How Do Lysosomes Cause Disease?

Today is my second day inside the cell. "Ok now that I'm in the cell, how am I supposed to go explore the cell with no transportation? Oh, nevermind I can use vesicles to take all around the cell.". I get on a vesicle and im zooming through the air like lightning. Looking around the cell I see the cytoplasm holding the organelles. It's the jelly like substance in the cell. ". There goes the lysosomes, in other words the recycling center.". The job for the lysosome is to break down and digest. The lysosomes seems to be working just fine. "Holy cow! There goes the mitochondria.". The mitochondria has a really hard job, it's one of the organnelles that use up more energy. The job of the mitochondria is to break down food into carbon dioxide and

Lysosomes are membranous sacs of enzymes that are typically are involved in the digestion of cellular macromolecules. They are made by both the endoplasmic reticulum and the Golgi complex. Lysosomes have various roles, including the recycling of the cell's organic material and in the intracellular digestion of macromolecules. The digestion of macromolecules is carried out through an intense concentration of enzymes. To be specific, lysosomes contain close to 50 different degrading enzymes that are capable of hydrolyzing proteins, DNA, RNA, polysaccharides, and lipids within the cell.1 All of lysosomal enzymes are acid hydrolases,

James Parkinson first described the disease named after him as a motor dysfunction through an essay on “shaking palsy” in the early nineteenth century, with Friedrich Lewy a century later describing atypical masses of protein (now known as Lewy bodies) within cell cytoplasm’s in the brainstems of those displaying symptoms of Parkinson’s disease including those with dementia. Because of the distinct similarities, there has been professional discussion that Parkinson’s disease, Parkinson’s with dementia, and dementia with Lewy bodies be grouped as one: Lewy Body Disease (Auning, E., A., & Aarsland, D., 2012, p. 233). Dementia associated with Parkinson’s is frequent, with the occurrence assessed. Those with Parkinson’s disease with dementia represent 5% of all people who have dementia, and of

Niemann-Pick’s disease Type C (NPC) is disease in which unesterified cholesterol and other lipids accumulate in late endosomes/lysosomes (LE/L) of all cells and tissues. Resulting in excessive amounts of cholesterol accumulation within the liver and spleen and excessive amounts of other lipids accumulating in the brain. The cause of NPC is quite distinct from A & B whose patients have defects in their lysosomal acid sphingomyelinase gene (3). On the contrary, NPC is a recessive, autosomal disorder that affects around 1 in 150,000 births and causes premature death due to relentless neurodegeneration as well as lung and liver dysfunction (4,5). NPC can further be divided into two subgroups known as C1 and C2, which are each, caused by a different gene mutation.

Autophagy is a evolutionarily conserved essential proteostasis and catabolic membrane trafficking process that has close associations with health and longevity [10, 11]. It maintains cellular homeostasis and viability by regulating the quantity and quality of cytoplasmic constituents such as organelles and macromolecules through lysosomal degradation, which is activated in response to nutrient starvation and other stressors to generate energy and allow survival [12]. Autophagy plays vital roles by self-degrading under a variety of physiological and pathological conditions such as maintaining the stem cell quiescent state [13], manipulating immunity [14], regulating bone growth [15], carcinogenesis [16-18] and cell metabolism [18]. Importantly, Autophagy directly targets pathogenic misfolded Aβ for degradation [19]. Chemical that enhances autophagy was shown to be capable of restoring nesting behavior in a murine model of Alzheimer disease [20]. Extensive efforts have been made on Aβ degradation by autophagy, though people also argued that

Parkinson’s disease (PD) is the most frequent movement disorder and the second most common neurodegenerative disease (Bueler 2009). Over 1% of the entire population over the age of 60, and up to 5% of age 80, is affected by PD (Wood-Kaczmar, Gandhi et al. 2006). The pathogenesis of PD remains unclear, but can be categorized as sporadic, being the most common form, and Mendelian, which accounts for 5-10% of all PD cases (Guo 2008). The studies of Mendelian onset of PD have lead to the identification of five genes being linked to this neurodegenerative disease (Guo 2008). α-Synuclein (SNCA) and Leucine-rich repeat kinase 2 (LRRK2) mediate autosomal dominant forms of PD. PTEN-induced putative kinase 1 (PINK1),

