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Endocrinology Vol. 139, No. 3 1208-1212
Copyright © 1998 by The Endocrine Society

ARTICLES

Demonstration of a Relaxin Receptor and Relaxin-Stimulated Tyrosine Phosphorylation in Human Lower Uterine Segment Fibroblasts1

Smita Palejwala, Daniel Stein, Andrea Wojtczuk, Gerson Weiss and Laura T. Goldsmith

Department of Obstetrics and Gynecology, New Jersey Medical School, Newark, New Jersey 07103

Address all correspondence and requests for reprints to: Dr. Laura T. Goldsmith, Department of Obstetrics and Gynecology, New Jersey Medical School, 185 South Orange Avenue, Newark, New Jersey 07103.

To elucidate the mechanism of relaxin action, we studied the binding characteristics of human relaxin and its effects on intracellular concentrations of cAMP and tyrosine phosphorylation of cellular proteins in a model system of human cervix, human lower uterine segment fibroblasts. Human relaxin labeled with 125I bound specifically to a single class of high-affinity relaxin binding sites, distinct from insulin receptors, with a mean (±SEM) dissociation constant (Kd) of 4.36 ± 1.7 x 10-9 M and a mean of 3220 ± 557 binding sites per cell in human lower uterine segment fibroblasts. Relaxin, in quantities that were shown previously to stimulate intracellular levels of cAMP in other cell types, had no effect on intracellular levels of cAMP in human lower uterine segment fibroblasts even in the presence of the phosphodiesterase inhibitor 3-isobutyl-1-methyl-xanthine (IBMX). Incubation of the cells with relaxin caused a significant increase in tyrosine phosphorylation of a protein with an apparent Mr of approximately 220 kDa in these cells. In concert with results of recent studies that demonstrated that the Mr of the relaxin receptor is approximately 220 kDa, our data suggest that the phosphorylated protein is likely to be the relaxin receptor.




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