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Endocrinology Vol. 139, No. 9 3876-3885
Copyright © 1998 by The Endocrine Society

ARTICLES

Prostaglandin F2{alpha} Stimulates the Raf/MEK1/Mitogen-Activated Protein Kinase Signaling Cascade in Bovine Luteal Cells1

Dong-bao Chen2, Suzanne D. Westfall, Hon W. Fong, Mark S. Roberson and John S. Davis

The Women’s Research Institute, Departments of Obstetrics and Gynecology and Internal Medicine, University of Kansas School of Medicine-Wichita (D.-b.C., H.W.F., J.S.D.), and the Research Service of the Department of Veterans Affairs (S.D.W., J.S.D.), Wichita, Kansas 67214; and the Department of Physiology, Cornell University (M.S.R.), Ithaca, New York 14853

Address all correspondence and requests for reprints to: John S. Davis, Ph.D., The Women’s Research Institute, Department of Obstetrics and Gynecology, University of Kansas School of Medicine-Wichita, 1010 North Kansas, Wichita, Kansas 67214. E-mail: jdavis3{at}kumc.edu

Upon binding to its G protein-coupled transmembrane receptors, the actions of PGF2{alpha} on the corpus luteum are initiated by the phospholipase C/diacylglycerol-inositol 1,4,5-trisphosphate (InsP3)/Ca2+-protein kinase C (PKC) pathway. However, little is known about the downstream intracellular signaling events that can lead to transcriptional activation in response to PGF2{alpha}. The present study was conducted to examine the involvement of the mitogen-activated protein kinase (MAPK) signaling cascade in the corpus luteum. Three isoforms of the Raf family of oncoprotein kinases (A-Raf, B-Raf, and Raf-1 or c-Raf) were detected in bovine luteal cells. Raf-1 and B-Raf, but not A-Raf, were activated by PGF2{alpha} (1 µM) and the pharmacological PKC activator phorbol myristate acetate (PMA, 20 nM). Kinetic analysis revealed that PGF2{alpha} rapidly and transiently activated Raf-1. In vitro protein kinase assays demonstrated that activation of Raf-1 and B-Raf resulted in the phosphorylation and activation of MAPK kinase (MEK1), which subsequently phosphorylated p42mapk. As determined by hyperphosphorylation, tyrosine phosphorylation, and enzymatic activity, p42mapk and p44 mapk were rapidly and transiently activated by both PGF2{alpha} (1 µM) and PMA (20 nM). Additionally, both PGF2{alpha} (1 µM) and PMA (20 nM) stimulated phosphorylation of Raf-1, MEK1, and p42mapk in 32P-labeled cells. Our data demonstrate that PGF2{alpha} activates the Raf/MEK1/p42/44mapk signaling cascade in bovine luteal cells and that the actions of PGF2{alpha} are mimicked by the PKC activator PMA. Activation of the Raf/MEK1/MAPK signaling cascade by PGF2{alpha} in luteal cells provides a mechanism to transduce signals initiated by PGF2{alpha} receptors on the cell surface into the nucleus. Activation of the Raf/MEK1/MAPK signaling cascade may be associated with transcriptional activation of luteal genes possessing activator protein-1-binding sites.




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