Autoradiographic localization of putative arginine vasotocin receptors in the kidney of a urodele amphibian.

The distribution and characteristics of putative arginine vasotocin (AVT) receptors in the urodele amphibian kidney were investigated using in vitro quantitative autoradiography. Specific binding sites for [3H]arginine vasopressin (AVP) in the kidney of the rough-skinned newt (Taricha granulosa) were located over the glomeruli. Scatchard analysis showed that, in the range of concentrations tested (0.2 to 22 nM), [3H]AVP bound to a single class of receptors with a dissociation constant of 1.4 nM and a binding site concentration of 36.5 fmol/mg protein. Binding displacement studies showed that both AVT and AVP were potent ligands for newt kidney receptors. Two specific antagonist peptides with anti-vasopressor (V1) activity, but not anti-antidiuretic (V2) activity, in rat tissues were tested as well. Both antagonists effectively displaced [3H]AVP from receptor sites in newt kidney slices, indicating that the binding sites in this amphibian resemble the V1 subtype of mammals in ligand specificity. Localization of AVT receptors over kidney glomeruli and ligand specificity of these sites is consistent with the hypothesis that AVT may cause antidiuresis in urodele amphibians at least in part via a glomerular vasoconstricting action.