A lysosome is a membrane-bound cell organelle that contains digestive enzymes. Lysosomes are involved with various cell processes. They break down excess or worn-out cell parts. They may be used to destroy invading viruses and bacteria. If the cell is damaged beyond repair, lysosomes can help it to self-destruct in a process called programmed cell death, or apoptosis. Now, the lysosome is a specific type of organelle that’s very acidic. So that means that it has to be protected from the rest of the inside of the cell. It’s a compartment, then, that has a membrane around it that stores the digestive enzymes that require this acid, low-pH environment. Those enzymes are called hydrolytic enzymes, and they break down large molecules into small molecules. For example, large proteins into amino acids, or large carbohydrates into simple sugars, or large lipids into single fatty acids. And when they do that, they provide for the rest of the cell the nutrients that it needs to… So, for example, if you can’t do that, it can’t break down large molecules into small molecules. You’ll have storage of those large molecules, and this is a disease. There’s also another type of lysosome storage disease in which the small molecules that are produced from those large molecules can’t get out of the lysosome. They’re stored there because the transporters for moving these small molecules out are missing genetically. And finally, one other function of the lysosome is to ingest bacteria so that the bacteria can be destroyed. So the lysosomes also provide a function against infection, and the cell will often engorge a bacterium and put it into its lysosome for destruction. So here’s an important organelle that has function against infection and function in a way in nutrition to break down large molecules into small molecules so that they can be reutilized.
Function and structure:
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. 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.
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.
TEM views of various vesicular compartments. Lysosomes are denoted by “Ly”. They are dyed dark due to their acidity; in the center of the top image, a Golgi Apparatus can be seen, distal from the cell membrane relative to the lysosomes.
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 hormoneinsulin 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 standardised 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.”
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. 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. 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. However, it has since been concluded that they only play a minor role in cell death.