Lysosome function

Lysosome function

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Does any cell have lysosomes in it? Or maybe there are other organelles that do the same function. I read about it a lot and I can't find a good answer.

The function of a lysosome is to essentially digest and break down molecules (often compared to the stomach of the cell).

For example, a cell with high proportions of lysosomes would be a macrophage, as its function is to neutralize pathogens. After the pathogen is engulfed by the macrophage, the vesicle formed, called a phagosome, fuses with a lysosome, and the lysosome's digestive enzymes work on breaking down the pathogen into harmless bits and pieces.

In most cells, however, lysosomes also function to recycle the cell's own components, called autophagy. Damaged organelles are broken down by the lysosome and recycled.

So, yes, there are many cells that do have lysosomes.

The importance of the lysosome is shown when there is a malfunction in the lysosome. These diseases, called lysosomal storage diseases, occur when the lysosome does not function properly and the cell eventually is impaired by the buildup of a molecule that should have been broken down by the lysosome (e.g. Tay-Sachs disease).


The AP Biology textbook

  • Campbell Biology 7th Edition, Chapter 6 - "Lysosomes: Digestive Compartments", although this is pretty much the same in any edition of this textbook
  • Campbell Biology in Focus, Chapter 4 - "Lysosomes: Digestive Compartments"

What Is The Function Of Lysosomes

The function of lysosomes is to remove waste as well as destroying a cell after it has died, called autolysis. A lysosome is an organelle containing digestive enzymes which it uses to function as the digestion and waste removal for cells, food particles, bacteria, etc.

The cells of both plants and animals have many different organelles. Organelles perform different functions that help the cell survive and replicate, and one of the organelles, the lysosome, carries out a wide variety of functions. Lysosomes are responsible for a number of different functions, including recycling old cells, digesting materials that are both inside and outside of the cell, and releasing enzymes. Let’s take a deep dive into the lysosomes and explore their various important functions in greater detail.


Christian de Duve, the chairman of the Laboratory of Physiological Chemistry at the Catholic University of Louvain in Belgium, had been studying the mechanism of action of a pancreatic hormone insulin in liver cells. By 1949, he and his team had focused on the enzyme called glucose 6-phosphatase, which is the first crucial enzyme in sugar metabolism and the target of insulin. They already suspected that this enzyme played a key role in regulating blood sugar levels. However, even after a series of experiments, they failed to purify and isolate the enzyme from the cellular extracts. Therefore, they tried a more arduous procedure of cell fractionation, by which cellular components are separated based on their sizes using centrifugation.

They succeeded in detecting the enzyme activity from the microsomal fraction. This was the crucial step in the serendipitous discovery of lysosomes. To estimate this enzyme activity, they used that of the standardized enzyme acid phosphatase and found that the activity was only 10% of the expected value. One day, the enzyme activity of purified cell fractions which had been refrigerated for five days was measured. Surprisingly, the enzyme activity was increased to normal of that of the fresh sample. The result was the same no matter how many times they repeated the estimation, and led to the conclusion that a membrane-like barrier limited the accessibility of the enzyme to its substrate, and that the enzymes were able to diffuse after a few days (and react with their substrate). They described this membrane-like barrier as a "saclike structure surrounded by a membrane and containing acid phosphatase." [18]

It became clear that this enzyme from the cell fraction came from membranous fractions, which were definitely cell organelles, and in 1955 De Duve named them "lysosomes" to reflect their digestive properties. [19] The same year, Alex B. Novikoff from the University of Vermont visited de Duve's laboratory, and successfully obtained the first electron micrographs of the new organelle. Using a staining method for acid phosphatase, de Duve and Novikoff confirmed the location of the hydrolytic enzymes of lysosomes using light and electron microscopic studies. [20] [21] de Duve won the Nobel Prize in Physiology or Medicine in 1974 for this discovery.

Originally, De Duve had termed the organelles the "suicide bags" or "suicide sacs" of the cells, for their hypothesized role in apoptosis. [22] However, it has since been concluded that they only play a minor role in cell death. [23]

Lysosomes contain a variety of enzymes, enabling the cell to break down various biomolecules it engulfs, including peptides, nucleic acids, carbohydrates, and lipids (lysosomal lipase). The enzymes responsible for this hydrolysis require an acidic environment for optimal activity.

In addition to being able to break down polymers, lysosomes are capable of fusing with other organelles & digesting large structures or cellular debris through cooperation with phagosomes, they are able to conduct autophagy, clearing out damaged structures. Similarly, they are able to break down virus particles or bacteria in phagocytosis of macrophages.

The size of lysosomes varies from 0.1 μm to 1.2 μm. [24] With a pH ranging from

4.5–5.0, the interior of the lysosomes is acidic compared to the slightly basic cytosol (pH 7.2). The lysosomal membrane protects the cytosol, and therefore the rest of the cell, from the degradative enzymes within the lysosome. The cell is additionally protected from any lysosomal acid hydrolases that drain into the cytosol, as these enzymes are pH-sensitive and do not function well or at all in the alkaline environment of the cytosol. This ensures that cytosolic molecules and organelles are not destroyed in case there is leakage of the hydrolytic enzymes from the lysosome.

