Abstract
Both oxytocin (OT) and [Arg 8]vasopressin (AVP) are found within the ovine pineal gland and may function to modulate melatonin secretion. However, the receptors which mediate the actions of these peptides have yet to be characterised. Preliminary studies of ovine pineal microsomal cell membranes showed binding of [ 3H]OT (79±9 fmol/mg) 10 times greater than binding of [ 3H]AVP (8±3 fmol/mg). Saturation studies using either [ 3H]OT or the selective OT receptor ligand [ 125I]d(CH 2) 5[Tyr(Me) 2,Thr 4,Orn 8,Tyr-NH 2 9]-vasotocin (OTA) revealed high affinity, single site kinetics ( K d=1.72±0.32 nM; B max=68±18 fmol/mg). Binding of [ 3H]AVP was more effectively displaced by OT than AVP, suggesting that binding may be due to cross-reaction with the OT binding site. Displacement of [ 3H]OT using a range of selective agonists and antagonist analogues revealed pharmacological characteristics similar to [ 3H]OT binding sites in the ovine and rat uterus. These data show that the ovine pineal expresses a high density of OT binding sites which may participate in the regulation of melatonin secretion.
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