[Effect of age, different light conditions, melatonin, and epitalon on lysosomal proteinase activity in the liver and kidneys of rats].
Ageing, melatonin, epithalon (tetrapeptide Ala-Glu-Asp-Gly) and different light conditions effects on protein content and cathepsins B and D activities in rat liver and kidneys lysosomal fractions were studied. Ageing leads to decrease of cathepsins activity in rat liver lysosomal fractions. Constant light and darkness conditions result in earlier age decline of cathepsins activity. Absence of day and night succession in comparison with alternating light conditions causes decline of both general and specific cathepsin D activity. Melatonin and epithalon administration resulted in decrease of cathepsin D activity in liver only under control interchangeable light conditions. Cathepsin B activity in liver and kidneys lysosomal fractions declined in all experimental light conditions. Cathepsins activity decrease under the influence of epiphysial factors is evidently connected with their inhibitory effect on protein and general metabolism.
Rendakov
N L
NL
Tiutiunnik
N N
NN
Vinogradova
I A
IA
D000375:Aging / Q000187:drug effects / Q000378:metabolism / Q000528:radiation effects; D000818:Animals; D005260:Female; D007668:Kidney / Q000187:drug effects / Q000201:enzymology* / Q000528:radiation effects; D008027:Light; D008099:Liver / Q000187:drug effects / Q000201:enzymology* / Q000528:radiation effects; D008247:Lysosomes / Q000187:drug effects / Q000201:enzymology* / Q000528:radiation effects; D008297:Male; D008550:Melatonin / Q000494:pharmacology*; D009842:Oligopeptides / Q000494:pharmacology*; D010447:Peptide Hydrolases / Q000378:metabolism*; D051381:Rats; D011919:Rats, Inbred Strains
D009842:Oligopeptides; D010447:Peptide Hydrolases; D008550:Melatonin; C421253:alanyl-glutamyl-aspartyl-glycine