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- W2091617340 abstract "The interaction between cardiac α1-adrenoceptors and GTP-binding regulatory proteins was characterized in isolated rabbit cardiac myocytes (thereby avoiding interference by other cell types present in the myocardium) by examining the α1-adrenergic stimulation of GTPase activity in sarcolemma-enriched membrane fractions. Stimulation of membrane-associated GTPase activity in both atrial and ventricular myocyte preparations by the α1-adrenergic agonists 1-noradrenaline and methoxamine (in the presence of propranolol) was observed to be both linear with time and saturable. α1-adrenergic stimulation did not change the Km for GTP (0.14–0.21 μM), but increased the Vmax by 39% and 72% above basal levels in atrial and ventricular membranes, respectively. Stimulation of GTPase activity by α1-agonists occurred in a concentration-dependent fashion and was blocked in the presence of the α-adrenoceptor antagonists phentolamine and prazosin, but not yohimbine. Prior treatment of myocytes with pertussis toxin had no effect on the α1-adrenergic stimulation of GTPase activity, but inhibited stimulation by muscarinic-receptor activation with carbachol. Finally, photoaffinity labelling of an approximately 75-kDa membrane-bound protein with [α-32P]GTP was enhanced in the presence of the α1-agonist methoxamine and abolished by addition of excess nonlabelled GTP, suggesting that this GTP-binding protein may interact with cardiac α1-adrenoceptors; a similar GTP-binding protein which may be coupled to α1-adrenoceptors has been reported in rat liver plasma membranes (Im, M. J. & Graham, R. M. (1990) J. Biol. Chem. 265, 18944–18951)." @default.
- W2091617340 created "2016-06-24" @default.
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- W2091617340 date "1993-04-01" @default.
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- W2091617340 title "Cardiac alpha1-adrenoceptors stimulate a high-affinity GTPase activity in sarcolemmal membranes from rabbit atrial and ventricular myocytes" @default.
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- W2091617340 doi "https://doi.org/10.1111/j.1432-1033.1993.tb17733.x" @default.
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