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Activation fosfolipaz

Fosfolipazy katalizirujut hydrolysis fosfolipidov, a part cellular membranes. These enzimy are widely presented in various cells. Researchers give special attention fosfolipazam À2 - group of the lipases which basic function consists at a distance of a membrane damaged fosfolipidov, by liberation of fat acids, podvergshihsja peroksidatsii.

Fosfolipazy À2 are Ca 2 + - and kalmodulin-dependent enzimami, and, hence, sensitive to calcium rising in a cytoplasma. Stimulation fosfolipazy calcium leads to destruction intensifying fosfolipidov membranes and to damage of cells. Rising of the maintenance of calcium in a cytoplasma, activation fosfolipazy, turn acceleration fosfolipidov with the subsequent  destruction of hepatocytes registered at a toxic lesion of a liver four-chloride Carboneum. Similar changes observed in cardiomyocytes and hepatocytes, inkubiruemyh in the conditions of an anoxia. Chlorpromazinum oppressing activity fosfolipaz, protects cells from damaging action tsiototoksikantov, breaking an intracellular homeostasis of calcium. These and other data confirm value of the surveyed mechanism in development of toxic damage of cells.


1.4.4. Activation of proteases

To number of proteases, with an optimum of activity in the field of neutral value rn, concern: ATF-DEPENDENT, ubikvitin-dependent, Sa 2 + _ dependent (kalpainy) proteases. Kalpainy are present practically at all cells of mammals. They are localised out of lysosomes, in membranous structures in the form of an inactive complex with ingibitornymi proteins (kalpastatiny). The basic functions kalpainov - a reparation of a cytoskeleton and cellular membranes, destruction of receptor proteins and their updating, activation of some enzimov, participation in mitosis processes.

1.4.5.

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Scientific source INGA MAMUCHISHVILI. INTERRELATION STRESS-INDUCED of DISTURBANCES In nejrogumoralnoj to SYSTEM And SYSTEM of POWER SUPPLY At TEENAGERS. The DISSERTATION on competition of a scientific degree of the doctor of medical sciences. Tbilisi - 2006. 2006

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