this is non-IgE-mediated immunological response to Fructose further worsening a metabolic Fructose Intolerance problem.
Whilst limiting Fructose intake is a general strategy for both Fructose Malabsorption and Fructose Intolerance, it is not to say that the body cannot absorb or metabolise ANY Fructose, but just that those pathways are impaired. Thus, a small amount of fruit or vegetable sources Fructose can and should be consumed, but no more. It may be impossible to completely eliminate Fructose and in addition those foods that do contain a small amount may well be good sources of other important nutrients and enzymes.
There are 3 main types of hereditary metabolic hepatic disorders concerning Fructose catabolism and metabolism, known as types of Fructose Intolerance. These are essentially problems of metabolising Fructose once it has been absorbed from the digestive tract and into the bloodstream.
The first is Hepatic Fructokinase Deficiency which prevents Fructose being used at all, thus affecting both the Fructose metabolic pathways Glycolysis and Gluconeogensis. The second disorder, Hepatic Fructokinase Deficiency, affects a further processed form of Fructose and affects both pathways. The third form, Fructose-1,6-Bisphosphatase Deficiency, affects only the Gluconeogensis pathway. The two pathways Glycolysis and Gluconeogenesis are described below.
'Glycolysis is the metabolic pathway that converts glucose, C6H12O6, into pyruvate, C3H3O3-. The free energy released in this process is used to form the high energy compounds, ATP (adenosine triphosphate) and NADH (reduced nicotinamide adenine dinucleotide).'
'Gluconeogenesis (GNG) is a metabolic pathway that results in the generation of glucose from non-carbohydrate carbon substrates such as lactate, glycerol, and glucogenic amino acids.'
Inhibition of gluconeogenesis can result in hypoglycaemia after about 12 hours once the glycogen stores have been depleted. This results in lactic acidosis as the cells underogo anaerobic respiration in the absence of glucose. Lactic acid build up is commonly associated with msucle ache after vigorous or high resistance exercises and overexertion and contributes to metabolic acidosis. The liver may try to compensate by producing glucose from the Short Chain Fatty Acids (SCFAs) Acetate, Propionate and Butyrate that are produced by the anaerobic bacterial fermentation of dietary fibre such as pectin and various vegetable fibres, and absorbed into the bloodstream from the colon. Some SCFAs are transported to the liver for storage. Rapid depletion of SCFAs in blood plasma is associated with HFI (discussed below). Glucose may still be released through the breakdown of glycogen in the glycogen stores until that is depleted, resulting in severe hypoglycemia.
Fructose intolerance symptoms depend on the nature of the exact condition but may include dizziness, fatigue, headaches and weakness.
Hepatic Fructokinase Deficiency
The Hepatic Fructokinase is responsible for the first step in the liver processing of Fructose, phosphorylating D-Fructose with ATP into ATP and D-Fructose-1-Phosphate.
http://en.wikipedia.org/wiki/Hepatic_fructokinase Hepatic fructokinase deficiency, a.k.a. Essential Fructosuria, is a condition whereby a deficiency in or worse still an absence of the Hepatic Fructokinase enzyme inhibits/prevents the conversion of Fructose into Fructose-1-Phosphate (F1P).
This can result in elevated levels of Fructose in the liver and kidneys, and excessive Fructose levels being excreted in the urine (as it cannot be utilised). A normal level of excretion of Fructose in the urine of a health person is typically 1-2% of that consumed or less, whereas in an individual with Hepatic Fructokinase Deficiency it can be as high as 10-20%. In the latter case, the remaining percentage of Fructose retained is most probably metabolised by adipose tissue via an alternative pathway of some description. This however poses no toxic consequence to the liver or kidney and sufferers do not usually present with any symptoms.
There is a second rare type of potential problem associated with Fructose. This is known as Hereditary Fructose Intolerance (HFI), a.k.a. Fructose Poisoning or Hereditary Fructosemia. This has nothing to do with problems absorbing Fructose from the digestive tract into the bloodsream, but is a genetic disorder of the liver. HFI is a hereditary condition caused by a deficiency of liver enzymes that metabolise fructose, specifically the metabolism of Fructose-1-Phosphate.
The liver enzyme in question is Aldolase-B which converts Fructose-1-Phosphate (F1P) to Dihydroxyacetone Phosphate (DHAP) and Glyceraldehyde. A defiency in this enzyme means that Fructose cannot be metabolised beyond Fructose-1-Phosphate (F1P). This results in the build up of F1P in the liver and kidneys, as well as a deficiency in Glucose. Unlike with Hepatic Fructokinase Deficiency, HFI (i.e. excessive F1P) has toxicological damage to the liver and kidneys.
Excessive levels of F1P prevents phosphates being utilised, in other words, it ties up all the available phosphate (from ATP) in the F1P sugar. F1P is enzymatically created out of Fructose and the high energy phosphate bond from ATP. ATP cannot be made and is continually used up. The metabolic consequence of this is a rise in Uric acid levels. The lack of phosphate and ATP also interferes with a number of other biosynthetic pathways that require ATP, synthesis of protein, RNA and DNA, cyclic AMP formation and also ammonia detoxification. High F1P levels also inhibits the phosphorylation of the enzymes Glycogen Phosphorylase (essential for provision of Glucose-1-Phosphate from Glycogen by Glycolysis) and also inhibits the Fructose-1,6-Bisphosphatase enzyme (essential for Gluconeogensis - see below). Without the ability to produce Glucose from Fructose, the liver will not function efficiently, and may impact energy levels generally.
Symptoms may include Hypoglycaemia and its associated adrenergic (adrenaline/noadrenaline related) symptoms such as sweating, palpitations, shakiness, anxiety glucagonic symptoms (related to hormone for carbohydrate metabolism) such as hunger, nausea, vomiting and abdominal pain and neuroglycopenic symptoms (shortage of glucose in the brain) including impaired judgement, ataxia (lack of coordination of muscle movements), fatigue, breathing difficulties and impaired speech. Other symptoms are those associated with the absence of Gluconeogenesis, described above, such as Lactic acid build up and muscle ache.
Those with CFS may experience some of these symptoms from time to time, usually after overdoing things for a prolonged period of time or going without a meal for too long, and recovery to one's 'normal' baseline of fatigue usually occurs within a few hours of eating, resting and/or sleeping. This does not necessarily mean they have HPI but it is more indicative of mitochondrial failure in general rather than a specific fructose metabolism problem.
HFI, if poorly managed, can result in a very acute condition. For this reason it is usually identified early in life. However, metabolic mishandling of Fructose in HFI sufferers can occur at any level of severity, from the very mild to the very severe, so some milder cases may go undiagnosed. Sufferers are recommended to completely avoid Fructose, Sucrose and Sorbitol. HFI may be a significant contibutary factor to fatigue and low ATP levels in a subsegment of CFS patients. Patients who suffer from kidney problems such as kidney stones or gout should consider being tested for HFI and related Fructose metabolism disorders.
HFI is normally identified by examining the blood Short Chain Fatty Acid levels. Another potential marker of HFI is a high level of Adenosine in the blood (which may also be a result of taking additional Methionine or SAMe amino acid supplements).
Dr Sarah Myhill recommends consumption of Probiotics in order to increase the amount of probiotic bacterial fermentation that occurs in the colon, in order to produce more SCFAs, in order to stave off Hypoglycaemia. Propionibacterium freudenreichii, in particular, produces Proprionic acid, as discussed on the Bacterial page. One could also try eating more soluble fibre, the food for probiotic Butyrate production. Another option would be to take a Calcium Magnesium Butyrate supplement, as referenced on the Liver Function page.
Fructose-1,6-BisPhosphatase (a.k.a. Fructose-Bisphosphatase or F-1,6-BP) is a Hepatic enzyme that converts Fructose-1,6-BisPhosphate into Fructose-6-Phosphate in Gluconeogenesis (the creation of Glucose from smaller substrates). Fructose Bisphosphatase performs the opposite role to Phosphofructokinase. Each enzyme is unidirectional, as one would expect.
Fructose BisPhosphatase Deficiency is a disorder whereby not enough Fructose-1,6-BisPhosphatase is available for Gluconeogensis to occur correctly (Fructose and Glycerol cannot be used as fuels). It is therefore a severe disorder of Gluconeogenesis and prevents the regeneration of Glucose. This may be of genetic origin or as a result of HFI described above (the suppressive effective of excessive F1P on the Fructose-1,6-BisPhosphatase enzyme.
The substrate Fructose-1,6-BisPhosphate builds up and levels of Fructose-6-Phosphate are very low. However, Glycolysis (the breakdown of Glucose) can still function.
The increased levels of glucagon result in the release of fatty acids from the fat cells (adipose tissue), which when combined with glucerol that cannot be utilised by the liver, result in the build up of triglycerides in the liver, resulting in a fatty liver. Excessive ketone bodies are also produced from the fatty acids, and can result in Ketosis.
The production of Pyruvate and Lactate result in a pH drop of the blood (metabolic acidosis).
Those who suffer from Fructose-1,6-Bisphosphate Deficiency should avoid fasting for long periods and eating high carbohydrate foods (especially those containing high levels of Fructose or Glucose), as this involves the need for Gluconeogenesis to create Glucose.
Sugar Alcohol Intolerance
[This section is somewhat one sided and will be updated shortly. Xylitol is also pre-biotic and useful in preventing and treating bacterial infections, and is somewhat controversial on account of some poor quality sources and excessive dosing]
A number of Sugar-free, sugar alcohol-based sweetners (sugar substitutes) are available on the market. These include Sorbitol, Mannitol and Xylitol. The reason these are low calorie sweetners is that they are very poorly digested and absorbed in the digestive tract, and are thus relatively 'inert' despite being sweet to the taste. They are thus used in a variety of products, including sweets and some medicines, particularly sublingual and chewable supplements, which often contain both Sorbitol and Mannitol, and sometimes all 3 (as well as Stevia)! Always read the label on sublingual and chewable supplements.
