Characterization and localization of 3H-arginine8-vasopressin binding to rat kidney and brain tissue.

Anatomic, behavioral and pharmacologic evidence suggests that arginine8-vasopressin (AVP) serves as a CNS neurotransmitter or neuromodulator. We have characterized AVP binding to membrane and tissue slice preparations from brain and kidney, and examined the anatomical distribution of these binding sites. Conditions for the binding assay were optimized using kidney medullary tissue. Binding of 3H-AVP (S.A. = 30-51 Ci/mmol, NEN) to brain and kidney membranes and tissue slices was saturable, temperature dependent, linearly related to protein concentration (or number of tissue slices), reversible, and specific since the ability of cold AVP to displace 3H-AVP from binding was greater than oxytocin and other related peptide fragments. Autoradiographic localization of 3H-AVP binding was restricted to kidney medullary tissue. In brain tissue, 3H-AVP binding was found to occur in concentrated foci. Brainstem areas such as the nucleus tractus solitarius (NTS) showed a high density of AVP binding sites. Since local injections of AVP into the NTS have been shown to influence blood pressure, the present study presents the first anatomical evidence for the presence of AVP specific binding sites which might mediate this effect.