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Am J Physiol Endocrinol Metab 274: E634-E641, 1998;
0193-1849/98 $5.00
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Vol. 274, Issue 4, E634-E641, April 1998

ERK2 mediates oxytocin-stimulated PGE2 synthesis

Zuzana Strakova1, John A. Copland1, Stephen J. Lolait2, and Melvyn S. Soloff1,3

1 Department of Obstetrics and Gynecology and 3 Sealy Center for Molecular Science, University of Texas Medical Branch, Galveston, Texas 77555-1062; and 2 Department of Medicine, Dorothy Crowfoot Hodgkin Laboratories, Bristol Royal Infirmary, Bristol BS2 8HW, United Kingdom

Oxytocin (OT) induces PG synthesis by both uterine endometrial and amnion cells. We showed previously that CHO cells stably transfected with the rat oxytocin receptor (CHO-OTR cells) also synthesize PGE2 in response to OT. In the present work we have demonstrated that OTRs are coupled to both Gi and Gq/11, using immunoprecipitation of solubilized OTR complexes and ADP ribosylation. OT treatment caused the rapid phosphorylation of extracellular signal-regulated protein kinase 2 (ERK2 or p42MAPK), which was partially inhibited by pertussis toxin (PTX), consistent with OTR-Gi coupling. The PTX-insensitive portion of ERK2 phosphorylation was linked to Gq, as inhibitors of both phospholipase C (U-73122) and protein kinase C (GF-109203X) blocked OT-induced ERK2 phosphorylation. OT-stimulated c-fos expression was also mediated by ERK2 phosphorylation. The ERK-c-fos pathway has been shown to be associated with cell proliferation, but OT had no effect on [3H]thymidine uptake by CHO-OTR cells. However, inhibition of OT-induced ERK2 phosphorylation with an ERK kinase inhibitor (PD-98059) markedly reduced OT-stimulated PGE2 synthesis, pointing to the importance of ERK2 activation in OT action.

mitogen-activated protein kinase, prostaglandin E2, oxytocin receptor, G proteins, protein kinase C


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