Why do tendons require over 100 days to make new collagen?

Why do tendons require over 100 days to make new collagen?

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Tendons require over 100 days to make new collagen.

Why does it take so long for tendons to make new collagen?


  • {1} Bass, L. M. T. "Tendinopathy: why the difference between tendinitis and tendinosis matters." International Journal of Therapeutic Massage & Bodywork: Research, Education, & Practice 5.1 (2012): 14-17.

Tendons from kangaroo rats are exceptionally strong and tough

Tendons must be able to withstand the forces generated by muscles and not fail. Accordingly, a previous comparative analysis across species has shown that tendon strength (i.e., failure stress) increases for larger species. In addition, the elastic modulus increases proportionally to the strength, demonstrating that the two properties co-vary. However, some species may need specially adapted tendons to support high performance motor activities, such as sprinting and jumping. Our objective was to determine if the tendons of kangaroo rats (k-rat), small bipedal animals that can jump as high as ten times their hip height, are an exception to the linear relationship between elastic modulus and strength. We measured and compared the material properties of tendons from k-rat ankle extensor muscles to those of similarly sized white rats. The elastic moduli of k-rat and rat tendons were not different, but k-rat tendon failure stresses were much larger than the rat values (nearly 2 times larger), as were toughness (over 2.5 times larger) and ultimate strain (over 1.5 times longer). These results support the hypothesis that the tendons from k-rats are specially adapted for high motor performance, and k-rat tendon could be a novel model for improving tissue engineered tendon replacements.

Why So Long?

Tendons and ligaments go through the same phases of healing as skin or other body tissues, but the process is much slower because of the way they&aposre built. Both structures are made up largely of an organized network of dense, elastic connective tissue, rich in a tough protein called collagen. Living cells called fibroblasts maintain the network.

Fibers of collagen run lengthwise through tendons. They stretch to take the load when your horse puts his weight on the leg and spring back like rubber bands when the weight comes off. But if he overloads the leg (perhaps by just putting a foot down wrong on uneven ground), the fibers can tear. Damage can be instant, or it can build up over time as repetitive loads outstrip the ability of the fibroblasts to keep up with repairs. There are relatively few of these cells compared to the amount of collagen in a tendon or ligament, and that&aposs one reason why these injuries heal slowly. In addition, tendons and ligaments have poor blood supplies.

A severe tear will take longer to heal than a mild one, and a 20-year-old horse may heal more slowly than a 5-year-old. Typically ligaments heal a bit faster than tendons but you&aposre still looking at nine to 12 months for all but the mildest of these injuries. And these injuries often heal poorly instead of long, strong collagen fibers, you get a disorganized tangle of scar tissue that&aposs less elastic and more prone to reinjury.

To get the best outcome, you&aposll need to follow a management and rehabilitation program that&aposs carefully matched to the progress of healing. Your veterinarian will help you set up a program that fits your horse&aposs injury. Diagnostic ultrasound scans, which many vets can do at intervals with portable equipment, can take much of the guesswork out of managing recovery and improve your odds of success.

Initially, ultrasound will show the extent of the injury. The machine beams ultrasonic waves into the leg and captures their echoes as they bounce off tissues. A tear in a tendon may show up as a gap in what should be a uniform pattern or as an area where echoes are less intense. Repeat exams can show how healing is progressing, letting you adjust your horse&aposs program. Your vet may want to do the exams at 30-, 60- or 90-day intervals, depending on the severity of the injury, the stage of rehabilitation and the total rest time that&aposs needed for healing.

How to Protect Your Collagen When You Have Lyme, Fibromyalgia, or Chronic Fatigue

by Dr. Bill Rawls
Updated 11/2/18

Collagen is so much bigger and more important than the skin anti-ager it’s best known to be: It plays a role in supporting your body head to toe, organs and all. And if you have a chronic illness like chronic Lyme disease, fibromyalgia, or chronic fatigue syndrome (CFS), there’s a good chance you’re losing your collagen at an accelerated rate. Find out why, and smart ways to both rebuild the collagen you’ve lost and protect what you have, below.

What is Collagen?

Before you worry about saving your collagen, it helps to understand exactly what it is and why it’s so worth your effort.

For starters, it’s the most abundant protein in your body. It’s what literally holds you together. Three strands of protein twist together to make a collagen fiber. And collagen fibers come together to form the tendons and ligaments that provide support for your entire skeleton.

Cartilage in joints is made of collagen. Collagen is also present in muscles and bones for added support. Without collagen, you would be a pile of bones on the floor. Collagen also provides support to skin, ligaments, blood vessels, heart muscle and valves, gums, eyes, intestines, and really anything in the body that needs to be supported.

In other words, collagen is really important. But not just to you: Many microbes that inhabit your body also use it as a nutrient resource. And that’s where things can get complicated.

Why Microbes Are After Your Collagen

Whether or not you’re struggling with a microbe-related chronic illness like Lyme or fibromyalgia, know that you are already in competition with microbes in your microbiome over your collagen.

We all have a microbiome, a vast ecological community of microbes that exists in our bodies. The microbiome was once thought to be isolated to your gut and on skin, but more recent research suggests that it’s quite a bit more complex.

Back in 2015, a study in PLOS One found that healthy mice have distinct populations of microbes as permanent residents in their muscle, liver, heart, and brain tissue. The researchers surmised that this was true of all creatures, and since then, human studies have confirmed that microbe populations exist in the brain tissue, joints, and other organs in healthy people. The evidence also strongly suggests that even healthy individuals harbor low concentrations of microbes in all tissues.

Some of these microbes have the ability to degrade collagen by producing enzymes for breaking down the protein. Many of them are potential pathogens that can exist within a person’s mouth, gut, and skin. Microbes that are typically associated with chronic illness, including borrelia (the prime suspect in Lyme), mycoplasma, and chlamydia, among many others, also have the ability to break down collagen.