The lysosome maintains its pH differential by pumping in protons (H + ions) from the cytosol across the membrane via proton pumps and chloride ion channels. Vacuolar-ATPases are responsible for transport of protons, while the counter transport of chloride ions is performed by ClC-7 Cl − /H + antiporter. In this way a steady acidic environment is maintained. [25] [26]

It sources its versatile capacity for degradation by import of enzymes with specificity for different substrates cathepsins are the major class of hydrolytic enzymes, while lysosomal alpha-glucosidase is responsible for carbohydrates, and lysosomal acid phosphatase is necessary to release phosphate groups of phospholipids.

Many components of animal cells are recycled by transferring them inside or embedded in sections of membrane. For instance, in endocytosis (more specifically, macropinocytosis), a portion of the cell's plasma membrane pinches off to form vesicles that will eventually fuse with an organelle within the cell. Without active replenishment, the plasma membrane would continuously decrease in size. It is thought that lysosomes participate in this dynamic membrane exchange system and are formed by a gradual maturation process from endosomes. [27] [28]

The production of lysosomal proteins suggests one method of lysosome sustainment. Lysosomal protein genes are transcribed in the nucleus in a process that is controlled by transcription factor EB (TFEB). [14] mRNA transcripts exit the nucleus into the cytosol, where they are translated by ribosomes. The nascent peptide chains are translocated into the rough endoplasmic reticulum, where they are modified. Lysosomal soluble proteins exit the endoplasmic reticulum via COPII-coated vesicles after recruitment by the EGRESS complex (ER-to-Golgi relaying of enzymes of the lysosomal system), which is composed of CLN6 and CLN8 proteins. [9] [10] COPII vesicles then deliver lysosomal enzymes to the Golgi apparatus, where a specific lysosomal tag, mannose 6-phosphate, is added to the peptides. The presence of these tags allow for binding to mannose 6-phosphate receptors in the Golgi apparatus, a phenomenon that is crucial for proper packaging into vesicles destined for the lysosomal system. [29]

Upon leaving the Golgi apparatus, the lysosomal enzyme-filled vesicle fuses with a late endosome, a relatively acidic organelle with an approximate pH of 5.5. This acidic environment causes dissociation of the lysosomal enzymes from the mannose 6-phosphate receptors. The enzymes are packed into vesicles for further transport to established lysosomes. [29] The late endosome itself can eventually grow into a mature lysosome, as evidenced by the transport of endosomal membrane components from the lysosomes back to the endosomes. [27]

As the endpoint of endocytosis, the lysosome also acts as a safeguard in preventing pathogens from being able to reach the cytoplasm before being degraded. Pathogens often hijack endocytotic pathways such as pinocytosis in order to gain entry into the cell. The lysosome prevents easy entry into the cell by hydrolyzing the biomolecules of pathogens necessary for their replication strategies reduced Lysosomal activity results in an increase in viral infectivity, including HIV. [30] In addition, AB5 toxins such as cholera hijack the endosomal pathway while evading lysosomal degradation. [30]

Lysosomes are involved in a group of genetically inherited deficiencies, or mutations called lysosomal storage diseases (LSD), inborn errors of metabolism caused by a dysfunction of one of the enzymes. The rate of incidence is estimated to be 1 in 5,000 births, and the true figure expected to be higher as many cases are likely to be undiagnosed or misdiagnosed. The primary cause is deficiency of an acid hydrolase. Other conditions are due to defects in lysosomal membrane proteins that fail to transport the enzyme, non-enzymatic soluble lysosomal proteins. The initial effect of such disorders is accumulation of specific macromolecules or monomeric compounds inside the endosomal–autophagic–lysosomal system. [15] This results in abnormal signaling pathways, calcium homeostasis, lipid biosynthesis and degradation and intracellular trafficking, ultimately leading to pathogenetic disorders. The organs most affected are brain, viscera, bone and cartilage. [31] [32]

There is no direct medical treatment to cure LSDs. [33] The most common LSD is Gaucher's disease, which is due to deficiency of the enzyme glucocerebrosidase. Consequently, the enzyme substrate, the fatty acid glucosylceramide accumulates, particularly in white blood cells, which in turn affects spleen, liver, kidneys, lungs, brain and bone marrow. The disease is characterized by bruises, fatigue, anaemia, low blood platelets, osteoporosis, and enlargement of the liver and spleen. [34] [35] As of 2017, enzyme replacement therapy is available for treating 8 of the 50-60 known LDs. [36]

The most severe and rarely found, lysosomal storage disease is inclusion cell disease. [37]

Metachromatic leukodystrophy is another lysosomal storage disease that also affects sphingolipid metabolism.

