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Different calcium-mobilizing receptors share the same guanine nucleotide-binding protein pool in hepatocytes.

High affinity binding of epinephrine to the alpha 1-adrenoceptor reflects the association of the ligand-receptor complex with a guanine nucleotide-binding protein (G protein) and thereby allows the receptor-G protein interaction to be assessed by radioligand binding methods. We have used [3H]prazosin/epinephrine competition binding to rat liver plasma membranes to examine the effects of other Ca(2+)-mobilizing hormones on the interaction between the alpha 1-adrenoceptor and its G protein. The aim of our experiments was to test whether the different Ca(2+)-mobilizing receptors in liver share the same limited pool of G proteins. [Arg8] Vasopressin (AVP) caused a concentration-dependent (EC50 = 0.49 +/- 0.03 nM) inhibition of the extent to which epinephrine formed a high affinity complex with the alpha 1-adrenoceptor; antagonist binding was unaffected by AVP. The effect of AVP was competitively antagonized (Kd = 0.27 +/- 0.10 nM) by a selective peptide antagonist of the V1 vasopressin receptor. We conclude that, in rat hepatocytes, alpha 1-adrenoceptors and V1 vasopressin receptors converge to interact with the same pool of G proteins.