In a scientific paper published in Infection and Immunity in 1996, researchers speculated why microbes might need to break down collagen, and proposed the following reasons:

  • To release amino acids for their growth
  • To break down natural tissue barriers to allow them to spread into deeper tissues
  • To create a protective environment in deeper tissues for growth of anaerobic microbes (bacteria that don’t use oxygen — examples include borrelia and mycoplasma)

In healthy people, collagen breakdown by microbes is probably occurring at a very low level. Their immune systems are able to keep microbes in check such that significant damage doesn’t accumulate, and they’re able to constantly rebuild new collagen.

Net loss of collagen due to microbes doesn’t occur unless immune system functions are compromised and microbes are allowed to flourish, in which case things can get out of hand quickly. Chronic Lyme disease is possibly the best example of this.

The Link Between Chronic Illness and Loss of Collagen

Borrelia is possibly the most well known microbe with the ability to break down collagen. Not surprisingly, many of the symptoms of chronic Lyme disease occur at locations of high-density collagen: joints, ligaments, skin, eyes, gums, heart, and brain tissue. Inflammation and breakdown of collagen by microbes are likely the driving forces behind symptoms at these locations.

But borrelia isn’t the only microbe causing problems a long list of possible coinfections are also typically present. Of the collagen-degrading microbes on the list, mycoplasma species are the most well studied.

Though mycoplasma commonly occurs as a Lyme coinfection, it has also been associated with a variety of other chronic illnesses, including rheumatoid arthritis and multiple sclerosis. And it’s been linked with damaged heart valves and arthritic joints (along with other microbes, including chlamydia and borrelia), both of which are associated with loss of collagen.

Interest in mycoplasma as a possible cause of rheumatoid arthritis (RA) dates back to the 1970s. In a flurry of research at the time, mycoplasma was found to be present in a high percentage of RA sufferers. However, interest in the connection seemed to die off when antibiotic therapy seemed effective in these patients. It is now known that mycoplasma is extremely resistant to antibiotic therapy.

More recently, interest in the mycoplasma-arthritis link seems to be rekindling. In 2000, a group of researchers published their findings in the Journal of Clinical Microbiology after examining samples of synovial fluid from the knees of 44 arthritis patients. They were able to detect Mycoplasma fermentans in 88% of cases of rheumatoid arthritis and other forms of arthritis, including ankylosing spondylitis, juvenile chronic arthritis, gout, and psoriatic arthritis (arthritis associated with psoriasis).

Later, in a 2006 study, the same lead researcher found Mycoplasma pneumoniae, a common cause of childhood bronchitis and chronic low grade pneumonia, in 79% of rheumatoid arthritis patients enrolled in the study, 80% of osteoarthritis patients, and 100% of those with other types of chronic arthritis.

Mycoplasma is a remarkably common microbe in human populations, with 40-60% of healthy people testing positive for some species of it. Though different species of mycoplasma are commonly spread by respiratory and genital infections, once the microbes are in the body, they can show up most anywhere. Sites of collagen are common final residences of the microbe.

When you add mycoplasma to the list of possible microbes that degrade collagen, and consider that symptoms of many chronic illnesses share collagen-located symptoms, the possibility of microbes being the driving force behind many types of chronic misery is highly likely.

The bottom line is that everyone harbors microbes with the potential to break down collagen — they’re just waiting for an opportunity. Some microbes are more threatening than others. Whether you will end up being ill or suffering from symptoms associated with collagen degradation depends on three factors:

  • Genetics: Some people are more inherently susceptible to rheumatoid illnesses than others.
  • Microbes: The type of microbes you pick up during your lifetime and harbor in your tissues can increase your risk.
  • Immune system function: How factors come together during your lifetime to disrupt your immune system impact the strength of your defenses against collagen-degrading microbes.

While you can’t change your DNA, there’s a lot you can do to keep stealth microbes under containment and your immune system running efficiently so you can prevent collagen loss and rebuild healthy levels.

How to Protect Your Collagen

Whether you’re struggling with a chronic illness associated with symptoms of collagen loss, or having aging-related mild arthritis and skin changes, you want to protect the collagen in your body. There are four specific categories of actions you can take.

1. Suppress Collagen-Degrading Microbes with Herbal Therapy

Though mycoplasma and borrelia were my primary examples above, there are many microbes known to break down collagen — which means you can’t target just one. What’s more, most all of these microbes fit into the category of stealth microbes, which live inside cells (intracellular), grow very slowly, and are widely distributed in low concentrations throughout tissues in the body. Most notably, they are all notoriously resistant to conventional antibiotic therapy.

A better approach is taking certain herbs with known antimicrobial properties, which work differently than conventional antibiotics. Instead of one potent chemical, herbs contain hundreds of chemical compounds known to suppress microbes — they hit the microbes from a variety of different directions at once.

Many of the chemical compounds found in herbs are fat-soluble, and therefore can penetrate cell membranes to affect stealth microbes where they live. Antimicrobial herbs typically don’t disrupt normal flora and are extremely well tolerated, so they can be used for months or even years without concern. That’s key, because long-term suppression appears to be the only effective solution for these microbes.

When multiple antimicrobial herbs are combined, the benefits are synergistic. They also support optimal immune functions and provide protective antioxidants. Some of the best antimicrobial herbs include andrographis, cat’s claw, Japanese knotweed, sarsaparilla, garlic, berberine.

2. Support Your Immune System

Your immune system’s most important job is managing the wide spectrum of microbes that inhabit your body. A healthy immune system is essential for staying well and protecting collagen. However, the modern world is saturated with factors that disrupt immune system functions — especially our highly processed diet, exposure to high concentrations of man-made environmental toxins, chronic stress, and tendency to lead a sedentary life.

