Properties of the specific binding site for arginine vasopressin in rat hippocampal synaptic membranes.

A. Frances Pearlmutter

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Neuroendocrine regulation and behavior Neuroscience and Neuropharmacology Research Neuropeptides and Animal Physiology

Abstract

In a previous paper (Pearlmutter, A. F., Constantini, M. G., and Loeser, B. (1983) Peptides 4, 335-341), we have shown that saturable, high-affinity binding sites for [3H]arginine vasopressin (AVP) are located in rat brain membrane preparations. Binding was dependent upon the presence of Ni2+ and could be dissociated by EDTA. In the hippocampus, [3H]AVP binding could be localized to synaptic membranes. In this paper, we characterize in more depth the specificity of [3H]AVP binding to a crude hippocampal synaptic preparation and the metabolism of [3H]AVP in our synaptic preparation. By means of HPLC analysis we demonstrate that the radioactive material specifically bound to hippocampal synaptic membranes is intact [3H]AVP. The ability of analogues of AVP to displace the high-affinity, specific binding of [3H]AVP parallels closely the potency of these analogues to inhibit the extinction of avoidance behavior. In the presence of membrane and Ni2+, [3H]AVP has a half-life of 7 h. In the absence of Ni2+, the half-life of [3H]AVP is 1.2 h. Fractionation by high-pressure liquid chromatography of the supernatant from the incubation media not containing Ni2+ yields three peaks of radioactivity. Analysis of the biological activity of the [3H]AVP peak and the two non-AVP peaks which represent breakdown products show the following: (a) the [3H]AVP peak (52%) and peak III (8%) bind to fresh membranes and (b) peak II (40%) has no binding activity. Although Ni2+, Co2+, benzamidine, and phenanthroline can prevent [3H]AVP degradation, only Ni2+ and, to a much lesser extent, Co2+, can potentiate specific [3H]AVP binding. The results show that AVP-specific binding has properties which parallel its biological activity in behavioral assays; that, ultimately, proteolysis by membrane-bound peptidases inactivates AVP; and that Ni2+ acts both by preventing AVP breakdown and by potentiating specific binding.

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References

1976Behavioral effects of intraventricularly administered vasopressin and vasopressin fragments 1982Vasopressin excites hippocampal neurones 1981Vasopressor receptor antagonist prevents behavioural effects of vasopressin 1978Neurohypophyseal principles and memory processes 1975Neurohypophyseal hormones, analogs, and fragments: their effect on puromycin-induced amnesia.1983Proteolytic conversion of arginine-vasopressin and oxytocin by brain synaptic membranes. Characterization of formed peptides and mechanisms of proteolysis.1978Modification of conditioned behavior of rats by neurohypophyseal hormones and analogues 1981Neurohypophysial peptides design of tissue-specific agonists and antagonists

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