Unfortunately, as these sugar-alcohol sweeteners are poorly digested and absorbed, they pass through the digestive tract, and are digested to some degree by the bacteria in the colon, resulting in excess wind. These alcohol sugars are also laxative in their action, as dissolved particles in the chyme and stools attract water from the intestinal walls and bloodstream, and excessive consumption may also result in diarrhea. In general, alcohol sugars are to be avoided and a much better choice (for occasional use) is the plant-based Stevia, which does not produce these symptoms.
Diabetes (mellitus) as you probably already know is a condition whereby the body does not produce enough insulin (Type I Diabetes), or where the cells do not utilise unsulin properly (Type II Diabetes). Gestational Diabetes is a temporary condition that affects some pregnant mothers who have high blood glucose levels. Insulin is of course the pancreatic hormone that enables cells to absorb glucose in order to undergo respiration and produce energy. Thus the excessive or mistimed consumption of sucrose for a diabetic may result in hyperglycemia (too high blood sugar) and excessive water loss (in an attempt to dump glucose), dehydration and electrolyte loss. This is a form of maladaptation to sugar intake or foods very high in sugar.
A number of nutrition and herbal based methods have been successfully employed by a number of Diabetes Type I and II sufferers to overcome their Diabetes. Diabetes is often caused in the first place by excessive consumption of foods and drinks containing refined sugar.
Type I Diabetes is genetically similar to Celiac Disease in 7 unusual genetic regions according to the latest research in a study of 20,000 volunteers. Both early-onset diabetes and Celiac disease are caused by improper immune system adaptation. Celiac Disease affects approximately 1% of the UK population as opposed to Diabetes which affects 0.5%.
Phenylketonuria is a genetic disorder characterised by a deficiency in the hepatic enzyme Phenylalanine Hydroxylase (PAH). This enzyme metabolises the amino acid Phenylalanine to the amino acid Tyrosine. When PAH is deficient, Phenylalanine accumulates in the digestive tract and some is converted into the metabolites Phenylacetate, Phenylpyruvate and Phenethylamine. This may result in a deficiency of Tyrosine in the body as well as bacterial catabolism of Phenylalanine in the digestive tract.
- Amino Acids as Food Additives:
We have examined above how certain amino acids can be problematic for the body in high concentrations, i.e. Homocysteine on the Nutritional page. We shall examine two others. The first is Glutamic acid or Glutamate (as Mono-Sodium Glutamate - MSG). The other is Aspartyl-Phenylalanine-1-Methyl Ester, a.k.a. Aspartame or Nutrisweet.
Monosodium glutamate, a.k.a. sodium glutamate and MSG, is the sodium salt of the non-essential amino acid Glutamic acid. It is used as a food additive and flavor enhancer, on account of its 'umami' taste. It was first patented in 1909 in Japan. It is a free glutamate, a white crystalline powder, which when dissolved in water or saliva, rapidly dissociates/ionises into Sodium cations and Glutamate anions. Until the 1960s it was prepared by the hydrolysis of wheat gluten, after which time it was prepared by the fermentation of carbohydrates such as starch, sugar beets, sugar cane or molasses. MSG has the HS code 29224220 and the E number E621.
The E number E620 to E640 are the category of food additives known as flavour enhancers. Numbers E620 to E625 comprise glutamic acid and glutamate salts.
Umami is one of the five basic tastes detected by receptor cells on the human tongue, which is triggered by the presence of glutamic acid or glutamates. Umami is Japanese for savoury. It is a natural trigger that the brain uses to encourage consumption of protein rich foods such as meats and cheeses, part of our 'cave man' genetic programming to ensure survival. However, in a modern society with abundant foods, it can lead one towards excessive consumption of glutamic acid/glutamate, exaccerbated by food manufacturers excessive use of glutamate rich ingredients to try to make their foods more appealing and 'tasty' and 'tangy' or 'beefy', and to sell more units.
MSG was once associated primarily with Chinese restaurants, but is currently used by many fast food chains and in many processed food products, often to cover up the use of cheap ingredients and cost cutting in quality, and to appeal to the 'baser taste instincts'.
It is frequently found in stock cubes, barbecue sauces, salad dressing, snack foods such as crisps/chips and seasoning mixtures.
For example, Walkers BBQ Rib Crisps contain 'flavour enhancer (monosodium glutamate)'.
Besides using MSG as a food additive, a number of food sources are already naturally high in glutamate or glutamic acid.
Glutamic acid, as discussed above, is of course an abundant amino acid found in all living cells, of plant or animal origin, primarily in the bound form as part of proteins. Amino acids in general are not found freely in food sources, but as the building blocks of larger protein molecules.
Meat, fish eggs, milk and cheese tend to be high in protein glutamate. Food sources rich in protein glutamate in some cases also have high levels of free glutamate, e.g. Parmesan cheese, corn, peas etc. If you look at the amino acid breakdown of various protein sources, both animal and plant, you will find that Glutamic acid or Glutamate is found is higher concentrations than any other amino acid. This is the way proteins are. This is nothing to be alarmed about!
Protein glutamate does not produce the 'umami' taste as the receptors on the tongue do not detect glutamate ions, or so many of them, as they are bound up in protein molecule structures.
Protein glutamate is of course still absorbed by the body, but the individual protein molecules first have to be broken down to release the glutamic acid or glutamate ions. This takes time and of course not all the protein may be broken down in the digestive tract.
Protein glutamate can of course become Free Glutamate if the protein in question is fermented or hydrolysed (boiled in acid). Please see below for details.
Only a small fraction of the glutamate in foods is in the 'free' form, i.e. individual glutamate anions. It is only free glutamate anions produce the 'umami' sensation. Proteins made up of glutamate are technically speaking not actual glutamate, in the same way that a book is not a piece of paper.
Whilst protein glutamate is slower to break and and absorb, free glutamate is readily absorbed in the GI tract and can quickly elevate blood plasma glutamate levels.
Whilst certain forms of extremely aged soy beans or their processed derivatives may be higher in free glutamate, there are certain health benefits from fermented soy products. Fermented soy tends inhibit the effects of phytic acid (IP6 - an 'anti-nutrient which prevents mineral absorption), increases the availability of isoflavones and also contains probiotic bacteria (in its live or raw form). However, fermented soy is still likely to contain as many phytoestrogens as unfermented soy, which are endocrine disrupting chemicals, and so excessive consumption of fermented soy is probably not a good idea in any case.
Examples of 'good' soy therefore include tempeh, natto, fermented tofu and soymilk, live soy milk kefir, live soy yoghurt - those products that have not been fermented so long and possibly miso and soy sauce - in moderation (these are the fermented types of soy that have been aged for a very long time). You can taste the free Glutamate in these products, to get an idea of their relative concentrations, and there is little evidence of this taste in soy kefir for example, but a very strong taste in Miso. Miso also contains a significant amount of salt which may accentuate this flavour.
Hydrolysis is a process whereby bonds are broken down chemically. In the case of hydrolysed protein, they are normally broken down enzymatically (using bacterial proteases). This results in a more bitter taste as more of the protein is in its constituent amino acid form. Hydrolysed protein is not usually 100% hydrolysed, and only a part has actually been hydrolysed, the rest remaining unhydrolysed. This may mean that the taste is not so bitter and more palatable. Hydrolysis of proteins (into hydrolysate) generally results in higher levels of free glutamate. Hydrolysed protein tends to contain glutamate at levels between 5 and 20%! Hydrolysed protein (e.g. hydrolysed soy protein) is sometimes used in place of MSG as a food additive as a flavour enhancer, but is rarely declared clearly on food labels as 'containing glutamate'.
This is why tomato sauces and fermented type sauces, and yeast extract based stocks are commonly used in cooking and added to processed food products.
These are often present in dried packet soups or flavouring sachets. Some manufacturers may declare such products as 'MSG free'! Hydrolysed soy protein is often found in vegetarian and vegan 'meaty tasting' food products.
Much fuss is made by some anti-MSG campaigners about the non-hydrolysed soy and whey protein isolates and concentrates, and soy lecithin with respect to Glutamate content. One may want to take this with a pinch of salt, as the hydrolysed versions of these proteins are more of concern. Lecithin is largely oil and carboyhydrate based and contains very little protein.
Glutamic Acid and Free Glutamate as Excitotoxins:
L-Glutamate (or Glutamic acid) is the most important excitatory neurotransmitter in the brain and plays an important part in brain chemistry. It is released by many different types of neurons and stimulates other neurons at the synapses. The excitatory neurotransmitters act to stimulate the next neuron (i.e. postsynaptic neuron) to fire an electrical impulse.
Inhibitory neurotransmitters tend to inhibit firing of neurons. The most important of these is GABA, which is synthesised from the amino acid Glutamine in the presence of Active Vitamin B6 (P5P). GABA is examined more on the Adrenal and Endocrine Systempage. Taurine is another, which performs many vital functions in the body, including nutritional metal transport into the cells. Taurine is examined in more detail on the Nutritional Deficiencies page.
GABA and Glutamate levels are balanced in the brain both in terms of absolute concentrations and relative ratios in a healthy individual. A P5P deficiency can thus result in an elevated Glutamate to GABA ratio in the brain and elevated levels of excitotoxicity. Excitotoxicity is the term used when the levels of the excitatory neurotransmitters are too high, at which point the level of neuronal activation or induced firing of neurons become neurologically damaging. Excitotoxins are a group of neurotoxins.
'Glutamate and GABA (gamma-aminobutyric acid) are the brain's major "workhorse" neurotransmitters. Over half of all brain synapses release glutamate, and 30-40% of all brain synapses release GABA. Since GABA is inhibitory and glutamate is excitatory, both neurotransmitters work together to control many processes, including the brain's overall level of excitation. Many of the drugs of abuse affect either glutamate or GABA or both to exert tranquilizing or stimulating effects on the brain.'
High levels of glutamic acid have been shown in animal studies to cause damage to parts of the brain unprotected by the blood-brain barrier, leading to a variety of chronic diseases.
'Excitotoxicity is the pathological process by which nerve cells are damaged and killed by glutamate and similar substances. This occurs when receptors for the excitatory neurotransmitter glutamate such as the NMDA receptor and AMPA receptor are overactivated. Excitotoxins like NMDA and kainic acid which bind to these receptors, as well as pathologically high levels of glutamate, can cause excitotoxicity by allowing high levels of calcium ions (Ca2+) to enter the cell. Ca2+ influx into cells activates a number of enzymes, including phospholipases, endonucleases, and proteases such as calpain. These enzymes go on to damage cell structures such as components of the cytoskeleton, membrane, and DNA.
