Cited by 79Neuroendocrine regulation and behaviorNeuropeptides and Animal PhysiologyCardiovascular, Neuropeptides, and Oxidative Stress Research

[1-deamino-4-cyclohexylalanine] arginine vasopressin: a potent and specific agonist for vasopressin V1b receptors

Derick, S., Cheng, L. L., Voirol, M. J., Stoev, S., Giacomini, M., Wo, N. C., Szeto, H. H., Ben Mimoun, M. +4 more·2002·Endocrinology

Abstract

To date, there are no vasopressin (VP) agonists that exhibit a high affinity and selectivity for the VP V1b receptor with respect to the V1a, V2, and oxytocin receptors. In this study, we describe the synthesis and pharmacological properties of [1-deamino-4-cyclohexylalanine] arginine vasopressin (d[Cha4]AVP). Binding experiments performed on various membrane preparations revealed that d[Cha(4)]AVP exhibits a nanomolar affinity for V1b receptors from various mammalian species (rat, bovine, human). It exhibits high V1b/V1a and V1b/oxytocin selectivity for rat, human, and bovine receptors. Furthermore, it exhibits high V1b/V2 specificity for both bovine and human vasopressin receptors. Functional studies performed on biological models that naturally express V1b receptors indicate that d[Cha4]AVP is an agonist. Like VP, it stimulated basal and corticotropin-releasing factor-stimulated ACTH secretion and basal catecholamine release from rat anterior pituitary and bovine chromaffin cells, respectively. In vivo experiments performed in rat revealed that d[Cha4]AVP was able to stimulate both ACTH and corticosterone secretion and exhibits negligible vasopressor activity. It retains about 30% of the antidiuretic activity of VP. This long-sought selective VP V1b receptor ligand with nanomolar affinity will allow a better understanding of V1b-mediated VP physiological effects and is a promising new tool for V1b receptor structure-function studies.

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Crossref · 10.1210/en.2002-220363

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Authors
Derick, S., Cheng, L. L., Voirol, M. J., Stoev, S., Giacomini, M., Wo, N. C., Szeto, H. H., Ben Mimoun, M., Andres, M., Gaillard, R. C., Guillon, G., & Manning, M.
Affiliations
  • Inserm (FR)
  • Medical College of Ohio (L.L.C., S.S., M.M.), Department of Biochemistry and Molecular Biology, Toledo, Ohio 43614
  • Centre Hospitalier Universitaire Vaudois (CH)
  • Cornell University (US)
  • Institut National de la Santé et de la Recherche Médicale, Unité 469 (S.D., M.B.M., M.A., G.G.), 34094 Montpellier Cedex 05, France
Corresponding author
Guillon, G.
Venue
Endocrinology
Published
2002-12-01
Volume
143
Issue
12
Pages
4655-4664
ISSN
  • 0013-7227 (ISSN-L)
  • 1945-7170
OpenAlex
W2085319220
Cited by
76
References
44
Citations by year
2025: 2 · 2024: 1 · 2022: 1 · 2021: 1 · 2020: 1 · 2019: 2 · 2017: 5 · 2016: 2 · 2015: 2 · 2014: 1 · 2013: 4 · 2012: 4
FWCI
6.49
Type
journal article
Language
en
Open access
closed
Locations
  • Endocrinology (publishedVersion)
  • PubMed (publishedVersion)
  • IRIS (submittedVersion)
  • SERVAL (Université de Lausanne) (submittedVersion)
Funders
National Institute of General Medical Sciences (GM25280, R01GM025280)
Topics
  • Social Sciences › Psychology › Social Psychology › Neuroendocrine regulation and behavior
  • Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuropeptides and Animal Physiology
  • Health Sciences › Medicine › Surgery › Cardiovascular, Neuropeptides, and Oxidative Stress Research
Keywords
vasopressin V1b receptor, receptor selectivity, V1a receptor, oxytocin receptor, V2 receptor, ACTH secretion, corticotropin-releasing factor, catecholamine release, anterior pituitary, chromaffin cells, corticosterone secretion, antidiuretic activity, receptor structure-function
MeSH terms
Adrenocorticotropic Hormone, Animals, Arginine Vasopressin, Catecholamines, Cattle, Cells, Cultured, Chromaffin System, Corticosterone, Corticotropin-Releasing Hormone, Diuresis, Female, Cricetinae, Humans, Pituitary Gland, Anterior, Transfection, Gene Expression, CHO Cells, Rats, Wistar, Receptors, Vasopressin, Receptors, Oxytocin, Rats

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