[Mechanism of the stimulating effect of estradiol on protein kinase C in plasma membranes of target cells].
Using inhibitors and activators of protein kinase C, it was demonstrated that in isolated plasma membranes of target cells estradiol-17 beta selectively stimulates protein phosphorylation by endogenous protein kinase C. In estradiol-dependent tissues, estradiol effectuates the translocation of protein kinase C from the cytosol to the membrane fraction within 10-12 minutes. Estradiol activates protein kinase C in cellular membranes of target tissues via a mechanism which is different from that of phorbol ester (TPA): 3H-estradiol, in contrast with 3H-TPA, it is not bound by protein kinase C and, in contrast with TPA, estradiol-17 beta does not activate purified protein kinase C in vitro. In this case, the specific stimulation of protein kinase C translocation to membranes and the estradiol-induced increase in the phosphorylation of plasma membrane proteins seem to be due to the estradiol-induced activation of the transmembrane system of polyphosphoinositide degradation, eventually resulting in the formation of diacylglycerol, a protein kinase C activator.
Morozova
T M
TM
Mitina
R L
RL
Rau
V A
VA
Sidorkina
O M
OM
D015127:9,10-Dimethyl-1,2-benzanthracene / Q000633:toxicity; D000818:Animals; D002462:Cell Membrane / Q000201:enzymology; D004789:Enzyme Activation; D004958:Estradiol / Q000494:pharmacology*; D005260:Female; D008325:Mammary Neoplasms, Experimental / Q000201:enzymology; D009376:Neoplasms, Hormone-Dependent / Q000201:enzymology; D011493:Protein Kinase C / Q000378:metabolism*; D051381:Rats; D011919:Rats, Inbred Strains
D004958:Estradiol; D015127:9,10-Dimethyl-1,2-benzanthracene; D011493:Protein Kinase C
Mekhanizmy stimuliruiushchego deĭstviia éstradiola na proteinkinazu C v plazmaticheskikh membranakh kletok-misheneĭ.