Zammit V A, Caldwell A M
Hannah Research Institute, Ayr, Scotland, U.K.
Biochem J. 1991 Jan 15;273(Pt 2)(Pt 2):485-8. doi: 10.1042/bj2730485.
The roles of protein kinase C, Ca2+/calmodulin-dependent protein kinase and AMP-activated protein kinase in the phosphorylation of 3-hydroxy-3-methylglutaryl-CoA (HMG-CoA) reductase induced by Ca2(+)-mobilizing conditions in isolated hepatocytes were investigated. Only partial evidence for the involvement of AMP-activated kinase was found. Antagonism of calmodulin action prolonged the decrease in expressed/total activity ratio induced by vasopressin plus glucagon. Protease inhibitors active against Ca2(+)-dependent cytosolic proteases or lysosomal proteolysis did not attenuate the loss of total HMG-CoA reductase induced by glucagon plus vasopressin, but calmodulin antagonists largely prevented this effect.
研究了蛋白激酶C、钙/钙调蛋白依赖性蛋白激酶和AMP激活的蛋白激酶在分离的肝细胞中由钙离子动员条件诱导的3-羟基-3-甲基戊二酰辅酶A(HMG-CoA)还原酶磷酸化过程中的作用。仅发现了关于AMP激活激酶参与的部分证据。钙调蛋白作用的拮抗作用延长了血管加压素加胰高血糖素诱导的表达/总活性比值的降低。对钙离子依赖性胞质蛋白酶或溶酶体蛋白水解有活性的蛋白酶抑制剂并未减弱胰高血糖素加血管加压素诱导的总HMG-CoA还原酶的损失,但钙调蛋白拮抗剂在很大程度上阻止了这种作用。