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・ Lysophosphatidylethanolamine
・ Lysophosphatidylinositol
・ Lysophosphatidylserine
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・ Lysophospholipid receptor
・ Lysopteryx
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・ Lysosomal alpha-glucosidase
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・ Lysosomal Pro-X carboxypeptidase
・ Lysosomal storage disease
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Lysosome
・ Lysosome-associated membrane glycoprotein
・ Lysostaphin
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Lysosome : ウィキペディア英語版
Lysosome

A lysosome (derived from the Greek words ''lysis'', meaning "to loosen", and ''soma'', "body") is a membrane-bound cell organelle found in most animal cells (they are absent in red blood cells). Structurally and chemically, they are spherical vesicles containing hydrolytic enzymes capable of breaking down virtually all kinds of biomolecules, including proteins, nucleic acids, carbohydrates, lipids, and cellular debris. They are known to contain more than 50 different enzymes, which are all optimally active at an acidic environment of about pH 4.5 (about the pH of black coffee). Thus lysosomes act as the waste disposal system of the cell by digesting unwanted materials in the cytoplasm, both from outside of the cell and obsolete components inside the cell. For this function they are popularly referred to as "suicide bags" or "suicide sacs" of the cell.〔(【引用サイトリンク】url=http://medcell.med.yale.edu/histology/keyword.cgi?keyword=lysosome )〕 Furthermore, lysosomes are responsible for cellular homeostasis for their involvements in secretion, plasma membrane repair, cell signalling and energy metabolism, which are related to health and diseases. Depending on their functional activity, their sizes can be very different—the biggest ones can be more than 10 times bigger than the smallest ones. They were discovered and named by Belgian biologist Christian de Duve, who eventually received the Nobel Prize in Physiology or Medicine in 1974.
Enzymes of the lysosomes are synthesised in the rough endoplasmic reticulum. The enzymes are released from Golgi apparatus in small vesicles which ultimately fuse with acidic vesicles called endosomes, thus becoming full lysosomes. In this process, the enzymes are specifically tagged with the molecule mannose 6-phosphate to differentiate them from other enzymes. Lysosomes are interlinked with three intracellular processes, namely phagocytosis, endocytosis and autophagy. Extracellular materials such as microorganisms taken up by phagocytosis, macromolecules by endocytosis, and unwanted cell organelles are fused with lysosomes in which they are broken down to their basic molecules. Thus lysosomes are the recycling units of a cell.
Synthesis of lysosomal enzymes is controlled by nuclear genes. Mutations in the genes for these enzymes are responsible for more than 30 different human genetic diseases, which are collectively known as lysosomal storage diseases. These diseases are due to deficiency in a single lysosomal enzyme, that prevents breakdown of target molecules; consequently the undegraded materials accumulate within the lysosomes and often giving rise to severe clinical symptoms. Further, such genetic defects are related to several neurodegenerative disorders, cancer, cardiovascular diseases, and ageing-related diseases.
==Discovery==

Christian de Duve, then 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 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 a 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.

抄文引用元・出典: フリー百科事典『 ウィキペディア(Wikipedia)
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