Excitotoxicity may be involved in spinal cord injury, stroke, traumatic brain injury and neurodegenerative diseases of the central nervous system (CNS) such as Multiple sclerosis, Alzheimer's disease, Amyotrophic lateral sclerosis (ALS), Parkinson's disease, Alcoholism and Huntington's disease. Other common conditions that cause excessive glutamate concentrations around neurons are hypoglycemia and status epilepticus.'
I have personally experienced excitotoxicity, but in particular, when taking a supplement with a high Glutamate content, when excitotoxicity-based inflammation is already present, led to a bad headache and visual disturbances such as seeing extra shadows where there were none. This was relieved to some extent by taking some L-Theanine or GABA, but the excitotoxicity levels drop down to their 'normal' levels after a few hours.
There are four main classes of receptor that are stimulated by excitatory neurotransmitters. These are the AMPA receptors, kainate receptors, metabotropic receptors and N-methyl-D-aspartate (NMDA) receptors (discussed on the Nitric Oxide, Superoxide and Peroxynitrite page in regards to its role in excessive Nitric Oxide production).
Elevated free glutamate levels may also be linked to bipolar disorder (manic depression) and glutamate blockers such as Lamictal are sometimes used in its treatment. Trends that show increased suicide levels in US teenagers after its introduction into commercially prepared food sources and also huge increases in suicide rates in China may be illustrative of the effects of high free glutamate intake, or it may be a coincidence and explained on account of other factors.
Scientists are however not in agreement over the sensitivity of humans to excitotoxins, with some scientists believing that they do not affect humans, whereas others believe that humans are actually 4-5 times more susceptible to the effects of excitotoxins than primates and rodents. We can however look at examples of those suffering the effects of high free glutamate (including MSG) intake and their neurological symtoms. Links have also been made between MSG intake and increased obesity and raised blood glucose and insulin levels (akin to type 2 diabetes), although this is not solely on account of eating more processed foods, as MSG studies in rats illustrate.
CFS and ME are believed to be hyper-excitory states, often with insufficient GABA production, resulting in neurological damage over time. Excessive free glutamate and MSG consumption in such cases is clearly an extremely a very bad idea.
Excitotoxins, e.g. NMDA, are also examined in the Peroxynitrite section on the Cardiac page.
Of all the Essential, Semi-Essential and Non-Essential Amino Acids, only two have a negative side chain charge at pH 7, Glutamic acid and Aspartic Acid (the excitotoxins). All the other amino acids described above have a positive or neutral side chain charge at pH 7.
Some have speculated that because of this negative side chain charge, these two non-essential amino acids are selectively more readily absorbed at the expense of other amino acids. If this is the case, the undigested protein, combined with an impaired digestive system in individuals with CFS, could result in an excess of undigested protein which in combination with a high refined sugar intake could lead to excessive candida overgrowth.
Side Effects of excessive free glutamate consumption:
Some commentators report that the side effects such as 'hangover' type headaches associated with excessive MSG consumption are down to excessive salt intake and insufficient water intake.
Some studies have found symptoms including a temporary worsening of asthmatic symptoms, headache, nausea, chest pain, burning sensations, tingling, numbness, rapid heartbeat, drowsiness and weakness, at dosages of between 0.5 - 2.5g of MSG.
Ways to combat the effects of excessive free glumate:
Besides decreasing one's intake of free glutamate, in terms of hydrolysed protein, MSG or yeast extract containing products, which is of course the obvious remedy to any problems associated with high free glutamate levels, there are a number of biochemical means to protect oneself or at least to make oneself more resilient.
There are a number of pre-disposing factors that can make an individual more susceptible to 'neurotoxicity' associated with excessive free glutamate levels. By addressing some of these, where applicable, one can reduce the effects. Some of these include vitamin B6 and B12 deficiencies, magnesium deficiency, Coenzyme Q10 deficiency, excessive vitamin A intake (vitamin A toxicity), and also taurine deficiency. Decreased liver function, diabetes and/or autism can also predispose one to excessive sensitivity. By ensuring one's intake of these is sufficient for one's requirements, and ensuring that one's is not taking in too much vitamin A and assisting proper liver function, one can negate much of the negative effects of one's free glutamate intake.
As mentioned previously, an amino acid analysis profile can be useful in determining if one's glutamate levels are too high or not, and indeed the overall balance of amino acids in the body as indeed there are blood tests to verfiy the levels of the above cofactors and vitamins. Please see the Identification page for more information.
Aspartyl-Phenylalanine-1-Methyl Ester, a.k.a. Aspartame, E951 or by the brand name NutraSweet, is an artificially synthesised , non-saccharide, amino acid-based sweetener. Aspartame (or APM) is the methyl ester of the dipeptide of the amino acids aspartic acid and phenylalanine. It is 180 times sweeter than sugar, weight for weight, but with no calorific content. Like many other peptides, aspartame may hydrolyze (break down) into its constituent amino acids at a temperature of 85F or 29.5C) or under high pH (alkalinity), including the carcinogen formaldehyde and the toxins formic acid and methanol. It is thus unsuitable for baking.
Aspartame is commonly used in 'diet' products like Soft Drinks, but also in many other supermarket food and drink products, to improve taste without adding calories. The popularity of Aspartame is on account of the general public's taste for junk food, soft drinks (sodas or fizzy drinks) and also sugary foods, and concern about weight gain (as opposed to health concerns) associated with these types of foods and this type of diet in general. Aspartame was seemingly the 'magic pill' when it was first introduced in the late 1960s, the answer to consumer prayers. However, it is regarded as being inferior in taste to sugar and although no conclusive evidence officially exists (presumably on account of 'low concentrations' of formic acid and formaldehyde being produced during its digestion in the body, rather than examining the cumulative effects over years), studies do suggest that it may play a part in a number of health conditions and diseases. Herbal-based sweeteners like Stevia and sugar alcohol sweetners like Xylitol have unfortunately been overlooked by the food and drinks industry.
'Upon ingestion, aspartame breaks down into residual chemicals, including aspartic acid, phenylalanine, methanol, and further breakdown products including formaldehyde, formic acid, and a diketopiperazine. There is controversy surrounding the rate of breakdown into these various products and the effects that they have on those that consume aspartame-sweetened foods. The naturally-occurring essential amino acid phenylalanine is a health hazard to those born with phenylketonuria (PKU), a rare inherited disease that prevents phenylalanine from being properly metabolized. Since individuals with PKU must consider aspartame as an additional source of phenylalanine, foods containing aspartame sold in the United States must state "Phenylketonurics: Contains Phenylalanine" on their product labels. In the UK, foods that contain aspartame must list the chemical among the product's ingredients and carry the warning "Contains a source of phenylalanine" Ð this is usually at the foot of the list of ingredients. Manufacturers should print '"with sweetener(s)" on the label close to the main product name' on foods that contain "sweeteners such as aspartame" or "with sugar and sweetener(s)" on "foods that contain both sugar and sweetener". "This labelling is a legal requirement", says the country's Food Standards Agency.'
Aspartic acid is an excitotoxin, and may contribute to neurological damage at high concentrations in humans. Please see the MSG section above regarding excitotoxins.
A list of reported side effects from aspartame use can be found at the links below. These have been refereed to as Aspartame Disease by some independent researchers. It has also been linked to some CFS cases.
Possible links to Gulf War Syndrome and excessive formaldehyde consumption with soft drinks cans being stored outside in the desert sun for extended periods of time is discussed on the Acidosis page and at the links below.
The Food Standards Agency in the UK issued the following statement about APM.
The web site Green Facts has made the following statements about APM, denying any scientific basis for health concerns.
General Digestive Enzyme and Stomach Acid Deficiencies:
As discussed above, the term Food Intolerance is usually applied to the specific digestive enzyme deficiencies and the subsequent inability to efficiently digest certain types of carbohydrate. However, as many sufferers of CFS and related conditions can vounch for, and a discussed above, the digestive system as a whole may be somewhat impaired, meaning a broader spectrum of food groups may be less efficiently digested if large volumes of food or large amounts of a particular food type are consumed at once. Some may wish to define Food Intolerance as only the former more specific type, and call the latter type a more generic type of gastrointestinal malabsorption or digestive dysfunction. Indeed such digestive dysfunction may develop as a result of the former type and also Secondary Immune Response as described above. Both are however caused largely by a lack of appropriate digestive enzymes.
A list of digestive enzymes can be found at the link below, according to the food groups digested.
Carbohydrate intolerance need not be restricted to the carbohydrates listed above. Whilst bacteria thrive most readily on undigested or unabsorbed sugars and carbohydrates in the digestive tract, they can also break down and rot proteins. This is a more generic type of food 'intolerance'. The presence of dysbiosis may also contribute to the IBS symptoms experienced by CFS sufferers for a variety of food sources.
Such food intolerances may thus be more generic in nature, being a result of inefficient digestion of certain types or multiple types of food group, because of a general deficiency in digestive enzymes, or certain classes of digestive enzymes, e.g. sufficient stomach acid levels and protease enzymes for digesting protein lipases and bile for breaking down and digesting fats and oils, etc. Part of the problem may also be the inefficiency of absorption of nutrients from the digestive tract into the villi and into the blood stream. This may be a result of excessive a lack of enzymes to carry across nutrients from the digestive tract to the blood stream, resulting in further nutritional deficiencies and digestive dysfunction it could be because of damage to the villi in the gut, effectively shortening them, because of Celiac Disease it could be because of excessive build up of mucoid plaque in the colon which physically limits the amount of absorption of digested nutrients or indeed a lack of blood supply or oxgen to the cells of the digestive tract, etc. on account of impaired cardiac output or stress.
One may indeed experience just one type of such wind, specific to the foods that one cannot digest properly, or two or three kinds, a different type of wind at different points of the day according to what one has eaten hours before.