The most obvious solution is to take steps to counter the modern-life system-disruptors that ding your immune system every day. That means doing things like eating a healthful diet full of fresh, whole foods (more on that below) filtering your water opting for organic foods and natural, non-toxic cleansers whenever possible and making time each day for yourself to find a little stress relief and move your body.

Herbal therapy is also an excellent choice for supporting optimal immune system functions. Antimicrobial herbs do some of that, but herbal adaptogens do even more. Not only do adaptogens help reduce damaging inflammation, but they also enhance the immune system’s ability to do its job by balancing hormones and increasing your resistance to stress. Common herbal adaptogens with immune-balancing properties include reishi, cordyceps, ashwagandha, rhodiola, and eleuthero.

3. Support Collagen Turnover

Collagen in your body is constantly being degraded and being rebuilt. A healthful diet is key for providing new raw materials for building new collagen. At the top of that list are kale and other deep-green leafy vegetables, cucumbers, salmon, sardines, eggs, celery, and olives.

Bone broth is the latest health fad for supporting collagen, and it’s one I can get behind. That’s because bone broth provides all the necessary ingredients for rebuilding cartilage, which is made up of collagen. You can make your own (many recipes are available on the web), or buy it in most grocery stores.

Eating gelatin is an easy way to add an extra supply of collagen to your diet. You can also get collagen in supplement form the recommended dose is about 6000 mg daily of collagen powder mixed in a smoothie or shake.

Another supplement to consider is silicon, which is a necessary component of collagen generation, plus it’s important for repairing myelin nerve sheaths. Natural silicon can be obtained from the herb, horsetail, or as stabilized orthosilicic acid, a liquid that’s dosed at about 20 drops a day (this also can be added to smoothies).

Out of all supplements for supporting collagen and joint function, glucosamine has the most scientific evidence to back it up. Glucosamine is a precursor for proteoglycans, the chemicals necessary for smooth and slick joint linings. It also stimulates synthesis of collagen. With age, normal glucosamine synthesis decreases, which may be a contributing factor to arthritis. The suggested dose of glucosamine is 500-750 mg, twice daily.

4. Minimize Other Collagen Disruptors

Microbes aren’t the only forces that degrade collagen in the body. There are variety of additional factors that are continually wearing it down. Check out five more top offenders below, plus simple advice for navigating around them.

  • Sugar and starch. Glucose and fructose — sugars from processed food products, table sugar, high fructose corn syrup, and concentrated fruit sugar — are notorious collagen crunchers. Sugar and starch (another type of carbohydrate) bind to collagen in a process called glycation and target it for destruction. Plus the processed foods they’re found in generate inflammation in the body. Try to minimize the amount of added sugars you consume, and reach for whole, fresh foods over packaged stuff with processed ingredients whenever possible.
  • Poor sleep. Your body repairs damaged collagen while you sleep, so you need at least 8 hours of quality sleep every night for optimal health. The secret of a good night’s sleep is finding moments of calm throughout the day and allowing plenty of time for adequate sleep at night — which may mean tacking on an extra hour to allow for the time it takes you to drift off.
  • Toxins. Toxins of any variety damage collagen, but smoking saturates the body with them. If you smoke, it’s time to quit. And look for other ways to prevent toxins from entering your body by ingesting them, breathing them in, or through skin absorption.
  • Physical stress. Extreme physical activity causes excessive wear and tear on joints and ligaments. Look for low-impact exercise that’s easier on your body. For instance, the gentle stretching of yoga helps maintain healthy ligaments, good posture, and skeletal support, and it’s also been found to reduce risk of osteoporosis.
  • Sunlight. UV, infrared, and visible light from the sun are potent collagen crunchers in skin. Sunblock protects against UV, but not infrared and visible light. You also gain significant protection from specific types of antioxidants that build up in skin layers and also the retina of the eye. Lutein and zeaxanthin (carrots, yellow vegetables, kale) and anthocyanins (blueberries and other blue produce) should be dietary staples. These antioxidants also protect collagen in blood vessels and other parts of the body.

Everyone should be thinking about protecting and rebuilding their collagen, but especially those who are staring down a chronic illness. The good news is, the tactics that work best to help support healthy collagen levels are the same ones that are most effective for overcoming Lyme, fibromyalgia, and CFS. Follow the tips outlined above, and you’ll be doing double duty for your health and well-being.

Dr. Rawls is a physician who overcame Lyme disease through natural herbal therapy. You can learn more about Lyme disease in Dr. Rawls’ new best selling book, Unlocking Lyme.
You can also learn about Dr. Rawls’ personal journey in overcoming Lyme disease and fibromyalgia in his popular blog post, My Chronic Lyme Journey.

Type 1 Collagen Benefits and Where to Find It

Type 1 collagen is the most abundant in the human body. You can find type 1 collagen in your eyes, skin, tendons, bone, and teeth. Even though it’s great for rebuilding your muscles, eyes, bones, and spine, it’s famous for minimizing fine lines and wrinkles and improving skin elasticity and hydration. It’s also good for strengthening your nails and helping you grow stronger, thicker hair.

There’s a lot of overlap when it comes to the benefits of type 1 and 3 collagen so you’ll often find products that contain both. However, Natural Force Marine Collagen, which is sourced from wild-caught cod, is particularly rich in type 1 collagen making it the best choice for those specifically seeking the benefits of type 1.

Types 1 and 3 are best for healing the gut lining, and type 1 collagen from marine sources is especially good for healing the tight junctions of your intestinal tract.