Dysfunctional lysosome activity is also heavily implicated in the biology of aging, and age-related diseases such as Alzheimer's, Parkinson's, and cardiovascular disease. [38] [39]

Sr. No Enzymes Substrate
1 Phosphates
A- Acid phosphatase Most phosphomonoesters
B- Acid phosphodiesterase Oligonucleotides and phosphodiesterase
2 Nucleases
A- Acid ribonuclease RNA
B- Acid deoxyribonuclease DNA
3 Polysaccharides/ mucopolysaccharides hydrolyzing enzymes
A- beta Galactosidase Galactosides
B- alfa Glucosidase Glycogen
C- alfa Mannosidase Mannosides, glycoproteins
D- beta Glucoronidase Polysaccharides and mucopolyssacharides
E- Lysozymes Bacterial cell walls and mucopolyssacharides
F- Hyaluronidase Hyaluronic acids, chondroitin sulphates
H- Arylsulphatase Organic sulfates
4 Proteases
A- Cathepsin(s) Proteins
B- Collagenase Collagen
C- Peptidase Peptides
5 Lipid degrading enzymes
A- Esterase Fatty acyl esters
B- Phospolipase Phospholipids

Lysosomotropism Edit

Weak bases with lipophilic properties accumulate in acidic intracellular compartments like lysosomes. While the plasma and lysosomal membranes are permeable for neutral and uncharged species of weak bases, the charged protonated species of weak bases do not permeate biomembranes and accumulate within lysosomes. The concentration within lysosomes may reach levels 100 to 1000 fold higher than extracellular concentrations. This phenomenon is called lysosomotropism, [41] "acid trapping" or "proton pump" effect. [42] The amount of accumulation of lysosomotropic compounds may be estimated using a cell-based mathematical model. [43]

A significant part of the clinically approved drugs are lipophilic weak bases with lysosomotropic properties. This explains a number of pharmacological properties of these drugs, such as high tissue-to-blood concentration gradients or long tissue elimination half-lifes these properties have been found for drugs such as haloperidol, [44] levomepromazine, [45] and amantadine. [46] However, high tissue concentrations and long elimination half-lives are explained also by lipophilicity and absorption of drugs to fatty tissue structures. Important lysosomal enzymes, such as acid sphingomyelinase, may be inhibited by lysosomally accumulated drugs. [47] [48] Such compounds are termed FIASMAs (functional inhibitor of acid sphingomyelinase) [49] and include for example fluoxetine, sertraline, or amitriptyline.

Ambroxol is a lysosomotropic drug of clinical use to treat conditions of productive cough for its mucolytic action. Ambroxol triggers the exocytosis of lysosomes via neutralization of lysosomal pH and calcium release from acidic calcium stores. [50] Presumably for this reason, Ambroxol was also found to improve cellular function in some disease of lysosomal origin such as Parkinson's or lysosomal storage disease. [51] [52]

Systemic lupus erythematosus Edit

Impaired lysosome function is prominent in systemic lupus erythematosus preventing macrophages and monocytes from degrading neutrophil extracellular traps [53] and immune complexes. [54] [55] [56] The failure to degrade internalized immune complexes stems from chronic mTORC2 activity, which impairs lysosome acidification. [57] As a result, immune complexes in the lysosome recycle to the surface of macrophages causing an accumulation of nuclear antigens upstream of multiple lupus-associated pathologies. [54] [58] [59]

By scientific convention, the term lysosome is applied to these vesicular organelles only in animals, and the term vacuole is applied to those in plants, fungi and algae (some animal cells also have vacuoles). Discoveries in plant cells since the 1970s started to challenge this definition. Plant vacuoles are found to be much more diverse in structure and function than previously thought. [60] [61] Some vacuoles contain their own hydrolytic enzymes and perform the classic lysosomal activity, which is autophagy. [62] [63] [64] These vacuoles are therefore seen as fulfilling the role of the animal lysosome. Based on de Duve's description that "only when considered as part of a system involved directly or indirectly in intracellular digestion does the term lysosome describe a physiological unit", some botanists strongly argued that these vacuoles are lysosomes. [65] However, this is not universally accepted as the vacuoles are strictly not similar to lysosomes, such as in their specific enzymes and lack of phagocytic functions. [66] Vacuoles do not have catabolic activity and do not undergo exocytosis as lysosomes do. [67]

The word lysosome ( / ˈ l aɪ s oʊ s oʊ m / , / ˈ l aɪ z ə z oʊ m / ) is New Latin that uses the combining forms lyso- (referring to lysis and derived from the Latin lysis, meaning "to loosen", via Ancient Greek λύσις [lúsis]), and -some, from soma, "body", yielding "body that lyses" or "lytic body". The adjectival form is lysosomal. The forms *lyosome and *lyosomal are much rarer they use the lyo- form of the prefix but are often treated by readers and editors as mere unthinking replications of typos, which has no doubt been true as often as not.