General Food Considerations:
Triticeae is a tribe within the Pooideae subfamily of grasses, including genera with many domesticated species. The major crop genera found in this tribe are wheat, barley and rye. (Bread) Wheat contains the genomes of 3 different species, only one of them originally a wheat Triticum species. The seed storage proteins (Gluten) in Triticaeae are implicated in various food allergies and intolerances.
Triticeae glutens are the seed stoage proteins in the mature seeds of the grass tribe Triticeae. The term 'Gluten' is used to describe the factors in bread wheat that give rise to the sticky property that allows dough to rise and retain its shape during baking. The same or very similar proteins are found in other Triticeae genera and species, but bread wheat contains the highest content and highest level of subcomponents, being a complex mixture of 3 grass species, Aegilops speltoides (Goatgrass a.k.a. Triticum speltoides), Aegilops tauschii - subspecies - strangulata (a.k.a. Goatgrass) and Einkorn wheat (Triticum monococcum), one of the earliest domesticated species.
The grains of non-Triticeae taxa also contain seed glutens with similar properties but do not match the 'performance' of Triticeae taxa and of these, particular the Triticum species (bread wheat, durum wheat etc.) Bread wheat has been optimised by cross fertilisation and hybridisation over millennia to offer the greatest elasticity, highest protein content and also a high cold weather resisistance. Wheat growing originated in Mesopotamia and Egypt.
Bread wheat is an allohexaploid, an allopolyploid with six sets of chromosomes, two homologous pairs or sets from each of three different species. It has undergone several millennia of hybridisation, and is somewhat far removed from the original wild grass species that were originally found and grown in the Tigris-Euphrates river-basin.
Of these four types of protein, the last two, Prolamin and Glutelin are what we consider to be constituents of Gluten in all Gluten-containing grains (Triticeae and non-Triticeae grains).
'Prolamins are a group of plant storage proteins having a high proline content and found in the seeds of cereal grains: wheat (gliadin), barley (hordein), rye (secalin), corn (zein) and as a minor protein, avenin in oats. They are characterised by a high glutamine and proline content and are generally soluble only in strong alcohol solutions. Some prolamins, notably gliadin, and similar proteins found in the tribe Triticeae (see Triticeae glutens) may induce coeliac disease in genetically predisposed individuals.'
'Glutelins are soluble in dilute acids or bases, detergents, chaotropic or reducing agents. They are generally prolamin-like proteins in certain grass seeds. glutenin is the most common glutelin as it is found in wheat and is responsible from some of the refined baking properties in bread wheat. The glutelins of barley and rye have also been identified. Typically there are HMW and LMW glutelins in these species, they crosslink with themselves and other proteins during baking via disulfide bonds. A HMW glutelin (glutenin) of the grass tribe Triticeae can be sensitizing agents for coeliac disease in individuals who possess the HLA-DQ8 class II antigen receptor gene (not yet characterized to the epitope level.)'
Gluten in bread wheat is a composite of two proteins, Gliadin (a Prolamin and a form of glycoprotein (sugar containing protein), and Glutenin (a Glutelin), combined with starch. It is located in the endosperms of certain grass-related grains.
The highest Gliadin concentrations can be found in the Triticeae grains Wheat, Barley and Rye. Giadin in bread wheat is encoded by 3 different genomes, AA, BB and DD. These produces slightly different Gliadins, which the body that can potentially produce different antibodies against. In general, Gliadin is the component of what is referred to as 'true Gluten' that is most generally associated with food allergies and intolerances.
Glutenin gives a grain flour its elasticity and grains high in Glutenin and Gliadin have been favoured historically as they are optimised for bread making. Gliadin is the most common constituent of Gluten that adverse immune system reactions occur with, although Glutenin can also be problematic for many.
As stated above, there are other grains and cereals of course that contain Gluten, but in a different form than in the Triticeae tribe. When most people and manufacturers refer to Gluten, they really mean Gliadin, from Wheat bread Gluten, or the Glutens of Rye and Barley, i.e. specifically the Gliadin and Glutenin content. Thus 'Gluten-free' really means Gliadin-free (and Glutenin-free), not necessarily Gluten free at all. However, most people assume or come to assume that Gluten to only mean 'true Gluten'.
Maize and rice for example contain proteins that are sometimes referred to as Glutens, but they do not contain Gliadin. Avenin, the Prolamin in oats, is known to be toxic to the intestinal submucosa in some Celiac Disease patients, although it is generally considered to be the least reactive of the grains. Rice gluten is the most significantly different in its chemical structure, but some may have an allergy or intolerance to it (i.e. an immune system mediated response). Basmati rice tends to be the best tolerated form and rice bran may cause a reaction in some individuals, on account of its higher protein concentration. Wheat breadcrumbs can be found in many coated or battered foods, and also in sausages.
As a general comparison of the highest risk gluten grains for those with food intolerances, one could follow this sequence in increasing order of likelihood of reaction: maize, oats, barley, rye, spelt, bread wheat.
These flours cannot be used as a straight swap for Gliadin-containing flour as they do not have the elasticity and will tend to crumble during bread making. However, they can be used as thickeners in sauces, and if combined with binders suach as grated apple, pectin powder, eggs and methyl cellulose, they can be used for pastries and bread-making. Alternatives include rice crackers, although these may be too high in simple carbohydrates (c/f Candida overgrowth or dysbiosis etc.) You can also buy/make buckwheat soba noodles, made with 100% wholegrain buckwheat.
Some of the highest Gliadin concentrations may be found in wheat extracts, such as wheat bran and wheat germ. Wheat bran, the outer hard casing or hull of the storage seed, is approximately 15.5% protein by weight. Wheat germ, the 'embryo' fraction of the seed, which is highest in lipids (and most susceptible to going rancid as a result), is approximately 30% protein! Normal wheat flour (based on the endosperm of the grain) is approximately 11% protein. Four used in pastry making is approximately 9% protein. Whole grain wheat flour and high gluten flour are approximately 14% protein. Wholegrain flour has a shorter shelf life than white flour on account of the germ and bran component going rancid more quickly.
Certain types of bread contain wheat flour with 'extra Gluten' added, in order to make them stronger. Examples include French sticks or French bread.
If you have a reaction to the higher protein (higher bran) versions of specific grains and cereals, then you may choose a lower protein form of them which you do not have any reaction to, for occasional consumption. Or perhaps just choose another grain to eat which provokes no reaction, even in the higher protein/fibre forms. There is clearly a balance between consuming enough fibre and avoiding proteins that cause you a reaction to. By consuming large quantities of a grain with little fibre is not going to do you any good if you have an issue with dysbiosis, or indeed may encourage dysbiosis over a period of time. Indeed, a lack of fibre may also cause an excessive build up of mucoid plaque. So if you are cutting out fibre in one area, you should make sure you are getting it from another source. And eating large amounts of any 'white' grain is perhaps not the best way of consuming carbohydrates, as complex carbohydrates are better. There is therefore potential for conflict with the Anti-Candida Diet and the Gluten Free Diet. As Food Intolerance can fuel the growth of dysbiotic and pathogenic micro-organisms, then one may well need to keep both in consideration, as even on an Anti-Candida Diet, if you are eating foods that you are intolerant to, then you are still fuelling the bacteria and attempts to kill them off may be ineffective.
True Gluten (or Triticeae tribe gluten), whilst found in fairly high concentrations naturally in wheat, barley and rye grain products, is found in significant concentrations in certain condiments and foods, as an additive or by food processing. e.g. as a stabilising agent in ice-cream and ketchup, which arguably have little nutritional value and contain refined sugar in any case. Such sources of Gluten are often referred to as Hidden Gluten.
It should be noted that the actual grass component of wheat and barley do not contain the protein Gluten, but contain proteins in other forms. Wheat grass and Barley grass are vegetables, and therefore technically speaking Gluten-free in an idealised manufacturing process. However, given the fact that some other grain products such as oats frequently contain traces of wheat (e.g. up to 70% of US oat stock is contaminated with wheat gluten), as they are either harvested at the same time as wheat or use the same processing equipment, then it is all the more likely that wheat grass and barley grass may similarly be contaminated with traces of actual Wheat or Barley grain. One may wish to consider this if one regularly consumes cereal grasse juice or powders. Some Barley Grass powders make statements such as 'Wheat Free' on the packaging - but not state Gluten Free! That is not to say that it does not contain traces of Barley grain and thus Gluten.
A widely quoted statement made by Cynthia Kupper, Executive Director of the Gluten Intolerance Group (GIG) of North America (www.gluten.net):
'According to information from USDA research chemists, specializing in wheat gluten and cereal proteins and a statement from the American Association of Cereal Chemists, gluten is found only in the seed kernel (endosperm) and not in the stem and grass leaves. If the grass is cut from a growing plant and does not include the seed kernel, it should be safe for persons with gluten intolerance to use. Wheat and barley grass are promoted as having superior nutrients, however the nutrient composition of the grasses is not superior to eating a variety of fruits and vegetables, which would be overall more healthy and less expensive than using this supplement. Bottom line is that I would stay away from it at this time and eat more fruits and vegetables!ÊMy personal and professional choice is not to use these products.Ê Instead, rely on a variety of gluten-free grains, fruits and vegetables for a nutrient-rich diet.ÊFeel that you must include a grass in your diet I would recommend alfalfa grass instead of the wheat or barley grass. As for sprouted wheat or other gluten-containing grains. These are sometimes used in breads that claim to be gluten-free. In talking with many of these bread companies, they claim their breads have no gluten, but none can guarantee that the seed kernels are completely removed before the sprouts are used or that their products have been tested for gluten content. This presents an unacceptable risk for persons with gluten intolerance. GIG does not recommend these products on a gluten-free diet.'
If you grow and harvest your own Wheat grass or Barley grass, growing them in a small tray or otherwise, then you can be sure they are Gluten-free of course assuming you know what you are doing and they are harvested before the grasses have matured to the stage where they produce grains. For those who like green superfoods, one can however rest assured that algae-based foods like Spirulina are going to be 100% Gluten free!
