Abstract
Incubation of rat hepatocytes with 10 mM mevalonate produces a decrease in HMG-CoA reductase activity and in the rate of synthesis of both monomeric and dimeric HMG-CoA reductase, and an increase in the rate of degradation of the monomeric form without significant change in that of the dimeric form. Since mevalonate promotes a short-term phosphorylation of the monomeric form without affecting the dimeric form, it is suggested that the mechanism of degradation of reductase is controlled by its phosphorylation state.
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