Anterograde transport

Kinesins are microtubule motors involved in the movement of multiple cytoplasmic organelles, including lysosomes (Hirokawa and Noda, 2008). Mammalian genomes encode about 45 kinesin superfamily (KIF) proteins, and many more variants are generated by alternative splicing of the corresponding mRNAs. All KIFs comprise a globular motor domain that attaches to microtubules, and a tail domain that interacts with specific adaptors or cargos. ATP hydrolysis by the motor domain provides the driving force for translocation of kinesins and associated cargos from the minus end to the plus end of microtubules (i.e. anterograde transport), with the exception of kinesin-14 members, which move in the plus-to-minus-end direction (Hirokawa and Noda, 2008). In non-polarized cells, microtubule plus-ends are generally found in the peripheral cytoplasm and in neurons they point towards axon terminals, so, in these cells, kinesins mediate transport from the cell center towards the periphery (known as centrifugal transport). In some polarized cells, however, microtubules can point in other directions, as is the case for neuronal dendrites, which have microtubules with mixed orientations (Baas et al., 1988 Yau et al., 2016). In these cases, kinesins can potentially mediate both centrifugal and centripetal transport.

Remarkably, lysosome movement has been shown to depend on not one but multiple kinesins, including kinesin-1 (KIF5A, KIF5B and KIF5C) (Nakata and Hirokawa, 1995 Tanaka et al., 1998 Rosa-Ferreira and Munro, 2011), kinesin-2 (KIF3) (Brown et al., 2005 Loubéry et al., 2008) and kinesin-3 (KIF1A and KIF1B) (Matsushita et al., 2004 Korolchuk et al., 2011 Bentley et al., 2015), as well as the kinesin-13 (KIF2) family members (Santama et al., 1998 Korolchuk et al., 2011) (Fig. 3). At present it is unclear why so many kinesins have evolved to move the same organelle. Possible explanations are (1) functional redundancy, (2) cell-type-specific expression (e.g. non-neuronal versus neuronal cells), (3) involvement in different lysosomal functions (e.g. autophagy versus exocytosis), (4) differential regulation, and (5) transport along different microtubule tracks. With regard to this latter possibility, several kinesins exhibit preferential association with microtubule tracks that are characterized by specific post-translational modifications (PTMs) of tubulin, microtubule-associated proteins (MAPs) or kinesin-binding proteins (KBPs) (Marx et al., 2005). For example, kinesin-1 motors move faster on microtubule tracks enriched in acetylated and GTP-bound tubulin, but slower motors that make longer processive runs have been observed on detyrosinated microtubules (Reed et al., 2006 Dunn et al., 2008 Hammond et al., 2008 Konishi and Setou, 2009 Nakata et al., 2011). Kinesin-2 (KIF17) and -3 (KIF1A) family members do not exhibit preferences for acetylated or detyrosinated microtubules (Cai et al., 2009), but KIF1A-dependent transport is influenced by tubulin polyglutamylation (Ikegami et al., 2007). MAPs often inhibit kinesin-dependent transport by acting as obstacles to movement. A prime example of this behavior is mediated by the protein tau, which blocks kinesin-1-dependent motility (Dehmelt and Halpain, 2005 Al-Bassam et al., 2007). Other MAPs (e.g. ensconsin and DCLK1), however, promote recruitment and activation of kinesins on specific populations of microtubules (Sung et al., 2008 Lipka et al., 2016). Finally, KBPs can modulate kinesin activity, as shown for the inactivation of the motor domains of the kinesin-3 KIF1A and kinesin-8 KIF18A by the protein KBP (also known as KIF1BP and KIAA1279) (Kevenaar et al., 2016). It remains to be determined how all of these factors influence the ability of different kinesins to mediate different patterns of lysosome movement.

Kinesins implicated in lysosome movement. Family names, domains and amino acid numbers are indicated. CC, coiled coil Gl, globular FHA, forkhead-associated UDR, undefined region PH, pleckstrin-homology.

Kinesins implicated in lysosome movement. Family names, domains and amino acid numbers are indicated. CC, coiled coil Gl, globular FHA, forkhead-associated UDR, undefined region PH, pleckstrin-homology.

