Eur J Endocrinol
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DOI: 10.1530/eje.0.1310385
European Journal of Endocrinology, Vol 131, Issue 4, 385-390
Copyright © 1994 by European Society of Endocrinology
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Molecular characterization of a cloned human oxytocin receptor

Tadashi Kimura, Yoko Makino, Fumitaka Saji, Masahiko Takemura, Tomoko Inoue, Tomoyuki Kikuchi, Yasue Kubota, Chihiro Azuma, Toshikatsu Nobunaga, Yoshihiro Tokugawa and Osamu Tanizawa

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 [3H]oxytocin, the dissociation constant (Kd) 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 [Phe2,Orn8]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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