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- W2043948615 abstract "Both isoproterenol and prostaglandin E1 increased the activation state of cyclic AMP-dependent protein kinase in cultured myocytes; however, only isoproterenol enhanced phosphorylase activity and contractile state. Following the incubation of intact myocytes with 32PO43−, 32 phosphoproteins were resolved from total cellular proteins by electrophoresis in sodium dodecyl sulfate polyacrylamide gels followed by autoradiography. Isoproterenol stimulated 32PO43− incorporated into 16 proteins, including 2 phosphoproteins not observed under control conditions. By contrast, prostaglandin E1 neither caused a measurable change in the protein phosphorylation pattern nor interfered with isoproterenol's capacity to do so. Isoproterenol stimulated myocyte protein phosphorylation in either the presence or absence of extracellular Ca2+. The results suggest that the regulation of protein phosphorylation following adenylate cyclase stimulation is: (1) an agonist-specific process and not due solely to a random accumulation of intracellular cycle AMP and activation of protein kinase; (2) the Ca2+ mobilization component of β-receptor activation does not account for the paradoxical effects of isoproterenol and prostaglandins E1; (3) activation of cyclic AMP-dependent protein kinase does not always result in an enhancement of protein phosphorylation." @default.
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- W2043948615 date "1982-01-12" @default.
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- W2043948615 title "Evidence for selective regulation of the phosphorylation of myocyte proteins by isoproterenol and prostaglandin E1" @default.
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- W2043948615 doi "https://doi.org/10.1016/0304-4165(82)90135-0" @default.
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