Interaction of a vasopressin antagonist with vasopressin receptors in the septum of the rat brain

Interaction of a vasopressin antagonist with vasopressin receptors in the septum of the rat brain The ability of d(CH2)5‐Tyr(Me)‐arginine‐8‐vasopressin, an antagonist of peripheral pressoric (V1‐type) vasopressin receptors, to label vasopressin binding sites in the septum of the rat brain was evaluated. Using crude membrane preparations from the septum, 3H‐arginine‐8‐vasopressin (AVP) specifically labels a single class of binding sites with a Kd of 2.9nM and maximum binding site concentration of 19.8 fmole/mg protein. 3H‐Antag also labels a single class of membrane sites but with higher affinity (Kd=0.47nM) and lower capacity (10.1 fmole/mg protein) than 3H‐AVP. The rank order of potency of various competitor peptides for 3H‐AVP and 3H‐Antag binding was similar. Oxytocin was 100–1,000 fold less potent than AVP in competing for binding with both ligands. 3H‐AVP and 3H‐Antag showed similar labeling patterns when incubated with septal tissue slices. Unlabeled Antag also effectively antagonized vasopressin‐stimulated phosphatidylinositol hydrolysis in septal tissue slices. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Synapse Wiley

Interaction of a vasopressin antagonist with vasopressin receptors in the septum of the rat brain

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Publisher
Wiley
Copyright
Copyright © 1988 Alan R. Liss, Inc.
ISSN
0887-4476
eISSN
1098-2396
DOI
10.1002/syn.890020306
pmid
2975069
Publisher site
See Article on Publisher Site

Abstract

The ability of d(CH2)5‐Tyr(Me)‐arginine‐8‐vasopressin, an antagonist of peripheral pressoric (V1‐type) vasopressin receptors, to label vasopressin binding sites in the septum of the rat brain was evaluated. Using crude membrane preparations from the septum, 3H‐arginine‐8‐vasopressin (AVP) specifically labels a single class of binding sites with a Kd of 2.9nM and maximum binding site concentration of 19.8 fmole/mg protein. 3H‐Antag also labels a single class of membrane sites but with higher affinity (Kd=0.47nM) and lower capacity (10.1 fmole/mg protein) than 3H‐AVP. The rank order of potency of various competitor peptides for 3H‐AVP and 3H‐Antag binding was similar. Oxytocin was 100–1,000 fold less potent than AVP in competing for binding with both ligands. 3H‐AVP and 3H‐Antag showed similar labeling patterns when incubated with septal tissue slices. Unlabeled Antag also effectively antagonized vasopressin‐stimulated phosphatidylinositol hydrolysis in septal tissue slices.

Journal

SynapseWiley

Published: Jan 1, 1988

References

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