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Binding of [³H]arginine vasopressin (AVP) and [³H]oxytocin to primary monolayer cultures of bovine adrenal chromaffin cells was time-dependent, and the binding sites for each peptide were specific and saturable. Studies with the V₁ AVP antagonist d(CH₂)₅Tyr(Me)²-AVP, the V₂ agonist 1-deamino-8-D-AVP and the V₂ antagonist d(CH₂)₅D-Leu²,Val⁴-AVP indicated that the AVP receptor was V₁ in specificity. Scatchard plots showed that each ligand interacted with a single high-affinity, low-capacity binding site: oxytocin dissociation constant (K_d) 0·29 ± 0·02 nmol/l, maximum binding capacity (B_max) 7·6 ± 0·2 fmol/10⁶ cells (or 4500 ± 102 sites/cell) (n = 3); AVP K_d 0·09±0·02 nmol/l, B_max 5·1±0·63 fmol/10⁶ cells (or 3050 ± 318 sites/cell) (n = 3). Although forskolin in concentrations from 1 nmol/l to 1 mmol/l stimulated cyclic AMP (cAMP) production in isolated chromaffin cells, this did not result in detectable catecholamine release. Neither AVP nor oxytocin in concentrations between 10 pmol/l and 10 µmol/l stimulated cAMP production in these cells. Vasopressin in concentrations as low as 10 pmol/l stimulated a sixfold increase in total inositol phosphates; the dose–response curve was triphasic. Oxytocin had little effect on total inositol phosphate accumulation at low concentrations, but concentrations above micromolar stimulated total inositol phosphate production approximately fourfold. There was no measurable release of catecholamines in response to either peptide. The physiological consequences of these AVP-induced changes in inositol phosphate concentrations remain to be elucidated.

Journal of Endocrinology (1989) 121, 133–139

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