The best sources for types 1 collagen:

  • Marine Collagen (for high concentrations of type 1 collagen)
  • Organic Bone Broth Protein Powder (rich in types 1, 2, and 3)
  • Bovine Collagen (rich in types 1 and 3)

There are 11 exercise types that help increase tendon strength and elasticity:

  1. Eccentric exercises – the negative movement
  2. Partial reps
  3. Plyometrics – explosive movement
  4. Explosive isometrics – quick forceful movements against an immoveable force
  5. Volume-increasing exercises
  6. Intensity training
  7. Stretching – using full range of motion
  8. Seeking mild discomfort while avoiding pain and injury
  9. Daily connective tissue training
  10. Avoiding rushing
  11. Massage and myofascial bodywork

1. Eccentric Exercises – training “the negative”

Many studies indicate that eccentric exercises (lowering the weight) are an effective way to treat tendon injuries. In one trial, ex-runners in their early 40s with chronic Achilles’ tendonitis were split into two groups. One group had conventional therapy (NSAIDs, rest, physical therapy, orthotics), the other did eccentric exercises. Exercisers would do a calf raise (concentric) on the uninjured foot and slowly lower themselves on the injured foot (eccentric heel drop) for 3 sets of 15 reps, twice a day, every day, for 12 weeks. Once this got easy and pain-free, they were told to increase the resistance with weighted backpacks. After 12 weeks, all the ex-runners in the exercise group were able to resume running, while those in the conventional group had a 0% success rate and eventually needed surgery.

If heel dips can heal Achilles’ tendinopathy and single-leg decline eccentric squats can heal patellar tendinopathy, I’d wager that eccentric movements can strengthen already healthy tendons. Any tendon should respond to eccentrics. Downhill walking, slowly lowering oneself to the bottom pushup position, eccentric bicep or wrist curls anything that places a load on the muscle-tendon complex while lengthening it should improve the involved tendons.

2. Partial reps

Early 20th century strongman George Jowett developed a program for “strengthening the sinews” that involved partial reps of extremely heavy weights. He focused on the final 4-6 inches before lockout of the primary exercises, like bench press, overhead press, squat, and deadlift.

3. Plyometrics

Explosive movements utilizing the recoil response of the tendons can improve that response. In one study, 14 weeks of plyometrics (squat jumps, drop jumps, countermovement jumps, single and double-leg hedge jumps) reduced tendon hysteresis. The trained group had better, more efficient tendon recoil responses than the control group. Tendons didn’t get any bigger or longer they just got more efficient at transmitting elastic energy. A previous 8-week plyometric study was unable to produce any changes in tendon function or hysteresis, so you need to give it adequate time to adapt.

4. Explosive isometrics

Explosive isometric training involves trying to perform an explosive movement against an immoveable force, like pushing a car with the parking break on, trying to throw a kick with your leg restrained by a belt, or placing your fist against the wall and trying to “punch” forward. In one study, explosive isometric calf training 2-3 times a week for 6 weeks was just as good as plyometric calf training at increasing calf tendon stiffness and jump height while being a lot safer and imposing less impact to the joints.

5. Volume-increasing exercises

Volume clearly matters. Just look at the beefy fingers of free climber Alex Honnold, who relies on them every day to support his bodyweight. Those aren’t big finger muscles. They’re thick cords of connective tissue. Pic not enough? In performance climbers with at least 15 years experience, the finger joints and tendons are 62-76% thicker than those of non-climbers. And a study showed that the extremely common crimp hold—where all five finger tips are used to hold a ledge—exerts incredible forces on the finger connective tissues, spurring adaptation. So if you’re up to the challenge, rock climbing (indoor or outdoor) is a great way to increase tendon volume.

6. Intensity training

You have to actually stress the tendons. We see this in the eccentric decline squat study mentioned earlier, where decline squats (which place more stress on the patellar tendon) were more effective than flat squats (which place less stress on the patellar tendon) for fixing patellar tendinitis. In another study, women were placed on a controlled bodyweight squat program. They got stronger, their musculature improved, and their tendons grew more elastic, but they failed to improve tendon stiffness, increase tendon elastic storage capacity, or stem the age-related decline in tendon hysteresis. The resistance used and speed employed simply weren’t high enough to really target the connective tissue. A recent study confirms that to induce adaptive changes in tendon, you must apply stress that exceeds the habitual value of daily activities. So, while walking, gardening, and general puttering about is great for you, it’s probably not enough to coax an adaptive response out of your ailing tendons. You need to increase the magnitude of the applied stress through tinkering with volume, speed, resistance, range of motion, and the proportion of eccentric vs. concentric movement.

7. Stretching – full range of motion

Deeper, longer stretches are probably best. Some examples:

  • Front squat. An ass-to-grass front squat, where the hip crease drops below the knees, will stretch/stress the patellar tendon that attaches the quad to the shin bone to a greater extent than squatting to just above parallel.
  • Pectoral stretch. You can use a door frame to take your pec stretch a little further, which will work the connective tissue in your shoulders.
  • Calf stretch. Instead of stretching your calves in a basic lunge, you can use stairs or a curb to lift your toes closer to your shins, targeting the achilles tendon.

8. Avoid pain, seek mild discomfort

Tendon discomfort is okay. Stress isn’t comfortable. Tendon pain is not and should be avoided. You want just enough discomfort to provoke a training stimulus, but not outright pain.

9. Daily practice to strengthen tendons

How to train strengthen your tendons and ligaments may not always be top of mind, but it’s best to think about — and train — your connective tissue every day. That could range from random sets of eccentric heel drops and static squat holds done throughout the day. I like Dan John’s “Easy Strength” program, where you basically pick a few movements to do each day—every day—with a fairly manageable weight. Front squat, Romanian deadlift, and pullups, for example. 2 sets of 5 reps each day for each exercise. Only add weight when it feels “too easy.”

10. Don’t rush take it easy

Pick a load and stick to it until it gets easy. In a pair of incredible appearances on Robb Wolf’s Paleo Solution Podcast, Christopher Sommer of Gymnastic Bodies explains how he puts together a tendon-centric program for an athlete. He has them stick with the same weight for 8-12 weeks. The first few weeks are hard. The weight feels heavy. At 4 weeks, it’s a lot easier but still a challenge. At 8 weeks, you start feeling like it’s too easy. And that’s where the tendon-building magic happens. By 12 weeks, what felt tough when you started is now “baby weight.” Your muscles are stronger and your tendons have had enough time to build collagen density. You’re able to manhandle the weight without a problem.