Endocytosis is the capacity to disguise material from outside the cell is critical for a few cell forms including the ingestion of fundamental supplements, expulsion of dead or harmed cells from the body, and guard against microorganisms. Eukaryotic cells disguise liquid, extensive and little particles, and even different cells from their surroundings by a procedure called endocytosis. Amid endocytosis, the plasma layer of the cell frames a pocket around the material to be disguised. The pocket closes and afterward isolates from within surface of the plasma layer to shape a film encased air pocket, or vesicle, containing the ingested

Resting tremors, slowness and rigidity of the limbs, Parkinson’s disease runs rampant among the elderly population and upon diagnosis, changes lives forever (Vilariño-Güell et al, 2013). With little to nothing known about what causes the disease or why it is so common in some families, the scene was set for a Canadian research team along with a Canadian Mennonite family to change that. Following careful examination the research team found that a mutation in the gene DNAJC13 caused the buildup of more and denser transport vesicles in the cells, resulting in the contraction of Parkinson’s (Vilariño-Güell et al, 2013). This mutation was found to be sustained over multiple generations,

Lytic granules are dual-functioned organelles that not only store and secrete cytotoxic molecules, but also degrade other proteins just like conventional lysosomes (Blott and Griffiths, 2002, Burkhardt et al., 1990). Lytic granules seem to be the only lysosome-type organelle present in NK cells and CTLs, unlike in melanosomes which contain both conventional and secretory lysosomes (Raposo et al., 2007). For the proper functioning of the lysosomal enzymes, lytic granules also have an acidic pH just like regular lysosomes. The pore-forming molecule perforin and the cell death-promoting molecule granzyme are localized in a dense core domain, whereas the membrane-associated and soluble lysosomal proteins are contained in a multi-vesicular cortical domain, as observed by electron microscopy (Peters et al., 1991). The relative amounts of the multi-vesicular cortex and the dense core, however, vary considerably among lytic granules (Stinchcombe et al., 2000).

Are organelles that have digestive enzymes. They help get rid of unnecessary organelles, food pieces, and viruses or bacteria. They pretty much get rid of the thigs your body doesn’t need. Whatever is damaged or old in your body, this cell stores it on the outside section of the lysosome. Then the membrane opens and the particle is moved to the lysosome. Inside, the enzymes that are made break down whatever particles were transferred to the lysosome. Finally, after everything has been broken up the lysosome opens and sends the remains into the cell in the form of a vesicle.

The golgi body packages proteins and carbohydrates into membrane-bound vesicles for “export” from the cell.

Lysosome plays important role in cells’ behavior, it not only the degradation and recycle place for cells, but it also associated with cellular processes such as autophagy and signaling. Especially in cancer cells, the lysosomes are greater in number, larger, more active than normal cells. [1] The mechanism for lysosome in cancer cells is that lysosome can release certain cathepsins, which is a kind of virtual acidic hydrolases released from tumor cells into the extracellular space, which lead to cancer cells’ progression and death by apoptosis and apoptosis-like pathways. [2] On the one hand, the cathepsins contribute to the degradation of intracellular substrates, regulation and recycle of extracellular substrates. On the other hand, the cathepsins control

Eukaryotic cells can massively transfer their own cytoplasmic contents into a lytic compartment, the vacuole/lysosome, for reprocessing through a conserved system called autophagy. The key process in autophagy is the separation of cytoplasmic

There are three defined forms of autophagy, Macro-autophagy, micro-autophagy, and chaperone-mediated autophagy; each form has its own way of carrying out autophagocytosis. Macro-autophagy delivers cargo to the Lysosome through a membrane-bound vesicle, also known as an autophagosome. The lysosome then carries out autolysosome to destroy the cargo. In micro-autophagy the cargo is taken directly taken up by the Lysosome instead of a vesicle bringing the cargo to it. Both Macro and Micro are capable of consuming large structures. In Chpaerone-mediated autophagy targeted proteins are carried across the lysosome membrane with chaperone proteins that result in their unfolding and degradation.

Digestion is the process of breaking larger food particles into smaller particles that can pass through the plasma membrane. The digestive system is in charge of this process. To begin, the mouth receives food, breaking it into smaller particles by chewing, a form of mechanical digestion with the teeth, for absorption. The tongue aids in this process of chewing and swallowing as a muscular organ. Additionally, the salivary glands in the mouth secrete saliva to help lubricate the food and begin chemical digestion with its digestive enzyme, salivary amylase. Also aiding in chemical digestion in the mouth is mucin. When in the mouth, salivary mucins functions as a protective layer.