By far the best-characterized kinesin involved in lysosome transport is kinesin-1 (Figs 3 and 4). This kinesin is a heterotetramer composed of two heavy chains (KIF5A, KIF5B or KIF5C) and two light chains (KLC1, KLC2, KLC3 or KLC4) (DeBoer et al., 2008). Kinesin-1 is recruited to lysosomes by a chain of interacting proteins, including the multisubunit BLOC-1-related complex (BORC), the Arf-like small GTPase Arl8 (which has two isoforms in mammals, Arl8a and Arl8b, hereafter generically referred to as Arl8), and the Arl8 effector SifA and kinesin-interacting protein (SKIP, also known as PLEKHM2) (Boucrot et al., 2005 Bagshaw et al., 2006 Hofmann and Munro, 2006 Rosa-Ferreira and Munro, 2011 Pu et al., 2015) (Fig. 4). BORC is an octameric complex comprising BLOS1, BLOS2 (also known as BLOC1S1 and BORCS1, and BLOC1S2 and BORCS2, respectively) and snapin (also known as BORCS3) subunits (all three of which are shared with the BLOC-1 complex involved in the biogenesis of lysosome-related organelles) (Falcon-Perez et al., 2002 Moriyama and Bonifacino, 2002 Starcevic and Dell'Angelica, 2004), plus the unique subunits KXD1 (also known as BORCS4), MEF2BNB (also known as BORCS8), myrlysin (also known as LOH12CR1 and BORCS5), lyspersin (also known as C17orf59 and BORCS6) and diaskedin (also known as C10orf32 and BORCS7) (Pu et al., 2015). BORC associates with the cytosolic face of lysosomes partly through the myristoylated N-terminus of myrlysin, and is subsequently required for recruitment of Arl8 from the cytosol (Pu et al., 2015). This function of BORC would be consistent with it being a guanine-nucleotide-exchange factor (GEF) (Rosa-Ferreira and Munro, 2011) for Arl8, but there is currently no biochemical evidence for this activity. SKIP in turn binds to Arl8 through an N-terminal RUN domain (Rosa-Ferreira and Munro, 2011). A WD motif in an unstructured region of SKIP then interacts with the tetratricopeptide repeat (TPR) domain of the KLC (Rosa-Ferreira and Munro, 2011), thus completing the linkage of lysosomes to KIF5 proteins. Various ways of negatively interfering with this chain of interactors inhibit lysosome movement towards the cell periphery, resulting in collapse of the entire lysosomal population to the cell center (Fig. 2). Conversely, overexpression of some components of this cascade, such as SKIP, causes accumulation of lysosomes at the cell periphery (Fig. 2). An alternative mechanism for coupling of late endosomes to kinesin-1 involves the ER-anchored protein protrudin, which binds simultaneously to the small GTPase Rab7 (which has two isoforms in mammals, Rab7a and Rab7b, hereafter generically referred to as Rab7) and phosphatidylinositol 3-phosphate [PtdIns(3)P] to bridge the ER and lysosomal membranes. Protrudin then transfers late endosomes to the Rab7 effector FYVE- and coiled-coil-domain-containing protein (FYCO1) and kinesin-1 for late endosome movement towards the cell periphery (Matsuzaki et al., 2011 Raiborg et al., 2016) (Fig. 4).

Mechanisms of late endosome and lysosome transport along microtubules. Anterograde transport of late endosome (LE) and lysosome transport is mediated by an ensemble of BORC, Arl8, SKIP and kinesin-1 (a heterotetramer composed of two KLC and two KIF5 chains). An alternative mechanism of anterograde transport uses Rab7 and FYCO1 as adaptors to kinesin-1. FYCO1 is loaded onto late endosomes by the action of the ER-anchored protrudin. Other kinesins depicted in Fig. 3 have also been shown to drive anterograde transport of lysosomes, but their mechanisms of coupling are less well understood. Retrograde transport is mediated by Rab7, RILP, ORP1L and dynein–dynactin. The names of some of the dynactin subunits are indicated (p150-glued, Arp1). Under low-cholesterol concentrations, ORP1L interacts with the ER-anchored protein VAPA, leading to dynein dissociation and redistribution of lysosomes to the cell periphery.

Mechanisms of late endosome and lysosome transport along microtubules. Anterograde transport of late endosome (LE) and lysosome transport is mediated by an ensemble of BORC, Arl8, SKIP and kinesin-1 (a heterotetramer composed of two KLC and two KIF5 chains). An alternative mechanism of anterograde transport uses Rab7 and FYCO1 as adaptors to kinesin-1. FYCO1 is loaded onto late endosomes by the action of the ER-anchored protrudin. Other kinesins depicted in Fig. 3 have also been shown to drive anterograde transport of lysosomes, but their mechanisms of coupling are less well understood. Retrograde transport is mediated by Rab7, RILP, ORP1L and dynein–dynactin. The names of some of the dynactin subunits are indicated (p150-glued, Arp1). Under low-cholesterol concentrations, ORP1L interacts with the ER-anchored protein VAPA, leading to dynein dissociation and redistribution of lysosomes to the cell periphery.

A recent study has shown that the recruitment of the kinesin-3 proteins KIF1A and KIF1Bβ is also dependent on BORC and Arl8 (Guardia et al., 2016), as well as several parts of the C-terminal tail domain (Bentley et al., 2015 Guardia et al., 2016). Considerably less is known about the mechanisms that couple other kinesins to lysosomes. For the kinesin-2 KIF3A, the accessory protein KAP3 has been implicated in lysosome movement (Brown et al., 2005), but other potential regulators and adaptors remain to be identified. It would be of particular interest to investigate whether the Arl8- and Rab7-regulated pathways also operate for other kinesins involved in lysosome movement.

Why study lysosome biology?

