Highly enriched, minimally disrupted plasma membrane vesicles from aortic myocytes grown in primary culture

Phosphorylation induced by carp-dependent protein kinase was examined in a plasma membrane-enriched fraction from control and P-adrenergic-stimulated rat aortic myocytes. Phosphorylation of a 16 kDa protein which copurified with the plasma membrane marker (Nab + Kc)-ATPase was most prominent. It was decreased by pretreatment of the myocytes with isoproterenol and the effect of isoproterenol was inhibited by propranolol. Both phosphorylation induced by CAMP-dependent protein kinase and its inhibition by isoproterenoi pretreatment declined in preparations exposed to endogenous phosphatase. These results provide strong evidence that @-adrenergic stimuiation of aortic myocytes induces in situ phosphorylation of a 16 kDa plasma membrane protein.(Rat aorta)

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Highly enriched, minimally disrupted plasma membrane vesicles from aortic myocytes grown in primary culture

Cited by 2 publications

References 47 publications

A 16 kDa protein substrate for protein kinase C and its phosphorylation upon stimulation of vasopressin receptors in rat aortic myocytes

A 16 kDa protein substrate for protein kinase C and its phosphorylation upon stimulation of vasopressin receptors in rat aortic myocytes

Cyclic AMP‐dependent phosphorylation of a 16 kDa protein in a plasma membrane‐enriched fraction of rat aortic myocytes

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