There are sources of Gluten-free cereals, such as Hale & Hearty Gluten Free Oats. However, they are perhaps 2-3 times more expensive than ordinary oat sources. However, if one is sensitive to Gluten, then they may be an alternative. That is not to say that the given person may not be allergic to Oats or indeed Rice. For example, in January 2010, I tried one brand of organic Gluten Free Oats, and developed a sore throat a short while afterwards in a similar fashion to regular organic oats.
Certain supplements contain Gliadin on account of its resilience to stomach acid, and as such is used Gliadin is used as a delivery mechanism for certain fragile/sensitive enzymes, such as Superoxide Dismutase (SOD), which is fused with Gliadin to form GliSODin. GliSODin is a registered trademark. It is usually described in the ingredients in the relevant products as 'Superoxide Dismutase/Gliadin Complex (GliSODin), e.g. Life Extension SODzyme.
For a detailed analysis of the composition and digestion of Lactose, milk sugar, please see the Metabolic Food Intolerances section above.
For some individuals, the (immune system mediated) intolerance or allergy to milk may be caused by the denatured protein of pasteurised as opposed to the non-denatured protein of raw (unprocessed and non-heat treated) milk. This may also be true for whey powders that use a non-heat treated whey source. Certain whey powders included partially digested whey protein, which may also help. If the immune system is reacting to the protein component of dairy products, then clearly the higher concentration dairy products may be more problematic as they contain more protein, for example, whey protein or cheeses.
Depending on the type of food intolerance you may have towards dairy, it can affect which types of dairy products you can tolerate more than others. Avoidance is probably the best strategy, but in some cases, occasional consumption may not cause any noticeable symptoms. Milk products are 'hidden' in a variety of food types where they are not normally expected to be found.
The predominant protein in cow's milk is Casein. Casein is a type of phosphoprotein and makes up approximately 80% of the protein content in milk.
Whey, a.k.a. milk plasma, is the liquid remaining after milk has been curdled and strained. It is also the by-product of cheese or casein manufacture. Some harshly refer to it as a waste. It has a number of health benefits for those who are not sensitive to dairy. Whey protein are the globular proteins (globinstagers) isolated from massive whey, typically 65% beta-lactoglobulin, 25% alpha-lactalubmin and 8% serum albumin. Whey has the highest known biological value (BV) of any known protein (100). BV is a measure of how efficiently a substance can be digested and absorbed through the villi of the small intestine into the blood stream, maintaining its original form.
Cow's milk is quite rich in protein and less watery compared with the milk of other animals,e.g. Goat's milk, and also Human mother's milk. This is why cow's milk is favoured in general. However it is the same reason that it is thought to cause more immune system reactions in susceptible people. If you are allergic to cow's milk, consuming less of an antigen is by no means the same as consuming 'no antigen', and Goat's milk should not be considered more than just 'less problematic'. It is still likely to be a problem in susceptible individuals.
Butter may be tolerated by some as it is mostly milk fat and water, containing little protein, and others may tolerate UHT milk but not normal pasturised milk.
If the lactose content of dairy products are causing a problem (i.e. metabolic food intolerance), It is likely that hard cheeses, such as Swiss, Emmental and Parmesan, will be best tolerated as they contain no lactose (all used up in fermentation and cheese production). Otherwise, live fermented milk products such as natural yoghurt or kefir will be lower in Lactose, the probiotic bacteria and yeasts having consumed some of the Lactose already (depending on the duration of fermentation). Lactose intolerance usually means one can tolerate a small amount of lactose but more than a certain amount, it will start ot appear further down in the intestines where it should not be. Therefore, one may still be able to consume milk, but just in very small amounts, e.g. with a cup of tea. Drinking a glass of milk or having cow's milk with your breakfast cereal (which may itself often contain milk powder as well as large amounts of refined sugar).
Infants should ideally be breastfed with their mother's milk rather than being given infant formulas or warmed cow's milk, which is intended for the infants of those animals. Even soy contains too many phytoestrogens that can affect a child's hormone balance. It is amusing to think that adults think the idea of drinking the milk from a woman's breast is disgusting but would happily drink milk that came from an animal's breast. Arnold Schwarzenegger was asked in the movie Pumping Iron by an interviewer whether he drank a large amount of milk to help with his muscle growth, he responded 'When I go out, I like to have a beer. Milk is for babies!'
I am not suggesting that beer drinking is very healthy either, but it is an amusing but poignant quotation in many respects.
Growth hormones are only still used in the USA. Some commentators generalise and imply that artificial growth hormones are used in all non-organic animal farming, but this is not strictly true. Bovine Growth Hormone (BGH), a.k.a. Bovine Somatotropin (BST), is a protein growth hormone produced in cattle. A synthetic version of the hormone was first created in 1994, known as recombinant bovine somatropin (rBST) (a.k.a. recombinant bovine growth hormone or rBGH or simply artificial growth hormone). rBGH has been used to make cow's grow bigger and to produce more milk volume. Milk from rBGH treated cows contains higher levels of IGF1 (Insulin-like Growth Factor 1) and also contains small amounts of puss where the too much milk from the rBGH has caused inflammation of the udders. IGF1 has not been conclusively proven to be detrimental to human health (and linked to an increased cancer risk) although studies on rats have revealed that it has a slight element of toxicity. The brand is Posilac, currently owned by Elanco Animal Health, a division of Eli Lilly & Co. rBGH was banned in Canada, Australia, New Zealand and most of Europe by 2000. Imported milk or beef from rBGH treated animals to these countries is not permitted, but convenience foods and condiments containing dairy ingredients from the USA (regardless of source) are permitted strangely.
Milk can be a nutritious addition ot one's diet in moderation, if one's immune system can tolerate the protein, and one has sufficient lactase enzymes to deal with the lactose. There are many other dietary sources of Calcium, for example, Soya milk, various beans, sesame seeds, brazil nuts, hazelnuts, okra, spring greens, water cress, parsley, and some fruits. Please see the Nutritional page for more information. Some even argue that regular dairy consumption prevents the absorption of Calcium and causes osteoporosis (on account on too high a Calcium intake.
Hazelnut is a food type that is sometimes identified in IgG blood testing as being a food that one reacts to. However, some commentators argue that this is a reaction, but not an allergic one (despite the test result). The Hazelnut protein is irritating to the tongue and it titillates the palate in small doses. This is why Hazelnuts are often used by Chocolatiers as opposed to other nuts. I have always wondered why Hazelnuts were used as they were never his favourite nut particularly.
One could however interpret this behaviour of hazelnuts as being reflecive of Oral Allergy Syndrome, that is a cluster of allergies (including IgE) in the mouth (typically burning sensation or itching of lips, mouth and/or pharynx) to eating certain fruits, nuts and vegetables, typically noted in hayfever sufferers who have cross-reaction with compounds in these foods that appears similar to birch pollen. These foods can include: apples, hazelnuts, peaches, cherries, almonds, pears, carrots, and celery. The symptoms are arguably somewhat different to those the majority of people who eat hazelnuts without itchy lips etc. It is more of a mild (physical) irritation to the tongue as opposed to an immune system-mediated response that affects more parts of the head and throat.
Tomatoes are a type of fruit that is frequently implicated in IgG reactions in susceptible patients. Some commentators argue that this is on account of their acidity or because of the properties of their skins (perhaps not having been washed properly and still being high (in relative terms for a person with multiple chemical sensitivities) in pesticides etc.) Sufferers tend to experience fewer symptoms when the Tomatoes are cooked than when eaten raw. Tomatoes are very high in antioxidants (as are other red fruits). Cooking tomatoes also helps to free up the lycopenes (red carotene pigment and phytochemical). Lycopene is considered helpful in preventing prostate cancer.
However, it should be noted that Tomatoes are rich in fruit sugars and also free glutamate, and may not be suitable for someone on an Anti-Candida Diet or who has Fructose-related disorders, or for someone who has a sensitivity to Glutamate/MSG.
Some commentators have argued or theorised that before agricultural societies evolved, those individuals that had more sensitive immune systems were generally better adapted to the natural environment than those who did not, as they were better able to seek out and destroy viruses and other infections in their bodies. Those individuals with antibodies that were less reactive were perhaps less inclined to survive, and more likely to fall victims of Natural Selection. Thus the law of Survival of the Fittest would dictate that more individuals with sensitive immune systems survived in each subsequent generation. The genetic and phenotypic predisposition to mistaking certain protein forms as viruses is from one perspective a good thing. However, with the advent of commecial food production and agriculture, and especially with hybridisation, this characteristic of having a more sensitive immune system then becomes a potential hazard to one's health, if one is not aware of the situation, well informed and that one is consuming proteins that resemble toxic and pathogenic viruses. Thus one could argue that modern society from a Neo-Darwinian perspective encourages the weaker and less robust and punishes the naturally 'stronger', thus creating a genetic disadvantage in the human gene pool, which as discussed above, arguably affects large segments of the population, who may be more prone to developing other allergies, asthma or even autoimmune diseases.
However this is not to say that the human body cannot adapt to som extent, and the various protocols to taming the immune system described below bear witness to this fact. In addition, when it comes to non-genetic metabolic food intolerances, e.g. Lactose Intolerance, over generations, a population may develop the ability to produce more Lactase, perhaps not through 'Natural Selection' as the 'ill' do not just die off or stop having children, in general, they just have a more miserable existence.
Some argue that there is nothing intrinsically wrong with any of the food sources that cause food sensitivities in some individuals, and in those individuals who do not suffer from these problems, they are a good source of nutrition.
Others, such as Dr Kenneth Fine of Enterolab, and various other natural living and natural food promoters, argue that Gluten containing grains and indeed milk, are 'unnatural' food sources. Some of the reasons for this have been discussed above. In addition, the majority of the population of the USA, for example, has some genes associated with Celiac Disease, even if excessive ATA production has not yet manifested itself, and that eating Gliadin over the long term may be a high risk strategy, as one might possibly develop a propensity towards Celiac Disease later in life. Thus Kenneth Fine argues that adopting a Gliadin(Gluten)-Free Diet is a sensible strategy for preventative medicine and health.