Like I just mentioned above, another example is Dan John’s “Easy Strength,” which has you lift almost every day using light-moderate loads, only adding weight when 2 sets of 5 reps becomes really easy. You won’t see the rapid progression of Starting Strength, but it’ll also be easier on your body, prepare your tendons for higher loads, and remove the need for a gallon of milk a day.

11. Massage and myofascial bodywork

Massages can increase blood flow to the otherwise avascular tendons. Self myofascial release using foam rollers or lacrosse balls (or even the good ol’ elbow) is worth doing, too. A qualified massage therapist knows exactly how to strengthen tendons, manipulating them in just the right way.

12th way to strengthen tendons and ligaments: collagen

Collagen isn’t a movement. It is a nutrient. Collagen is in every cell throughout the human body, and it is highly concentrated in your connective tissue. Studies show you need 10 grams of glycine, a component of collagen, every day for collagen maintenance, more if you are recovering from an injury. It’s not easy to get 10 grams of glycine unless you are eating tough cuts of meat or offal every single day. For the rest of us, collagen peptide supplements fill in the gaps. Hydrolyzed collagen peptides in powder form are easy to use – you can get collagen powders that are flavored or unflavored, and they mix into virtually any liquid. You can read more about collagen here.

What is collagen, and why do people use it?

Collagen is the most abundant protein in the human body, found in the bones, muscles, skin, and tendons.

It is the substance that holds the body together. Collagen forms a scaffold to provide strength and structure.

Endogenous collagen is natural collagen, synthesized by the body. Exogenous collagen is synthetic. It comes from an outside source, such as supplements.

Endogenous collagen has a number of important functions. Breakdown and depletion is linked to a number of health problems.

Exogenous collagen is used for medical and cosmetic purposes, including the repair of body tissues.

Share on Pinterest Collagen has a sturdy structure. Gram-for-gram, some types are stronger than steel.

Collagen is a hard, insoluble, and fibrous protein that makes up one-third of the protein in the human body.

In most collagens, the molecules are packed together to form long, thin fibrils.

These act as supporting structures and anchor cells to each other. They give the skin strength and elasticity.

There are at least 16 different types of collagen, but 80 to 90 percent of them belong to types 1, 2, and 3. These different types have different structures and functions.

The collagens in the human body are strong and flexible.

Type 1 collagen fibrils are particularly capable of being stretched. Gram-for-gram, they are stronger than steel.

Collagen is secreted by various cells, but mainly by connective tissue cells.

It is found in the extracellular matrix. This is an intricate network of macromolecules that determines the physical properties of body tissues. A macromolecule is a molecule containing a large number of atoms.

In the dermis, or the middle layer of skin, collagen helps form a fibrous network of cells called fibroblasts, upon which new cells can grow. It also plays a role in replacing and restoring dead skin cells.

Some collagens act as protective coverings for delicate organs in the body, such as the kidneys.

With age, the body produces less collagen. The structural integrity of the skin declines. Wrinkles form, and joint cartilage weakens.

Women experience a dramatic reduction in collagen synthesis after menopause.

By the age of 60 years, a considerable decline in collagen production is normal.

Collagen is resorbable. This means it can be broken down, converted, and absorbed back into the body. It can also be formed into compacted solids or lattice-like gels.

Its diverse range of functions and the fact that it is naturally occurring make it clinically versatile and suitable for various medical purposes.

Collagen for medical use can originate from humans, cows, pigs, or sheep.

Skin fillers

Collagen injections can improve the contours of the skin and fill out depressions.

Fillers that contain collagen can be used cosmetically to remove lines and wrinkles from the face. It can also improve scars, as long as these do not have a sharp edge.

These fillers are sourced from humans and cows. Skin tests should be done before using collagen from cows, to avoid aggravating any allergies.

Collagen can fill relatively superficial volumes. More extensive gaps are usually filled with substances such as fat, silicone, or implants.

Wound dressing

Collagen can help heal wounds by attracting new skin cells to the wound site. It promotes healing and provides a platform for new tissue growth.

Collagen dressings can help heal:

  • chronic wounds that do not respond to other treatment
  • wounds that expel bodily fluids such as urine or sweat
  • granulating wounds, on which different tissue grows
  • necrotic or rotting wounds
  • partial and full-thickness wounds
  • second-degree burns
  • sites of skin donation and skin grafts

Collagen dressings are not recommended for third-degree burns, wounds covered in dry eschar, or for patients who may be sensitive to products sourced from cows.

Guided tissue regeneration

Collagen-based membranes have been used in periodontal and implant therapy to promote the growth of specific types of cell.

In oral surgery, collagen barriers can prevent fast-growing cells around the gum from migrating to a wound in a tooth. This preserves a space where tooth cells have the chance to regenerate.

Collagen-based membranes can aid healing in these cases and they are resorbable, so this barrier does not need to be surgically removed after the main operation.

Vascular prosthetics

Collagen tissue grafts from donors have been used in peripheral nerve regeneration, in vascular prostheses, and in arterial reconstruction.

While collagen prostheses are compatible with the human body, some have been found to be thrombogenic, or likely to cause coagulation of the blood.

Treatment of osteoarthritis

Collagen supplements or formulations may help treat osteoarthritis.

A 2006 review found that supplements containing collagen helped decrease painful symptoms and improving joint function in people with osteoarthritis.

As the supplement was absorbed, collagen accumulated in the cartilage, and this helped to rebuild the extracellular matrix.

Not all studies have supported these findings, however.

Skin revitalization

Many products containing collagen, including creams and powders, claim to revitalize the skin by increasing collagen levels within the body.

