Autodegradation of rat liver proteasomes (large multicatalytic proteinase complexes).
Purified proteasomes (large multicatalytic proteinase complexes) were found to be very stable, showing no change in activities or structures during prolonged incubation in medium of pH 7.5 at 37 degrees C. However, on addition of urea they were degraded autocatalytically in a time- and dose-dependent manner, suggesting that destruction of the proteasomal complexes acts as a signal for their autolysis. ATP at a physiological concentration greatly stimulated the urea-dependent breakdown of proteasomes. The autolysis induced by urea was almost completely inhibited by hemin, but not by other protease inhibitors tested, such as leupeptin, chymostation and Ep-475. Thus, autolytic degradation of proteasomes appears to be important for the regulation of enzyme levels in eukaryotic cells.
Tanaka
K
K
Institute for Enzyme Research, University of Tokushima, Japan.
Ichihara
A
A
D000255:Adenosine Triphosphate / Q000494:pharmacology; D000818:Animals; D002384:Catalysis; D003546:Cysteine Endopeptidases / Q000378:metabolism*; D066298:In Vitro Techniques; D008099:Liver / Q000201:enzymology*; D008970:Molecular Weight; D009097:Multienzyme Complexes / Q000302:isolation & purification / Q000378:metabolism*; D011480:Protease Inhibitors / Q000494:pharmacology; D046988:Proteasome Endopeptidase Complex; D051381:Rats; D014508:Urea / Q000494:pharmacology
D009097:Multienzyme Complexes; D011480:Protease Inhibitors; D000255:Adenosine Triphosphate; D014508:Urea; D003546:Cysteine Endopeptidases; D046988:Proteasome Endopeptidase Complex