Whether such proteins are 'toxic' as they resemble viruses is another matter. However, there is considerable evidence to suggest that consuming large quantities of gluten containing foods, especially Gliadin, and indeed dairy consumption is not something the human body is generally geared towards digestiing nor indeed has been geared to digesting over the 10s of thousands of years we have been Homo sapiens and many 100s of thousands of years and indeed a million or so years in pre-hominid species. These are convenience foods, in the case of wheat, that have allowed modern society to evolve. In the case of Dairy, it is perhaps more of a vice than anything else!
Wheat and dairy do not appear to be particularly good for anyone, it is perhaps more a case of how much the irritation they potentially cause bubbles over the surface into immunological and other factors that are deemed to be significant or not. It depends where you want to draw the line perhaps. This is true for many other foods of course, but particularly more so with Wheat and Dairy. There are many other food sources available and it depends on your own personal judgement and choice at the end of the day, as it is your body. But seeing as many of the reactions to foods go unnoticed, it might be wise to at least investigate whether you do have any forms of Food Intolerance or not.
Observation, Elimination, Reintroduction:
One can observe the symptoms of food allergy, intolerance or sensitivity through observation of symptoms after eating certain food types, how and when they occur. Most people are familiar with their allergies if the symptoms are very severe, but if they are mild, and they are not familiar with the range of possible IgE food reactions or indeed, other immune modulated food sensitivities, and signs of food intolerance, then they may not believe there is a problem with the food types they are eating.
The easiest way to identify the potential problem foods is through testing, and totally eliminate them one's diet (e.g. start a gluten- or dairy-free diet) as otherwise the traditional 'elimination diet' involves removing one food type at a time from one's diet and observing symptom changes over many weeks, and then reintroducing it and starting on the next food type, but without any direction or prior knowledge, this is a very slow alternative.
If one eliminates certain food sources, one should only do so with the advice of a nutritionist so that one does not omit any important food groups or nutrient sources. Elimination means replacing one thing with another, in order to maintain one's calorific intake and also to ensure one is not losing sources of nutrition from one's diet. Elimination does not simply mean that one will skip breakfast because one cannot eat whatever food type one is used to eating at that time.
One example of an elimination diet is the Gluten-free or Dairy-free diet. If one is wanting to eliminate the food type to allow the symptoms of the food intolerance to subside, before one reintroduces it as a 'food challenge' to see whether there really was a reaction or not, then the recommendation is to avoid that food type for a minimum of two weeks. Some practitioners recommend 3 months, but this may perhaps pose a different type of approach, where one is looking not just to identify a food intolerance but to treat it.
One may find that one has cravings for some of the food types that one has eliminated or a possible worsening of symptoms during the first couple of days of avoidance/elmination. This is not uncommon and is nothing to be concerned about. This may be partly due to the body wanting to continue its disequilibrium and that avoidance starts to create a physiological change in the body that feels new and strange. It may also be due to excessive physiological adaptation to simple carbohydrate consumption or for other reasons. It is perhaps in some sense like breaking a bad psychological habit, the mind has cravings to go back to its own habit, even though it is not in its best interest.
During the avoidance phase, one can note any changes in how one feels, and either stick to this new regime, or experiment with reintroducing some of the suspected problematic foods (in significant quantities if one knows one does not have an IgE reaction to them - after at least 2 weeks) and notice what effect it has on the body. If one starts to feel better whilst eliminating a certain food type, then this may well indicate that one has a food sensitivity to this particular item.
Reintroduction, a.k.a. food challenge should be a single portion of that food item, and careful observation of symptoms over the next few hours. If no observable symptoms are noticed, then one may elect to eat another portion of that food type the following day. and assess for symptoms again. If the symptoms are severe, then you should avoid this food type for a prolonged length of time. This reintroduction or food challenge should verify whether one's suspicions were correct or not. If the challenge symptoms are mild, you may want to consider only eating it occasionally.
Another variant on the food challenge is to eat a very large amount of that particular food type of the day of the food challenge (after a 2 week total elimination), and then avoid it again for 2-3 days, all the while observing the effects. Continue with the avoidance of that food type and move onto the next food challenge (of the next food type, 2-3 days after the previous food challenge). This assumes that you stopped eating all the food types to be tested/challenged at the beginning.
Reintroduction of certain food types (a.k.a. food challenge) after only brief elimination may well result in a swifter and stronger response than was experienced when the food types were consumed every day or regularly. This can be useful if one is looking to simply identify a food intolerance reaction, but if one is looking to treat the food intolerance, then clearly one should try to aim for prolonged avoidance. Certain food types you may wish to avoid for months or years or indefinitely.
In general, prolonged avoidance tends to build tolerance. When you reintroduce the food type after careful avoidance for weeks or months, the reaction to the food may be diminished. However, copious and regular consumption of that food type again may well build up the adverse reaction again.
Be aware that just because you are avoiding Gliadin for example, if you are Gliadin sensitive, does not necessarily mean that your gut will improve significantly, if there are other complications involved. If you have significant levels of mucoid plaque and bacterial and candida overgrowth and you are simply eating low fibre, high carbohydrate gluten-free foods (e.g. Gluten-free comfort foods, soya milk and cornflakes), your IBS-type symptoms may not improve, and indeed may become much worse. Equally, if you are substituting foods for those you have eliminated, be aware that you may be introducing foods that you are intolerant to. You have to take all factors into consideration.
A structured approach to elimination and reintroduction, as part of taming food allergies and sensitivities, is discussed in the next section. One should determine what one's approach and strategy should be from the outset or one will invariably end up being unstructured and achieving very little at best.
It is useful to keep a food diary and note any changes in symptoms in this each day and/or each week, and one can go back and refer to this, when excluding further foods from one's diet. It is also recommended to do the above in conjunction with a qualifiied nutritionist and allergy specialist, who can provide you with advice and monitor your progress as you go along. It is a common occurrence for over-zealous parents to simply eliminate certain food types from a child's diet, often erroneously (i.e. misidentification of the problem foods) and not replace that food type with anything else suitable for the child's nutritional needs.
One should note that the presence of other diseases and conditions (e.g. microscoptic colitis) may mask the change in symptoms one would normally have experienced with an elimination diet.
Food Intolerance, i.e. the absence or low levels of specific digestive enzymes, can be detected formally by a Hydrogen Breath Test. This works on the basis of ingesting a fixed amount of a given type of sugar, and breathing into a Hydrogen gas detector every 20 minutes for a period of 2 hours. If the sugar is not digested properly, then there will be a rise in bacterial activity to ferment that sugar. One of the byproducts of such fermentation is Hydrogen gas, which is absorbed into the blood stream and is dissipated out of the lungs in the breath. In general, hydrogen levels tend to rise moderately if one is not intolerant, but rise massively if one is.
Please see the Tests page for more information.
IgA, IgE, and IgG antibody testing for a variety of food types is available in the form of blood tests and stool tests.
For IgE testing, i.e. for food allergies, a RAST (RadioAllergoSorbent Test) blood test is usually employed, to detect the levels of IgE antibodies present in blood plasma to a particular antigen or antigens being tested for. Some critics argue that most laboratories who provide IgE testing do not request/take a large enough blood sample to do the testing properly and so the blood tests often come back negative. It may be best to enquire with a particular laboratory as to their test methodology, how much blood they require and how it compares with the next one.
Whilst IgG blood tests are quite convenient, the localised IgG and IgA levels in the colon may be elevated in response to certain food types, and the levels in the blood stream may not be detectable at a given stage in one's condition. IgG blood testing is arguably still not clinically verified, and a negative or indeterminate result for IgG antibodies for Gliadin (for example) does not necessarily mean you definitely do not have a sensitivity to Gliadin. Observation of symptoms may perhaps be more reliable. However it can still be a useful tool, especially as it can cover so many possible food sources in one test, and if used in conjunction with other forms of testing and observation.
Celiac Disease Testing is usually performed by measuring levels of anti-tissue transglutaminase (tTGA) and anti-endomysium antibodies (EMA) in the blood or preferably the stools, in other words a method of detecting Celiac Disease (the resulting inflammation) before it has actually developed. These anti-tTG antibodies and anti-Gliadin antibodies are not generally found in the blood of many Celiac patients. Detection of these antibodies in the stool is however 100% reliable.
Please see the Tests page for more information.
Intestinal Malabsorption Testing:
Intestinal malabsorption is one indicator of the progression of genetic Gliadin sensitivity to the point where symptoms of Intolerance are occuring (i.e. Celiac Disease). The shortening of the intestinal villi will result in less absorption of nutrients and thus a great proportion of unabsorbed or bacterially fermented nutrients in the stool. Of course, there are a number of other reasons why intestinal malabsorption can occur, and may be related to metabolic food intolerance (i.e. genetic or phenotypic deficiency in a particular carbohydrate enyzme, e.g. Lactase), or it may be due to a more general deficiency in enzymes that is acquired, e.g. that present in CFS, ME and Fibromyalgia patients, with deficiencies in stomach acid and enzyme production (i.e. biochemical problems resulting in these deficiencies in production). A test for intestinal malabsorption is therefore a direct measure of the intestinal damage caused by Celiac Disease, unlike Antibody levels, assuming no other factors for intestinal malabsorption are operating. In many cases an intestinal malabsorption test provides inform about both Celiac induced villi damage and also any insufficiencies in pancreatic enzyme production. It is difficult to separate out the two. Antibody tests can however tell you about damage that may be occuring now and/or that will be occurring in the future unless one changes one's diet.
There are various different stool tests available to detect for intestinal malabsoprtion, some of which are specifically for Celiac Disease (e.g. Enterolab) or geared towards dysbiosis (e.g. Doctor's Data) which still examine some of the same parameters. Regular stool tests may also shed some light on the possibility of Celiac Disease, in particular stool pH, Lymphocyte counts, the presence of (undigested) fat stains etc. Neither of these are 72 hour stool collections, collecting all stool in that period (!), as with some older types of tests, but are single collections.
Genetic Testing for Celiac Disease:
The genes that control the immune system's reaction to Gliadin (Gluten) are the Human Leukocyte Antigens or HLAs. There are several types of HLA genes with each person, the HLA-DQB1 locus type being the most useful in determining the probability that a person may be sensitive to Gliadin. HLA-DQB1 alleles belong to the HLA-DQ2 serotype group.