This is unlikely, however, as collagen molecules are too large to be absorbed through the skin.

Any benefit is probably due to the moisturizing effects of these products. They do not directly increase collagen.

Such treatments are also not classified as drugs, so any claims regarding their efficacy do not need to be scientifically proven. Caution is advised when using these products.

Laser therapy can help treat stretch marks, as it can stimulate the growth of collagen, elastin, and melanin.

A healthful diet can help the body produce collagen.

Nutrients that may support collagen formation include:

  • Proline: In egg whites, meat, cheese, soy, and cabbage.
  • Anthocyanidins: In blackberries, blueberries, cherries, and raspberries. C: In oranges, strawberries, peppers, and broccoli.
  • Copper: In shellfish, nuts, red meat, and some drinking water.
  • Vitamin A: Occurring in animal-derived foods and in plant foods as beta-carotene.

What damages collagen?

Some factors can deplete the levels of collagen within the body. Avoiding them could keep the skin healthy for longer.

High sugar consumption: A high-sugar diet increases the rate of glycation, a process where blood sugars attach to proteins to form new molecules called advanced glycation end products (AGEs).

AGEs damage nearby proteins and can make collagen dry, brittle, and weak.

Smoking: Many chemicals present in tobacco smoke damage both collagen and elastin in the skin.

Nicotine also narrows the blood vessels in the outer layers of the skin. This compromises skin health by reducing the delivery of nutrients and oxygen to the skin.

Sunlight: Ultraviolet rays in sunlight cause collagen to break down more rapidly, damaging collagen fibers and causing abnormal elastin to build up.

The UV rays in sunlight damage the collagen in the dermis, and the skin rebuilds incorrectly, forming wrinkles.

Autoimmune disorders: Some autoimmune disorders cause antibodies to target collagen.

Genetic changes can affect the extracellular matrix. The collagen that is produced can be lower, or it may be dysfunctional, mutated collagen.

The aging process causes collagen levels to deplete naturally over time. There is no way to prevent this.

Avoiding tobacco and excess sun exposure and following a healthful dietary and exercise regime can help reduce visible aging and protect collagen, keeping the skin, bones, muscles, and joints healthy for longer.

Important Vitamins and Minerals

Several vitamins and minerals are related to ligament and tendon health. These vitamins and minerals also impact healing.

  • Vitamin A. According to a 2016 study in the American College of Sports Medicine Health and Fitness Journal, vitamin A can help enhance collagen development. Collagen is important for the formation and function of tendons, ligaments, cartilage and bone. Vitamin A can be found in many foods, including carrots, mangoes, squash and sweet potatoes.
  • Vitamin C. According to a 2016 study in the American Journal of Clinical Nutrition, vitamin C can increase collagen production to help ligament and tendon function. Vitamin C is most commonly found in citrus fruits. Many foods have both vitamin A and vitamin C. Leafy green vegetables like kale and spinach have both, along with other beneficial vitamins and minerals.
  • Vitamin D.Vitamin deficiency slows healing of ligaments and tendons. It's important to get enough vitamin D, especially if you're physically active or suspect an injury.
  • Magnesium. Magnesium is an essential nutrient for good tissue health. Magnesium and tendon repair have been correlated for many years. Magnesium-deficient diets have been shown to increase degeneration of tendons and other connective tissues.
  • Trace minerals, including copper, manganese and zinc. The trace minerals play a role in collagen metabolism. Lack of these trace minerals results in poorer collagen synthesis and can negatively impact ligament and tendon health.

Anti-Aging Part One: The Importance of Collagen

Every woman over 25 (and some men) are constantly reading about collagen pertaining to beauty products and anti-aging. But what does it all really mean in your personal everyday quest in finding the fountain of youth?

First, let's examine what collagen is. Collagen is a protein produced in the human body. It is in the bones, tendons, muscles and skin. It is also found in the cornea of the eyes, blood vessels, gut lining, teeth, and nails. The word collagen is derived from the Greek word “kolla” meaning glue. So basically collagen is the “glue” that holds the entire body together. The body produces collagen naturally and it is in abundance when young, but unfortunately production starts to decline at about age 25, and continues. It decreases even more in women after menopause. Collagen also decreases with other factors such as smoking, sugar and ultraviolet rays. This decrease leads to wrinkles and sagging skin. There is no way to prevent collagen decreases in the body.

Don’t panic you are NOT doomed! While there is no way to completely stop aging, there are ways to do so more gracefully. You can help your body maintain and build collagen, once you have some of the basic information. There is a great deal of misleading and debatable information when it comes to collagen. One fact that most seem to agree on is that collagen skincare products do NOT add collagen to the skin. They are basically “hope in a jar”. Collagen molecules are simply too large to penetrate the skin. They can help moisturize your skin but they will not help build or replace collagen. The active ingredients will just sit on top of your skin. If the active ingredient is collagen it is always from an animal source. Most of the creams and dietary supplements on the market come from either cowhide or chicken bones. Since collagen is a form of protein, It also can not be digested whole. It has to be broken down by the stomach just like every other protein we eat. This basically means you can not eat collagen to build collagen.

It is very important to consume adequate amounts of protein so your body has the amino acids it needs to produce collagen. It’s also very important to consume a diet rich in antioxidants (vitamins E, C and beta-carotene) B vitamins and minerals such as magnesium and zinc also play an important role. Foods like blueberries, dark leafy greens, mango, eggs, are also great collagen boosters. You should also consider switching your current oil to avocado oil. A 2006 study published in the Journal of Rheumatology found that avocado oil “significantly increased type II collagen”.

If you can not always eat a collagen producing diet supplements are another alternative. The best ones would be a plant-based supplement that helps the body in production. Garden of Life recently launched MyKind Organic Plant Based Collagen Builder. Not only is this supplement organic but the ingredients are non-GMO and, suitable for both vegans and vegetarians. It basically contains the vitamins and minerals needed to help build collagen. Take this with a good protein source and your hair, skin, and nails will love you!

