Proteolysis during in vitro-maturation of rabbit reticulocytes.
We investigated the ATP-dependent proteolysis, cytochrome oxidase and the succinate-cytochrome c-oxidoreductase in reticulocytes under different conditions of incubation in vitro at 37 degrees C. Under standard conditions the proteolysis virtually stops after 4 h. The degradation of the stroma proteins amounted to 30-65% depending on the percentage of reticulocytes. The decrease of the cytochrome oxidase amounted to 70% after 20 h of incubation. Inhibition of the cytosolic reticulocyte lipoxygenase (LOX) by the reversible inhibitor salicylhydroxamate (SHAM) leads to an inhibition of both proteolysis and cytochrome oxidase activity by about two-thirds after 20 h of incubation. In the presence of a Ca++-ionophore the rate of proteolysis was increased by 33%, while the cytochrome oxidase and succinate-cytochrome c-oxidoreductase activities both decreased more rapidly than in the control experiments.
D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D002454:Cell Differentiation; D003576:Electron Transport Complex IV / Q000378:metabolism; D066298:In Vitro Techniques; D008084:Lipoxygenase / Q000378:metabolism; D016859:Lipoxygenase Inhibitors; D008928:Mitochondria / Q000378:metabolism; D010447:Peptide Hydrolases / Q000378:metabolism*; D011817:Rabbits; D012156:Reticulocytes / Q000166:cytology / Q000378:metabolism*; D012457:Salicylamides / Q000494:pharmacology; D013384:Succinate Cytochrome c Oxidoreductase / Q000378:metabolism
D016859:Lipoxygenase Inhibitors; D012457:Salicylamides; D000255:Adenosine Triphosphate; C005703:salicylhydroxamic acid; D013384:Succinate Cytochrome c Oxidoreductase; D008084:Lipoxygenase; D003576:Electron Transport Complex IV; D010447:Peptide Hydrolases