Lysosomes are degradative organelles present in all eukaryotic cell types and perform multiple critical functions in addition to their role as an &lsquoincinerator&rsquo in the cell. Lysosomes are the epicenter of all trafficking pathways and integrate cellular metabolism to permit critical decisions on life and death, and growth or quiescence. They are critically important organelles as evidenced by genetic inborn errors collectively term &lsquolysosome storage diseases&rsquo which result from deficiency of structural or enzymatic proteins in the lysosomes and trigger global lysosome dysfunction. These disease affect the central nervous system and/or the heart in every single instance indicating how critical lysosome function is these differentiated primary cell types. My lab&rsquos primary interest is to define the role of lysosomes in cellular homeostasis and response to stress. Work from our lab and others has uncovered evidence for acquired lysosome dysfunction in cardiovascular, metabolic and neurodegenerative diseases. We have shown that acquired lysosome dysfunction is a major contributor to cardiac myocyte loss in myocardial ischemia-reperfusion injury and in cardiomyopathy and heart failure. Our work has also extended these findings to uncover evidence for lysosome dysfunction in various CNS cell types in Alzheimer&rsquos disease and in pancreatic beta cells in obesity-induced diabetes. Remarkably, all these diseases are predisposed to by a common set of risk factors. For example, aging is a common risk factor for all these diseases and has been implicated in causing progressive lysosome dysfunction. As the PI or co-investigator on studies funded through National funding mechanisms, we have developed the expertise and tools to experimentally perturb and evaluate lysosome biology, concomitantly with disease modeling in in vitro and in vivo systems. Our goal is to understand the mechanisms for acquired lysosome dysfunction in human diseases, assess the efficacy and safety of therapeutically targeting lysosome biogenesis and function in animal models and develop therapies that can be translated to humans to treat diseases characterized by acquired lysosome dysfunction.


Lysosomes are membrane bound vesicular cytoplasmic organelles containing hydrolytic enzynes. So, Lysosomes are specialized vesicles within cells that digest large molecules through the use of hydrolytic enzymes. They are found in almost all animal cells and remain scattered in the cytoplasm. Lysosomes are not seen in plant cells except those of meristematic tissue. The number of Lysosomes in animal cells is variable. These are present in large numbers in secretory cells and white blood cells.

Origin of Lysosomes

By the joint action of Endoplasmic Reticulum and Golgi body the Lysosomes are formed. The hydrolytic enzymes of Lysosomes are synthesized in the rough Endoplasmic Reticulum and then passed to the Golgi body, from where in conclusion by a process of budding, membrane bound and enzyme filled vesicles are released in the cytoplasm which is called Lysosomes.

Structure of Lysosomes

Just like membrane enclosed vesicles Lysosomes generally look like. The surrounding membrane is a single membrane like the cell membrane. The average diameter varies from 0.2-0.8 urn. The shape, size and internal structure of Lysosomes are variable in nature. In some cases, the inner part is denser than its outer part, while in others the outer part is denser than the inner part. There are granules and minute vacuoles are seen within Lysosomes. The Lysosomes contain hydrolytic enzymes, where as the micro-bodies contain oxidative enzymes. So that, though Lysosomes and micro-bodies have similar structures because both are single membrane bound, small, vesicular organelles containing specific enzymes but they should not be confused.

Functions of Lysosomes

In brief the Lysosomes has the following types of functions:
i) Extracellular digestion
ii) Intracellular digestion
iii) Bactericidal action
iv) Fertilization
v) Hormone secretion
vi) Protection from diseases.

Extracellular digestion

Newly formed Lysosomes are called primary Lysosomes that contain a specific type of enzyme. Some cells exude Lysosomes enzymes into their surroundings for hydrolysis or digestion of extracellular materials. This is called extracellular digestion. Saprophytic fungi derive their nutrition by this type of extracellular digestion.

Intracellular digestion

Digestion of a material within a cell is called intracellular digestion. Depending upon whether the material to be digested is exogenous or endogenous it may be either of the two types respectively : -
a ) heterophagy
b) autophagy


This is a process in which a material engulfed by a cell is digested within it. The material engulfed by phagocytosis or pinocytosis forms a digestive vacuole or phagosome which then fuses with a primary Lysosomes to form a secondary Lysosomes or heterophagosome. Inside it, the food particles are hydrolysed and the, digestion products are absorbed into the cytoplasm across its membrane. If some undigested residue is left in the heterophagosome, such Lysosomes are called residual body which expels the excretory materials from the cell.


Autophagy is a process by which the old, non-functional and spoiled organelles of a cell are digested by its own lysosomal enzymes. In this process, a primary Lysosomes engulfs a non-functional organelle to form an autophagosome within which the organelle is digested and its constituents are absorbed into the cytoplasm. The hydrolytic enzymes of Lysosomes remain enclosed within its membrane so that the living and active mechanism of a cell are protected from autolysis. It to be noted that the hydrolytic enzymes are released in the cytoplasm and the entire cell is self digested which is called autolysis of a cell.

Bactericidal action

Lysosomes of phagocytic cells contain bactericidal agents that help to kill and destroy the bacteria engulfed by the cell.