There are other ways that collagen production can be stimulated in the skin (specifically the face) by visiting a plastic surgeon or medical spa. Fillers such as Radiesse and Sculptra both make claims to increase collagen production in the skin. There is also Microneedling which is a technique to increase the body's collagen and elastin. The procedure uses micro needles (hence the name) and is minimally invasive. A trained professional makes thousands of minuscule needle puncture marks on the skin stimulating your body to make more collagen in that area.

Next week, we will ask an expert to give his expertise about collagen production through alternative measures. Dr. Ramtin Kassir is a prestigious New York City board certified plastic surgeon. According to ABC News Dr. Kassir is one of the top plastic surgeons in New York City. He treats patients that are trying to look younger and increase collagen production. There are so many procedures on the market, that it is best to make an informed decision (so ask an expert). Next week in part 2 of this series, we will get expert advice from Dr. Ramtin Kassir. Until then, I wish you lots of love and collagen.

Common Tendinopathies


Rotator Cuff Tendinopathy . Shoulder pain is one of the top three causes of musculoskeletal symptoms, with an estimated incidence of 19 cases per 1,000 person years.55 , 56 Rotator cuff pathology is the most common cause. The rotator cuff comprises four muscles: the supraspinatus, infraspinatus, teres minor, and subscapularis. Its primary function is to maintain the position of the humeral head during glenohumeral movement. The supraspinatus is the most likely tendon to show signs of injury.57 , 58 The etiology of rotator cuff tears (partial or complete) is a complicated interaction of intrinsic, extrinsic, and environmental factors. A chronic degenerative injury can lead to significant pain, disability, or a complete tear.4 , 57

Patients with rotator cuff tendinopathy typically report weakness, stiffness, constant pain that is exacerbated with certain movements, and pain that makes it difficult to sleep on the affected side. The mainstay of treatment is rehabilitative exercise focusing on scapular stabilization and biomechanics to decrease subacromial impingement.59 Eccentric exercise has not been proven superior to conventional exercise in treating rotator cuff tendinopathy, and home-based programs are as effective as clinic-based programs.55 , 60 Subacromial corticosteroid injections are commonly used to provide short-term pain relief, which can be useful when initiating physical therapy.61 If the patient remains symptomatic after six months of therapy, other treatments such as extracorporeal shock wave therapy, platelet-rich plasma injections, or dextrose prolotherapy can be considered. If these treatments are ineffective, surgery may be a consideration.33 , 62

Biceps Tendinopathy . The long head of the biceps (LHB) is the major source of pain in the anterior aspect of the shoulder. The LHB tendon sheath is a continuum of the glenohumeral joint and is closely associated with rotator cuff pathology it is estimated that chronic LHB tendinopathy is the primary injury in only 5% of patients with shoulder pain.63 , 64 Repetitive traction, friction, and shear forces in the narrow bicipital groove from constant glenohumeral rotation lead to the insidious and progressive pain that can occur with repetitive overhead movements. Reproduction of pain with direct palpation of the tendon in the bicipital groove is the most common physical examination finding. In some patients, palpation is painful even in nonpathologic tendons, so it is important to also palpate the unaffected, contralateral side. Several other tests have been developed to diagnose LHB tendinopathy, but none has a high predictive value, whether used alone or in specific combinations.64 , 65

Therapeutic injections may be helpful in establishing the diagnosis of LHB tendinopathy vs. rotator cuff pathology. Persistent pain of the LHB tendon after a subacromial injection or improvement in pain after an injection directly into the bicipital groove can confirm LHB tendinopathy. Because of the high correlation with rotator cuff pathology, most rehabilitative exercises for LHB tendinopathy also focus on addressing problems with the rotator cuff. Primary LHB tendon rehabilitation focuses on range of motion, muscle balance, and dynamic stability of the shoulder.63 , 65

Epicondylitis . Epicondylitis is a misnomer there is no inflammation at the humeral epicondyles. These conditions are tendinopathies of the common extensor and flexor tendons of the forearm. Medial epicondylitis is not as common as lateral epicondylitis, but the treatments are generally the same.66 Lateral epicondylitis, or tendinopathy of the extensor carpi radialis brevis, affects 1% to 3% of Americans each year.11 , 31 Patients report pain with wrist extension and reduced grip strength, and they have reproducible pain with palpation approximately 1 cm distal to the lateral epicondyle. Although it is also called tennis elbow, lateral epicondylitis is more commonly associated with occupational overuse injuries than athletic activities.11

Physical therapy with an emphasis on eccentric exercises has short- and long-term benefit for epicondylitis compared with no treatment or corticosteroid injections.31 , 67 Bracing can treat pain and does not negatively affect strength.21 A comparison of cock-up wrist braces vs. counterforce straps showed that wrist braces may have an advantage because of complete immobilization, but the strap is more practical for daily use.22 – 24 If conservative treatment is ineffective, corticosteroid injections, deep friction massage, dry needling, and platelet-rich plasma injections are appropriate. Referral for surgery is appropriate if these treatments are ineffective.27 , 68 , 69


Greater Trochanteric Pain Syndrome . Greater trochanteric pain syndrome (GTPS) is lateral hip pain with tenderness over the greater trochanter, and has been attributed to trochanteric bursitis.70 GTPS is an inaccurate diagnosis because the primary etiology of the pain is a degenerative tendinopathy of the gluteus medius or gluteus minimus tendons with some secondary bursal distention.71 , 72 GTPS is a common condition, affecting 1.8 to 5.6 per 1,000 adults each year with a 4: 1 female-to-male prevalence.73 Risk factors include being 40 to 60 years of age or obese, and having low back pain, knee or hip osteoarthritis, a sedentary lifestyle, or poor running biomechanics with increased hip adduction.71 , 74 Patients with GTPS report insidious onset of chronic intermittent lateral hip pain that worsens with activity, sitting with legs crossed, or lying on the affected side. GTPS is a clinical diagnosis that is confirmed with pain over the greater trochanter and other findings such as pain with resisted hip abduction, nonradicular pain extending down the lateral thigh, and pain with FABER testing (hip flexion, abduction, and external rotation).75

