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Stimulates the Raf/MEK1/Mitogen-Activated Protein Kinase Signaling Cascade in Bovine Luteal Cells1
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
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. 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 (1 µM) and the pharmacological PKC
activator phorbol myristate acetate (PMA, 20 nM). Kinetic
analysis revealed that PGF2 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 (1 µM)
and PMA (20 nM). Additionally, both PGF2 (1
µM) and PMA (20 nM) stimulated
phosphorylation of Raf-1, MEK1, and p42mapk in
32P-labeled cells. Our data demonstrate that
PGF2 activates the Raf/MEK1/p42/44mapk
signaling cascade in bovine luteal cells and that the actions of
PGF2 are mimicked by the PKC activator PMA. Activation
of the Raf/MEK1/MAPK signaling cascade by PGF2 in luteal
cells provides a mechanism to transduce signals initiated by
PGF2 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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