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Molecular Cloning and functional characterization of v 2 [ 8-Iysine ] Vasopressin and oxytocin receptors from a pig kidney cell

[Arg8]vasopressin and oxytocin are the two main members of the neurohypophysial hormone family found to be present in nearly all mammals. [Lys]vasopressin ([Lys]VP) has been identified as the antidiuretic hormonein pig and some marsupial families. The porcine-derived kidney epithelial cell line, LLC-PK~> expresses both [Lys8]VP receptors coupled to the activation of adenylate cyclase (V 2 receptors) and oxytocin receptors. Here we report the molecular cloning of the V 2 [Lys]VP receptor and the oxytocin receptor from LLC-PK1 cells. The cloned V 2 [Lys]VP receptor differs from human and rat V 2 [Arg8] receptors mainly in its N-terminal region, in residues located in the extracellular loops and in intracellular phosphorylation sites. When expressed in COS7 cells, the V2 [Lys]VP receptor exhibits the relative order of Iigand affinity [Lys]VP = [Arg8]VP ~ 1deamino[n-Arg8]VP ~ oxytocin and adenylate~cyclase stimulation, expected for the porcine V2 [Lys8]VP receptor but different from V 2 [Arg8]VP receptors. Adenylate-cyclase activation by [Lys8]VP was inhibited in COS7 cells by a V 2 antagonist. The cloned oxytocin receptor exhibits in COS7 cells a ligand specificity typical of mammalian oxytocin receptors. mRNA-distribution analysis revealed a single 5.5-kb transcript in the uterus from pregnant guinea pig.