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Originally published In Press as doi:10.1074/jbc.M110936200 on November 21, 2001

J. Biol. Chem., Vol. 277, Issue 5, 3293-3302, February 1, 2002
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A Calcium/Calmodulin-dependent Activation of ERK1/2 Mediates JunD Phosphorylation and Induction of nur77 and 20alpha -hsd Genes by Prostaglandin F2alpha in Ovarian Cells*

Carlos O. StoccoDagger , Lester F. Lau§, and Geula GiboriDagger

From the Dagger  Department of Physiology and Biophysics, University of Illinois College of Medicine, Chicago, Illinois 60612 and the § Department of Molecular Genetics, University of Illinois College of Medicine, Chicago, Illinois 60607

We have previously demonstrated that prostaglandin F2alpha (PGF2alpha ) induces a rapid and transient expression of Nur77 in luteal cells. We have shown that Nur77 plays an important role in ovarian physiology by mediating the PGF2alpha induction of 20alpha -HSD, a steroidogenic enzyme involved in the catabolism of progesterone. In this report we established, using luteinized granulosa cells, that PGF2alpha stimulates in vitro nur77 expression in a time- and dose-dependent manner. Serial 5'-deletion of the nur77 promoter revealed that the necessary and sufficient elements for PGF2alpha induction of Nur77 promoter activity are located between the nucleotides -86 and -33 upstream of the transcription start site, this region containing two AP1 elements. JunD binds to these AP1 sites, but its binding is not stimulated by PGF2alpha . However, mutation of the AP1 sites as well as a dominant-negative JunD abolished nur77 induction by PGF2alpha . PGF2alpha induces phosphorylation of JunD bound to the nur77 promoter. Stimulation of nur77 expression and JunD phosphorylation were prevented by inhibitors of calcium, calmodulin, or ERK1/2 kinase. PGF2alpha -induced ERK1/2 phosphorylation was prevented by calcium/calmodulin inhibitors. We conclude that activation of JunD through a calmodulim-dependent activation of ERK1/2 mediates nur77 induction by PGF2alpha . Finally, we demonstrated that this molecular mechanism also mediates 20alpha -hsd induction.

* This work was supported by National Institutes of Health Grants HD11119 and HD12356 and by Consejo Nacional de Investigaciones Científicas y Técnicas, Argentina (to C. O. S.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence and requests for reprints should be addressed: Dept. of Physiology and Biophysics (M/C 901), University of Illinois, 835 S. Wolcott Ave., Chicago, Il 60612-7342. Fax: 312-413-0159; E-mail: ggibori@uic.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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