Throughout fertilization, the lysosomal enzyme secreted from the sperms disperses the cells covering the ovum so as to make possible union of gametes. This is a extracellular digestion by lysosomal enzymes.

Hormone secretion

Discharge of thyroid hormone-from its site of storage in the gland is mediated by the action of lysosomal enzymes of thyroid cells.

Protection from diseases

Not working of Lysosomes is associated with a number of diseases like inflammation, arthritis, storage disease, cancer etc.

A lysosome has three main functions: the breakdown/digestion of macromolecules (carbohydrates, lipids, proteins, and nucleic acids), cell membrane repairs, and responses against foreign substances such as bacteria, viruses and other antigens. When food is eaten or absorbed by the cell, the lysosome releases its enzymes to break down complex molecules including sugars and proteins into usable energy needed by the cell to survive. If no food is provided, the lysosome&rsquos enzymes digest other organelles within the cell in order to obtain the necessary nutrients.

In addition to their role as the digestive component and organelle-recycling facility of animal cells, lysosomes are considered to be parts of the endomembrane system. Lysosomes also use their hydrolytic enzymes to destroy pathogens (disease-causing organisms) that might enter the cell. A good example of this occurs in a group of white blood cells called macrophages, which are part of your body&rsquos immune system. In a process known as phagocytosis or endocytosis, a section of the plasma membrane of the macrophage invaginates (folds in) and engulfs a pathogen. The invaginated section, with the pathogen inside, then pinches itself off from the plasma membrane and becomes a vesicle. The vesicle fuses with a lysosome. The lysosome&rsquos hydrolytic enzymes then destroy the pathogen.

Figure: Lysosomes digest foreign substances that might harm the cell: A macrophage has engulfed (phagocytized) a potentially pathogenic bacterium and then fuses with a lysosomes within the cell to destroy the pathogen. Other organelles are present in the cell but for simplicity are not shown.

A lysosome is composed of lipids, which make up the membrane, and proteins, which make up the enzymes within the membrane. Usually, lysosomes are between 0.1 to 1.2&mum, but the size varies based on the cell type. The general structure of a lysosome consists of a collection of enzymes surrounded by a single-layer membrane. The membrane is a crucial aspect of its structure because without it the enzymes within the lysosome that are used to breakdown foreign substances would leak out and digest the entire cell, causing it to die.

Lysosomes are found in nearly every animal-like eukaryotic cell. They are so common in animal cells because, when animal cells take in or absorb food, they need the enzymes found in lysosomes in order to digest and use the food for energy. On the other hand, lysosomes are not commonly-found in plant cells. Lysosomes are not needed in plant cells because they have cell walls that are tough enough to keep the large/foreign substances that lysosomes would usually digest out of the cell.


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Lysosome, subcellular organelle that is found in nearly all types of eukaryotic cells (cells with a clearly defined nucleus) and that is responsible for the digestion of macromolecules, old cell parts, and microorganisms. Each lysosome is surrounded by a membrane that maintains an acidic environment within the interior via a proton pump. Lysosomes contain a wide variety of hydrolytic enzymes ( acid hydrolases) that break down macromolecules such as nucleic acids, proteins, and polysaccharides. These enzymes are active only in the lysosome’s acidic interior their acid-dependent activity protects the cell from self-degradation in case of lysosomal leakage or rupture, since the pH of the cell is neutral to slightly alkaline. Lysosomes were discovered by the Belgian cytologist Christian René de Duve in the 1950s. (De Duve was awarded a share of the 1974 Nobel Prize for Physiology or Medicine for his discovery of lysosomes and other organelles known as peroxisomes.)

Lysosomes originate by budding off from the membrane of the trans-Golgi network, a region of the Golgi complex responsible for sorting newly synthesized proteins, which may be designated for use in lysosomes, endosomes, or the plasma membrane. The lysosomes then fuse with membrane vesicles that derive from one of three pathways: endocytosis, autophagocytosis, and phagocytosis. In endocytosis, extracellular macromolecules are taken up into the cell to form membrane-bound vesicles called endosomes that fuse with lysosomes. Autophagocytosis is the process by which old organelles and malfunctioning cellular parts are removed from a cell they are enveloped by internal membranes that then fuse with lysosomes. Phagocytosis is carried out by specialized cells (e.g., macrophages) that engulf large extracellular particles, such as dead cells or foreign invaders (e.g., bacteria), and target them for lysosomal degradation. Many of the products of lysosomal digestion, such as amino acids and nucleotides, are recycled back to the cell for use in the synthesis of new cellular components.

Lysosomal storage diseases are genetic disorders in which a genetic mutation affects the activity of one or more of the acid hydrolases. In such diseases, the normal metabolism of specific macromolecules is blocked and the macromolecules accumulate inside the lysosomes, causing severe physiological damage or deformity. Hurler syndrome, which involves a defect in the metabolism of mucopolysaccharides, is a lysosomal storage disease.

The Editors of Encyclopaedia Britannica This article was most recently revised and updated by Kara Rogers, Senior Editor.

