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- W2024083623 abstract "The activity of 3-hydroxy-3-methylglutaryl coenzyme A reductase (HMG-CoA reductase, EC 1.1.1.34) was increased severalfold in the microsomes isolated from HeLa S3G cells grown in the presence of 10−6m dexamethasone. HMG-CoA reductase activity was inactivated by ATP + Mg2+. This inactivation was a function of time of incubation and ATP + Mg2+ concentration. Nevertheless dexamethasone-treated cells always showed higher activity. The inactivated enzyme was reactivated by incubation with potato acid phosphatase. Incubation of the microsomes with either purified alkaline phosphatase from intestine or HeLa cell homogenates as a source of alkaline phosphatase showed no effect on the activity of HMG-CoA reductase. ML236B, a competitive inhibitor of HMG-CoA reductase, partially inactivated the enzyme. Both in the presence and in the absence of this compound, dexamethasone-treated cells showed higher activity. However, the relative percentage inhibitions by ML236B at a fixed HMG-CoA concentration remained the same for both control and dexamethasone-treated cells. The results suggest that the increase in HMG-CoA reductase activity elicited by dexamethasone is due to the increased level of the enzyme." @default.
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- W2024083623 date "1980-08-01" @default.
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- W2024083623 title "Modulation of 3-hydroxy-3-methylglutaryl coenzyme A reductase by dexamethasone not mediated by phosphorylation and dephosphorylation" @default.
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- W2024083623 doi "https://doi.org/10.1016/0003-9861(80)90159-9" @default.
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