[Heterogeneity of protein metabolism and activities of certain enzymes in functionally different structures of nerve tissue].
The article deals with a review of the results of studies conducted at the department which evidence for inhomogeneity of localization, composition and different intensity of intravital renewal of proteins as well as for different activity of some enzymes most important for the nervous system functions in the macro- and microstructural formation of the nerve tissue. On the basis of the experimental data concerning the presence in the nerve tissue of a wide range of rates for intravital renewal of proteins in the structures of different functions as well as of those concerning subcellular and suborganoid localization of intracellular peptid-hydrolases, a conclusion is drawn that catabolism of the protein molecules occurs mainly on the cell membrane structures. The effect of acid peptide-hydrolases is chiefly manifested in the died and damaged cells and neutral ones in the intact functioning cells. As among the proteins most important functionally for the nervous activity ATP-hydrolyzing enzymes occupy a special place, the article provides basic data of studies in the ATPase activity in the nervous tissue, intracellular localization of the enzyme, its sensitivity to uni- and bivalent ions, as well as in the mechanism of interaction with ouabain--specific inhibitor and with melipramine--neurotropic substance.
D000251:Adenosine Triphosphatases / Q000378:metabolism; D000818:Animals; D002413:Cations, Divalent; D002414:Cations, Monovalent; D009419:Nerve Tissue Proteins / Q000378:metabolism*; D009420:Nervous System / Q000187:drug effects / Q000378:metabolism*; D009928:Organ Specificity; D010042:Ouabain / Q000494:pharmacology; D010447:Peptide Hydrolases / Q000378:metabolism
D002413:Cations, Divalent; D002414:Cations, Monovalent; D009419:Nerve Tissue Proteins; D010042:Ouabain; D010447:Peptide Hydrolases; D000251:Adenosine Triphosphatases