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Can somebody help me regarding the best concentration of lysosomes to lysis the protein. Thank you in advance. anon336301 May 27, 2013

@TreeMan and titans62: The cell uses diffusion and osmosis to get rid of waste. -- Sophomore at UW-Madison jcraig October 15, 2011

@jmc88 - I tried to look up some information about Tay-Sachs disease, but I couldn't really find anything about the exact mechanisms that cause it. All I could find out was that it is a disease of the nervous system.

As far as the function of the lysosomes, is there any interaction with vacuoles in terms of either transferring materials or pH balance in the cell?

Also, the article mentioned quite a few different molecules you could expect to find in a lysosome that help break down proteins and other molecules. Where are the enzymes created in the first place? Are there other organelles that are responsible for building the enzymes and then passing them on to the lysosome, or does the lysosome create enzymes itself? jmc88 October 14, 2011

@TreeMan - I may be completely wrong about this, but I seem to remember something in my high school biology class about there being special cells that are designed to seek out old or unnecessary cells and "eat" them. I'm sure during that process, the lysosome materials from one cell and transferred to another.

Since a ruptured lysosome would be dangerous for a cell, I'm curious if there are any diseases or viruses that specifically target the wall of the lysosome and cause it to burst and destroy cells. Maybe that is what Tay-Sachs does. Does anyone know? TreeMan October 14, 2011

@titans62 - I am not certain, but my best guess would be that the lysosome connects with the cell membrane and releases the waste materials into the lymph system where the molecules are picked up by white blood cells and carried to other parts of the lymph system to eventually be excreted by the body.

Along those same lines, do white blood cells tend to have more lysosomes compared to something like a nerve cell, for instance?

What happens to the material inside the lysosomes when a cell is destroyed or accidentally ruptures? How does an organism make sure that cells around it aren't damaged?

I had heard of Tay-Sachs disease, but didn't have any idea it was caused by a problem with an organelle in the cell. What exactly happens in Tay-Sachs disease, and how are the lysosomes involved? Is there any way to prevent the disease? If I remember correctly, it is usually something that affects you when you are young.

Something else I was wondering about the lysosome function is how the lysosome actually gets rid of waste materials after it is done breaking them down. Does it just release them into the blood stream somehow, or what happens, since the article mentions the waste materials being very acidic?


The main function of these microscopic organelles is to serve as digestion compartments for cellular materials that have exceeded their lifetime or are otherwise no longer useful. In this regard, the lysosomes recycle the cell's organic material in a process known asautophagy. Lysosomes break down cellular waste products, fats, carbohydrates, proteins, and other macromolecules into simple compounds, which are then transferred back into the cytoplasm as new cell-building materials. To accomplish the tasks associated with digestion, the lysosomes utilize about 40 different types of hydrolytic enzymes, all of which are manufactured in the endoplasmic reticulum and modified in the Golgi apparatus. Lysosomes are often budded from the membrane of the Golgi apparatus, but in some cases they develop gradually from late endosomes, which are vesicles that carry materials brought into the cell by a process known as endocytosis.

Like other microbodies, lysosomes are spherical organelles contained by a single layer membrane, though their size and shape varies to some extent. This membrane protects the rest of the cell from the harsh digestive enzymes contained in the lysosomes, which would otherwise cause significant damage. The cell is further safeguarded from exposure to the biochemical catalysts present in lysosomes by their dependency on an acidic environment. With an average pH of about 4.8, the lysosomal matrix is favorable for enzymatic activity, but the neutral environment of the cytosol renders most of the digestive enzymes inoperative, so even if a lysosome is ruptured, the cell as a whole may remain uninjured. The acidity of the lysosome is maintained with the help of hydrogen ion pumps, and the organelle avoids self-digestion by glucosylation of inner membrane proteins to prevent their degradation.

The discovery of lysosomes involved the use of a centrifuge to separate the various components of cells. In the mid-twentieth century, the Belgian scientist Christian René de Duve was investigating carbohydrate metabolism of liver cells and observed that that the cells released an enzyme called acid phosphatase in larger amounts when they received proportionally greater damage in the centrifuge. To explain this phenomenon, de Duve suggested that the digestive enzyme was encased in some sort of membrane-bound organelle within the cell, which he dubbed the lysosome. After estimating the probable size of the lysosome, he was able to identify the organelle in images produced with an electron microscope.

Lysosomes are found in all animal cells, but are most numerous in disease-fighting cells, such as white blood cells. This is because white blood cells must digest more material than most other types of cells in their quest to battle bacteria, viruses, and other foreign intruders. Several human diseases are caused by lysosome enzyme disorders that interfere with cellular digestion. Tay-Sachs disease, for example, is caused by a genetic defect that prevents the formation of an essential enzyme that breaks down complex lipids calledgangliosides. An accumulation of these lipids damages the nervous system, causes mental retardation, and death in early childhood. Also, arthritis inflammation and pain are related to the escape of lysosome enzymes.

Watch the video: Lysosome (July 2022).


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