The presence of the genes (or HLAs) associated with Celiac Disease and Gluten Sensitivity in the tissue Transglutaminase, when combined with Gliadin stimulates the body's immune response. Each HLA-DQx is a Human Leukocyte Antigen Serotype within the HLA-DQ serotype group. Each DQ class gene contains two heterodimers or gene pairs (alleles), which together form the DQ heterodimer, a cell surface receptor essential to the function of the immune system.
The older style 'serologic' type used to describe HLA-DQ genes include the numbers 1 to 4, i.e. (HLA-)DQ1, DQ2, DQ3 and DQ4 including integeric types , DQ5 and DQ6 as subtypes of DQ1 DQ7, DQ8 and DQ9 as subtypes of DQ3. Because the actual protein structure on the cells, as determined by the serologic typing, that determines the gene's biological action, genes with the same serologic type tend to function almost identically, biologically speaking, e.g. HLA-DQ3 subtype 8 (one of the main Celiac genes) compared with HLA-DQ3 subtype 7, 9 and other DQ3 sub-subtypes.
- (a more Northern European Caucasian gene)- 90% (a.k.a. DQ3 subtype 8 - a more Southern European/Mediterranean Caucasian gene) - 9% or DQ3 - comprising less than 1%
Studies to date show that for Gliadin/Gluten Sensitivity to result in Celiac Disease (i.e. the villous atrophy of small intestine), it requires at least 2 other genes also. Thus, not everyone with DQ2 or DQ8 will develop villous atrophy when ingesting Gliadin regularly.
Dr Kenneth Fine believes that anyone with thes above genes will incur some sort of immune response to Gliadin. According to Fine's latest research, when DQ1,1 and DQ3,3 are present together in the same individual, they result in far more severe immunological responses to Gliadin that if one only had one of the Celiac Genes alone (e.g. DQ2,2, DQ2,8 or DQ8,8 which tend to portend a severe form of Celiac Disease).
Of the remaining 19%, most have DQ7,7, a pair (allele) almost identical in structure to DQ2,2 (the most predisposing of all the Celiac genetic combinations), which Fine has found have very high Anti-Gliadin Antibody counts in. He postulates that it is only really those who have DQ4,4 that have no genetic presdisposition to Gluten sensitivity at all - a rare gene combination in Northern America.
Dr Kenneth Fine believes that because testing for the HLA-DQB1*201 locus type as opposed to testing for both it and its heterodimer HLA-DQA1*0501 is the most efficient and cost effective manner to detect for genetic predisposition. Fine has found that DQ2 positivity being the Celiac-related HLA-DQB1*0201 allele is overhelmingly more frequent that the 0202, 0203, 0204 or 0205 alleles. By linkage disequilibrium, the HLA-DQA1*0501 will usually accompany the HLA-DQB1*0201. The presence of HLA-DQ2 assessed serologically (i.e. the functional presence of any DQ2 gene product) has always shown itself to produce antibodies to bind to Gliadin, and therefore predispose a person to Gliadin sensitivity (with or without the villous atrophy).
As mentioned, 90% of Celiac sufferers have the DQ2 gene, and so a test such as Enterolab's for one of the heterodimers of the DQ2 gene will only capture 90 out of 100 genetically predisposed Celiac sufferers. However, if the test is taken in conjunction with a stool test for AGAs and ATAs, then a more complete picture can be obtained.
Having the HLA-DQ genes does not definitely mean one has Celiac Disease now, but that Gliadin sensitivity is possible and a risk for the future. Genetic testing is most useful when performed in conjunction with Antibody Testing, in particular Stool Antibody Testing for Anti-Gliadin IgA Antibodies (AGAs) and Anti-tTG IgA Antibodies. HLA-DQ testing can also be useful in patients who have been on a Gluten-free diet for many years, and may not have any measurable IgA or IgG antibodies against Gluten to detect, but who may still be at risk of relapse of symptoms if Gluten is reintroduced - a Gluten challenge in such cases is unreliable.
Please see the Tests page for more information on Enterolab tests.
Lymphocyte Proliferation Tests (LPT):
These are blood tests that isolate White Blood Cells (Lymphocytes or WBCs) and expose them to quantities of a specific food type in order to observe their behaviour. Such testing is slow and expensive and not the preferred route for most patients when it comes to Food Sensitivity Testing. Such tests include Nutron (involving a Nutron diet), Cytotoxic and ALCAT and FACT tests and are not fully scientifically validated, and may not correlate with other allergy testing methods' results.
Applied Kinesiological and Muscle Testing
It is theoretically possible to test a variety of food types using Applied Kinesiology or Muscle Testing (or other Bio-Feedback Testing). This form of testing is discussed on the Tests page and Treatment Approach page. It is used successfully for many patients in conjunction with determining the best combination of supplements to use. However, for food types, it may be less practical, to bring food types with you to your appointment. A friend could help test them for you. It may be impractical to use this form of testing for all food types and groups, instead perhaps using it as a back up or for a specific food. The above forms of testing would probably suffice.
Bio-feedback devices are also reputed to detect the presence of allergies in the body, even those which do not yet come up on IgG testing or which one has not yet noticed, e.g. certain foods that one has been eating regularly. Bio-feedback devices are often much quicker than manual kinesiological testing.
If one is experiencing either an allergic response, slow immune response or intolerance symtpoms to a given food type, it would be highly sensible to refrain from eating this food type in the short term, to allow the body a chance to recover and function more normally. This is especially important for foods that you experience a rapid, IgE type reaction to.
As discussed above, an Elimination Diet is a useful method of identifying a food sensitivity. One may choose to go different routes from there, and elect to either completely avoid the given food type, to consume it only very occasionally if there is only a moderate non-IgE type reaction to it, or to embark on a programme of controlled reintroduction, after a sufficiently long abstainance period. Your practitioner and/or nutritionist should be able to offer you specific advice on the amounts and frequency of consumption of the problem foods, as too much or too often could result in the return of your adverse symptoms and lower energy levels, or much worse. In general, Elimination Diets with Controlled Reintroduction are considered to be a viable strategy for gradually de-sentisiting the body to foods that the immune system reacts to, either IgE, IgA or IgG. Of course, one does so at one's own risk, and consuming too much of a food one has a potentially life threatening reaction to is not clever and can result in death. It is doubtful that Controlled Reintroduction would do anything for classic Food Intolerance, where a deficiency in Enzymes is the main problem.
There is of course nothing wrong with simply avoiding problematic foods. It doesn't 'solve' the reason for the reaction but can in the short term and long term result in a reduction in symptoms and the effects of food sensitivites and allergies. Adverse symptoms from Celiac Disease tend to resolve more quickly in the short term than general non-IgE-mediated immune reactions to food, but of course the damage to the intestine may take some time to heal. Kenneth Fine has found that Celiac Disease tends to resolve itself in 6 to 12 months once a rigid Gluten-Free Diet has been followed, with the intestinal villi restoring themselves back to their original form again. This process may be accelerated with some of the supplements used for treating Leaky Gut Syndrome. Kenneth Fine in his early research has found that many autoimmune conditions also improve with the elimination of Gliadin from one's diet. The more adversely immune stimulating foods one removes from one's diet, the greater the benefit it is likely to have on one's well being and also any autoimmune diseases present. This may depend on the individual, but common examples, as discussed above, including dietary yeast, some other grains and soy. For arthritic patients the nightshades are often particularly pertinent (e.g. tomatoes, potatoes, egg plant and red hot chilli peppers).
It may also be applicable to adopt an Anti-Candida Diet and adopting certain anti-microbial treatments whilst treating Food Intolerance, to treat the downstream effects of the Dysbiosis and other harmful overgrowths that may have arisen in the colon on account of the Food Intolerance over time. As discussed in the Gluten section above, there may be some conflict between the two types of diet, so one may have to use one's common sense in balancing and harmonising the two approaches and avoiding grains where only the low fibre, high carbohydrate forms are tolerated. In addition, many 'gluten free' convenience foods being sold are high in sugar and are not really very good for you. Common sense applies, and just because something is 'vegetarian' or 'gluten free' does not make it a healthy food necessarily!
Supplemental Digestive Support:
Digestive support will not likely directly affect the fast and slow immune system responses to problem foods in the short term, although better nutrient absorption and better digestion of proteins and carbohydrates will help the body in general and may serve to calm down the immune system to some extent in the long term.
The treatment of food allergies and intolerance reactions involves several components, avoidance or limitation of those food types or ingredients that cause the problems, to support the digestive tract and system, and to try to tame the body's immune system response. One component of this taming of the immune system response is to avoid certain triggers of incorrect and overactive immune system response. Stress or more specifically brain overstimulation or hyperexcitation can be one cause of elevated adverse immune system responses to certain foods. Prolonged periods of stres or intellectual and mental stimulation or computer use over many months may result in less ability to full relax or calm the brain, which may in turn result in more inflammatory type responses in the digestive tract. Excitotoxicity caused by elevated free Glutamate and Aspartate levels may also result or contribute to overstimulation or excitation of the neurons, as discussed above. Stress or overexcitation of the brain is one factor of many possible triggers in activating the immune system and excessive inflammatory response and oxidative stress.
The presence of heavy metals in the body may also be implicated in adverse and excessive immune system responses to certain food items or indeed in cases of Multiple Chemical Sensitivies (and other inflammatory illnesses driven by excessive Nitric Oxide/Peroxynitrite formation). The removal of heavy metals from the body by chelation may temporarily elevate the levels of heavy metals circulating in the blood, which may temporarily elevate the degree of sensitivity to problem foods or indeed to harmful electromagnetic fields or other external adverse stimuli. In the long term, mind calming techniques, avoidance of problem foods, heavy metal chelation and/or antioxidant therapy may reduce such symptoms. It seems that many of these stimuli can result in a vicious circle of elevated inflammatory responses. In other words one needs to keep one's focus slightly wider than just food and look at all lines of causation.
