Nature and properties of human platelet vasopressin receptors

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Abstract
The binding of 3H-labelled [8-arginine]vasopressin to human platelets or crude platelet membranes was examined. Both preparations specifically bound [8-arginine]vasopressin. The binding increased linearly with protein concentration, it was temperature- and time-dependent, saturable and could be reversed to a large extent by EDTA (10 mM). In this latter case, addition of an excess of MgCl2 (20mM) restored the initial level of binding. Intact platelets and membranes derived from these platelets presented a single population of binding sites with a dissociation constant (Kd) of 1.3 .+-. 0.2 and 1.8 .+-. 0.3 nM and a maximal binding capacity of 142 .+-. 48 and 270 .+-. 17 fmol/mg of protein, respectively. The Kd values of various analogues correlated well with those determined on rat liver membrane V1 vasopressin receptors but not with those determined on rat kidney membrane V2 receptors.