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- W2040576441 abstract "The regulation of and the intracellular events following α1-adrenergic receptor stimulation of myocardium are not completely understood. The α1-adrenergic stimulation of phosphoinositide breakdown was examined in a culture of neonatal rat ventricular myocytes and the influence of a protein kinase C activator, phorbol 12-myristate 13-acetate, on this process was studied. Inositolphosphate accumulation was stimulated by phenylephrine (EC50 5 μm) in the presence of 10 mm LiCl. The increase was antagonized by prazosin (10−6 m) but not by propranolol (10−6 m). The rate of inositolphosphate accumulation after prolonged α1-adrenoceptor stimulation decreased without clear evidence of depletion of the membrane phosphatidylinositolbisphosphate pool. Phorbol ester treatment (IC50 10−8 m) led to a dose-dependent inactivation of α1-adrenoceptor stimulated phosphoinositide breakdown. These findings provide evidence that protein kinase C plays a role in the regulation of α1-adrenoceptor sensitivity." @default.
- W2040576441 created "2016-06-24" @default.
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- W2040576441 date "1989-07-01" @default.
- W2040576441 modified "2023-10-16" @default.
- W2040576441 title "Phorbolester inhibits α1-adrenoceptor mediated phosphoinositide breakdown in cardiomyocytes" @default.
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- W2040576441 doi "https://doi.org/10.1016/0022-2828(89)90607-x" @default.
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