Treatment of Systematic Microbial Infections:
The presence of bacterial, fungal and parasitic infections in the GI tract, and the necessity of their eradication, have been mentioned briefly above. Pathogenic micro-organisms can also be present as systematic infections, i.e. outside of the GI, e.g. in the bloodstream, organs, and even inside the cells (intracellular). Here they can put a constant strain on the immune system and in many cases excrete neurotoxic biotoxins (i.e. neurotoxins) that interfere with nervous system function, and to some degree, our immune system function. Such organisms may be introduced into the bloodstream via the digestive tract (e.g. leaky gut syndrome), via dental infections, or via insect bites (e.g. tick bites).
Examples include Cell Wall Deficient (CWD) bacteria such as mycoplasma, Borrelia species bacteria (the primary cause of Lyme Disease), Lyme Disease co-infections such as Babesia protozoa, Bartonella bacteria species, Chlamydia pneumoniae (Cpn) etc. These infections can be detected by advanced blood smear microscopy, PCR blood tests, and also by muscle testing although these methods are not 100% reliable. Many cases go undiagnosed and this is particularly true for CFS, ME and FMS patients, where one of the main drivers of their condition may actually be a systematic infection.
Treatment is often difficult compared with eliminating undesired microbes in the GI tract, as one has to absorb the agents into the bloodstream and treat the outside as well as the inside of our cells, without causing too much toxicity or free radical damage to the cells themselves. The pathogenic microbes may also hide inside biofilms, which offer a defensive wall against antimicrobial agents.
If one has a significant pathogenic infection such as Lyme Disease, where the bacteria are excreting neurotoxins, attempts to retrain a poisoned and malfunctioning immune system are unlikely to be wholly successful, and more progress may be made in this area once the pathogens and biotoxins have been removed. If you do have Lyme Disease, it is unlikely that any of your allergies will ever get significantly better until you eradicate the infection.
A friend of mine, Paul, noted that once he eradicated the Cryptostrongylus pulmoni (roundworm) using Ivermectin (an anhelmintic drug), his hayfever disappeared completely along with most of his other allergies, and he postulates that the presence of such pathogens, particularly roundworm, are probably behind nearly all allergies.
A vicious cycle of free radical and oxidant production may occur in the body, that spirals out of control and inflames the brainstem, causing an abnormal immune response as well as excessive excitotoxicity in the nervous system and an increase in free radical damage and inflammation in the body. This is known as the Nitric Oxide/Peroxynitrite cycle. There are many possible causes, stress and overexcitation are discussed above. The presence of heavy metals is another possible factor, discussed above also. The main treatment for elevated Nitric Oxide/Peroxynitrite is antioxidant therapy and mitochondrial support. When we say antioxidant therapy, we are interested mainly in those antioxidants that are targetted at scavenging Nitric Oxide and Peroxynitrite derivatives. This can be a combination of antioxidant rich (high ORAC value) foods as well as antioxidant supplementation and in large quantities! With as much antioxidant diversity as possible. This is discussed on the Nitric Oxide and Peroxynitrite page. It would seem sensible to combine one's Gluten/Dairy Free Diet (or other variant of an elimination/avoidance diet) and the Anti-Candida Diet with a diet rich in antioxidants (and perhaps noting which foods are nurturing and which foods to avoid from an Oriental Medicine perspective).
Causes and effects of traumatic brain injury (TBI)
Traumatic brain injury can happen when a sudden, violent blow or jolt to the head results in damage to the brain. In the United States and elsewhere, it is a major cause of disability and death.
As the brain collides with the inside of the skull, there may be bruising of the brain, tearing of nerve fibers and bleeding. If the skull fractures, a broken piece of skull may penetrate the brain tissue.
Causes include falls, sports injuries, gunshot wounds, physical aggression, and road traffic accidents.
The Centers for Disease Control and Prevention (CDC) define a TBI as “a disruption in the normal function of the brain that can be caused by a bump, blow, or jolt to the head, or penetrating head injury.”
The severity of symptoms will depend on which part of the brain is affected, whether it is in a specific location or over a widespread area, and the extent of the damage.
In mild cases, temporary confusion and headache may occur. Serious TBI can result in unconsciousness, amnesia, disability, coma, and death or long-term impairment.
The CDC estimate that, in 2013, TBI contributed to the deaths of some 50,000 people. In 2012, 329,290 people aged under 19 years sought emergency treatment for a TBI resulting from a sporting or recreational activity.
Parents, guardians, and teachers should ensure that children are properly supervised and that they wear appropriate safety equipment during sporting and other activities.
A head injury or suspected TBI needs medical attention.
Share on Pinterest A head injury can lead to cognitive impairment.
Signs and symptoms may appear at once, within 24 hours, or they may emerge days or weeks after the injury. Sometimes the symptoms are subtle. A person may notice a problem but not relate it to the injury. Some people will appear to have no symptoms after a TBI, but their condition worsens later.
The effects can be physical and psychological.
The initial physical effects include bruising and swelling. Increased pressure in the brain can cause:
Signs of internal bleeding include bruising behind the ears (battle sign) or around the eyes (raccoon eyes). These can potentially indicate a severe or life-threatening injury. They need immediate medical attention.
Other signs that may indicate severe injury include:
The following signs and symptoms can also indicate a need for urgent attention:
These may appear at once, within hours, or later. A person who has received a TBI but who appears to have no symptoms should be closely monitored for 24 hours, as signs of injury may not be immediate.
Anyone who experiences the above symptoms even days or weeks after a TBI should see a doctor.
Share on Pinterest A child with a TBI may become irritable and listless.
Children will have the same signs and symptoms, but they may be less likely to let others know how they feel.
If an infant has received a blow or jolt to the head and any of the following signs or symptoms occur, call a doctor:
If these signs are noticed, the child should see a doctor.
In sport, the participant should leave out the game and not play again until the doctor gives permission to return, whether or not they lose consciousness. Not every TBI or concussion involves a loss of consciousness.
Repeated head injuries in rapid succession can be particularly harmful to the brain in the long term.
It is important to monitor a person who has had a TBI because their condition can deteriorate rapidly and symptoms that appear mild can become severe.
There is growing evidence that a TBI or repeated TBIs can have long-term effects on health, including an increased risk of dementia and other neurological and neurodegenerative disorders. Football players with high scores on tests for depression have also been found to have a larger number of concussions.
In a mild case of TBI, symptoms normally go away without treatment. However, repeated, mild TBIs can be dangerous or fatal . This is why it is essential to rest and avoid further exposure until a doctor gives the go-ahead.
More severe cases will require hospitalization, possibly with intensive care.
Emergency care aims to stabilize the patient’s condition and prevent any worsening of brain damage.
This will involve ensuring the airway is open, providing ventilation and oxygen, and maintaining blood pressure.
Medications may be used to help control symptoms.
Surgery may be necessary in some cases.
A person who experiences a severe TBI may need rehabilitation.
Depending on the extent and type of their injury, they may need to relearn how to walk, talk, and carry out other everyday tasks.
This may include treatment in a hospital or in a specialized therapy center. It can involve a physical therapist, an occupational therapist, and others, depending on the type of injury.
Tips for recovery
Tips that can aid recovery:
It is important to follow the doctor’s instructions after a TBI, because the impact of a brain injury can be severe, and it is not always immediately apparent.
There are two major types of TBI: open and closed. In open TBI, the skull is broken. In a close TBI, it is not.
Concussion: A direct impact trauma that may or may not involve a loss of consciousness. This is the most common type of TBI. It is often mild, but it can be fatal.
Contusion: When a direct blow causes localized bleeding in the brain, possibly resulting in a blood clot.
Diffuse axonal injury: When tears occur in the brain structure due to shearing by the skull.
Penetrating injury: When a sharp object enters the brain.
TBI is caused by a severe jolt or blow to the head, or a head injury that penetrates and disrupts normal brain function.
The human brain is protected from jolts and bumps by the cerebrospinal fluid around it. The brain floats in this fluid inside the skull.
A violent blow or jolt to the head can push the brain against the inner wall of the skull, which can lead to the tearing of fibers and bleeding in and around the brain.
According to the CDC, the leading causes of TBI in the U.S. in 2013 were:
Other causes include domestic violence and work-related and industrial accidents.
Apart from the immediate dangers, a TBI can have long-term consequences and complications.
Seizures: These may occur during the first week after the injury. TBIs do not appear to increase the risk of developing epilepsy, unless there have been major structural brain injuries.
Infections: Meningitis can occur if there is a rupture in the meninges, the membranes around the brain. A rupture can allow bacteria to get in. If the infection spreads to the nervous system, serious complications can result.
Nerve damage: If the base of the skull is affected, this can impact the nerves of the face, causing paralysis of facial muscles, double vision, problems with eye movement, and a loss of the sense of smell.
Cognitive problems: People with moderate to severe TBI may experience some cognitive problems, including their ability to:
Personality changes: These may occur during recovery and rehabilitation. The patient’s impulse control may be altered, resulting in inappropriate behavior. Personality changes can cause stress and anxiety for family members, friends, and caregivers.
Problems with the senses: These may lead to:
Coma: Patients who enter a coma and remain in a comatose state for a long time may eventually wake up and resume normal life, but some people will wake up with long-term problems and disabilities. Some people do not wake up at all.
Long-term neurological problems: A growing body of evidence has linked TBI with depression, Alzheimer’s, Parkinson’s disease, and other cognitive and neurological conditions.
When to get professional advice
Pharmacy First Scotland: Mouth ulcer treatment from your pharmacy
Mouth ulcers can be painful, which can make it uncomfortable to eat, drink or brush your teeth.
It's usually safe to treat mouth ulcers at home, although your pharmacist may advise that yousee your GP or dentist if:
Mouth ulcers are also a possible symptom of a viral infection that mainly affects young children, called hand, foot and mouth disease. Speak to your GP or call the NHS 24 111service if you're unsure.
An undiagnosed or poorly controlled overactive thyroid can lead to a rare but serious reaction called a thyroid storm. It affects around 1 in 100 people with an overactive thyroid gland.
A thyroid storm is a severe and sudden flare-up of symptoms caused by the metabolism going into overdrive, often due to triggers such as:
Symptoms of a thyroid storm include:
A thyroid storm is a medical emergency. If you think you or someone in your care is experiencing this complication, you need to call 999 for an ambulance.