Molecular characterization of a cloned human oxytocin receptor
Abstract
Kimura T, Makino Y, Saji F, Takemura M, Inoue T, Kikuchi T, Kubota Y, Azuma C, Nobunaga T, Tokugawa Y, Tanizawa O. Molecular characterization of a cloned human oxytocin receptor. Eur J Endocrinol 1994;131:385–90. ISSN 0804–4643 We describe here the binding and functional properties of a cloned human oxytocin receptor (OTR). We established a transient OTR expression system on COS-1 cells, which do not express vasopressin receptors. With the transfected cells and [ 3 H]oxytocin, the dissociation constant (K d ) of OTR to oxytocin was 6.0 ±1.1 nmol/l; the binding properties of several oxytocin-related peptides were also examined. The functional properties of OTR were determined by an electrophysiological method, using a Xenopus laevis oocyte injected with in vitro transcribed OTR mRNA. These two methods showed that [Phe 2 ,Orn 8 ]vasotocin, a vasopressin agonist, was an OTR antagonist. A combination of these methods using cloned OTR cDNA is a novel and effective method for the investigation of oxytocin-related ligands. Tadashi Kimura, Department of Obstetrics and Gynecology, Osaka University Medical School, 2-2 Yamadaoka, Suita City, Osaka 565, Japan
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There can be differences of around 10-100 fold in the selectivity of OTRs and AVP receptors for OT and AVP.
“Nevertheless, it appears that there can be differences of around 10–100 fold in the selectivity of OTRs and AVP receptors for OT and AVP.”
From Cross-talk among oxytocin and arginine-vasopressin receptors: Relevance for basic and clinical studies of the brain and periphery (2018) · cites this paper as [30]
AVP has similar affinity for OTRs, V1aRs, and V1bRs, whereas OT may have a higher affinity for OTRs than for V1aRs or V1bRs.
“AVP has a similar affinity for OTRs, V1aRs, and V1bRs while OT may have a higher affinity for OTRs than V1aRs or V1bRs [28; 29; 30; 31; 32; 33].”
From Cross-talk among oxytocin and arginine-vasopressin receptors: Relevance for basic and clinical studies of the brain and periphery (2018) · cites this paper as [30]
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Navarro, Y., & Thelma, N. (2010)
- Authors
- Kimura, T., Makino, Y., Saji, F., Takemura, M., Inoue, T., Kikuchi, T., Kubota, Y., Azuma, C., Nobunaga, T., Tokugawa, Y., & Tanizawa, O.
- Affiliations
- Osaka University Hospital (JP)
- Rohto Pharmaceutical (Japan) (JP)
- Corresponding author
- Kimura, Tadashi
- Venue
- European Journal of Endocrinology
- Publisher
- Oxford University Press (OUP)
- Published
- 1994-10
- Volume
- 131
- Issue
- 4
- Pages
- 385-390
- ISSN
- 0804-4643 (ISSN-L)
- 1479-683X
- OpenAlex
- W2037835851
- Cited by
- 77
- References
- 0
- Citations by year
- 2026: 2 · 2024: 1 · 2023: 4 · 2022: 2 · 2021: 1 · 2020: 6 · 2019: 2 · 2018: 3 · 2017: 5 · 2016: 1 · 2015: 1 · 2014: 2 · 2013: 2 · 2012: 5
- FWCI
- 7.77
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- European Journal of Endocrinology (publishedVersion)
- PubMed (publishedVersion)
- 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
- oxytocin receptor, receptor cloning, ligand binding, dissociation constant, arginine vasotocin, receptor function, COS-1 cells
- MeSH terms
- Animals, Cell Line, Cloning, Molecular, DNA, Female, Humans, Oocytes, RNA, Messenger, Tritium, Xenopus laevis, Receptors, Oxytocin
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