There is no universally accepted physical therapy program for GTPS. Therapy should focus on patient-specific deficits in combination with stretching of the piriformis and iliotibial band and strengthening of the gluteal and core muscle groups. In addition to therapy, corticosteroid injections provide short- and medium-term pain control, and extracorporeal shock wave therapy provides medium- to long-term pain control.49 GTPS is a self-limiting condition, and conservative treatment is successful in up to 90% of patients.70 , 73 , 74 , 76 However, relapse is common if the underlying cause is not addressed.

Patellar Tendinopathy . Patellar tendinopathy, or jumper's knee, is a common cause of anterior knee pain. The highest incidence is in jumping sports such as basketball, volleyball, and soccer. As with most tendinopathies, its etiology is multifactorial. Risk factors include high body mass index, leg length discrepancies, pes cavus, weak and inflexible quadriceps, and inflexible hamstrings.29 Patients report insidious onset of anterior knee pain that is exacerbated with knee flexion and prolonged activity. Localized tenderness at the inferior pole of the patella is a consistent physical examination finding. The decline squat test is the most specific maneuver ( Figure 6 ) 1 patients with patellar tendinopathy will be limited by pain in the number and depth of squats they can perform.

Decline squat test for patellar tendinopathy. This test places greater load on the patellar tendon than a squat performed on level ground.

Illustration by Marcia Hartsock

Reprinted with permission from Wilson JJ, Best TM. Common overuse tendon problems: a review and recommendations for treatment . Am Fam Physician. 200572(5):817 .

Decline squat test for patellar tendinopathy. This test places greater load on the patellar tendon than a squat performed on level ground.

Illustration by Marcia Hartsock

Reprinted with permission from Wilson JJ, Best TM. Common overuse tendon problems: a review and recommendations for treatment . Am Fam Physician. 200572(5):817 .

Initial management of patellar tendinopathy includes relative rest and pain control with NSAIDs or cryotherapy. A patellar counterforce brace, which works by positively altering tendon biomechanics, helps decrease pain and increase function14 , 29 , 77 , 78 ( Figure 7 77 ) . Eccentric exercise is another proven treatment modality and should be part of any physical therapy program for patellar tendinopathy.14 Up to 45% of patients will not respond to eccentric exercise alone in these cases, treatments such as corticosteroid injections, topical nitroglycerin, extracorporeal shock wave therapy, and other therapeutic injections are options before surgery.14 , 29

Patellar tendon strap for patellar tendinopathy.

Reprinted with permission from Sprouse RA, McLaughlin AM, Harris GD. Braces and splints for common musculoskeletal conditions . Am Fam Physician. 201898(10):572 .

Patellar tendon strap for patellar tendinopathy.

Reprinted with permission from Sprouse RA, McLaughlin AM, Harris GD. Braces and splints for common musculoskeletal conditions . Am Fam Physician. 201898(10):572 .

Achilles Tendinopathy . Achilles tendinopathy is common, particularly in patients who engage in regular running-related activities. Studies have estimated an annual incidence of 7% to 9% in current runners and a lifetime prevalence of 52% in former runners.15 However, 30% of referred patients report not regularly participating in exercise, which suggests a multifactorial etiology.16 , 54 Achilles tendinopathy is a clinical diagnosis characterized by pain, swelling, and impaired tendon performance. The pain initially starts at the beginning of and at the termination of exercise as the condition becomes more chronic, the pain persists throughout exercise and can impair activities of daily living. The pathology typically occurs in two locations: 55% to 65% at the midportion of the tendon (2 cm to 6 cm proximal to the insertion), and 20% to 25% at the insertion ( Figure 8 ) .2 If the location is uncertain based on examination findings, ultrasonography or magnetic resonance imaging can be performed.54 , 79

Location of pain in midsubstance Achilles tendinopathy (red) and insertional Achilles tendinopathy (purple) .

Reprinted with permission from Childress MA, Beutler A. Management of chronic tendon injuries . Am Fam Physician. 201387(7):487 .

Location of pain in midsubstance Achilles tendinopathy (red) and insertional Achilles tendinopathy (purple) .

Reprinted with permission from Childress MA, Beutler A. Management of chronic tendon injuries . Am Fam Physician. 201387(7):487 .

Initial management of Achilles tendinopathy begins with risk factor modification, relative rest, and location-specific rehabilitative exercise. Midportion tendinopathy is treated with an eccentric exercise program initially (, then a combination of eccentric and concentric exercises.79 Insertional tendinopathy does not respond as well to eccentric exercise, so rehabilitation focuses on concentric exercise.14 , 15 , 79 Orthotics to correct foot malalignment are another noninvasive and inexpensive modality that can be used for initial treatment.1 As with other tendinopathies, corticosteroid injections, topical nitroglycerin, extracorporeal shock wave therapy, and platelet-rich plasma injections are options if initial conservative treatments are not successful.

This article updates previous articles on this topic by Wilson and Best, 1 and by Childress and Beutler. 2

Data Sources: A PubMed search was completed in Clinical Queries using the key terms tendinitis, tendinopathy, chronic tendinopathy, and management of tendinopathy. The search included meta-analyses, randomized controlled trials, clinical trials, and reviews. We also searched the Agency for Healthcare Research and Quality evidence reports, Clinical Evidence, the Cochrane database, Essential Evidence Plus, the Institute for Clinical Systems Improvement, the National Guideline Clearinghouse database, and the evidence summary provided by AFP . Search dates: January 2019 to April 2019.


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