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Am J Physiol Endocrinol Metab 268: E825-E831, 1995;
0193-1849/95 $5.00
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AJP - Endocrinology and Metabolism, Vol 268, Issue 5 E825-E831, Copyright © 1995 by American Physiological Society

ARTICLES

Characterization of type A endothelin receptors in cultured human myometrial cells

V. Heluy, M. Breuiller-Fouche, F. Cavaille, T. Fournier and F. Ferre
Institut National de la Sante et de la Recherche Medicale Unite 361, Maternite Baudelocque, Paris, France.

The aim of the present study was to characterize endothelin (ET)-receptors in human myometrial cells in culture. 125I-labeled ET-1 binding to myometrial cells was specific and saturable, with a dissociation constant of 64.2 +/- 12.8 pM. Competition binding studies showed the following order of potency: ET-1 > ET-3, which is consistent with the presence of the ETA receptor subtype. FR-139317 and BQ-123, two ETA antagonists, both inhibited 125I-ET-1 binding. BQ-123 only elicited a partial inhibition. The fraction resistant to BQ-123 did not represent the ETB receptor subtype, since no specific 125I-ET-3 binding could be detected. ET-1 and ET-3 were found to stimulate [3H]inositol phosphate (IP) accumulation in cultured myometrial cells, with corresponding half-maximal effective concentration values of 0.26 +/- 0.04 and 87 +/- 17 nM, respectively. Both ETA antagonists inhibited ET-1-induced accumulation of [3H]IP. BQ-123 was only a partial inhibitor, whereas FR-139317 totally suppressed ET-1-stimulated production of [3H]IP. We conclude that human myometrial cells in culture exclusively possess ETA receptor subtypes coupled to phospholipase C.


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