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J. Biol. Chem., Vol. 277, Issue 5, 3293-3302, February 1, 2002
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From the We have previously demonstrated that
prostaglandin F2
A Calcium/Calmodulin-dependent Activation of ERK1/2
Mediates JunD Phosphorylation and Induction of nur77 and
20
-hsd Genes by Prostaglandin F2
in
Ovarian Cells*
,¶
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
(PGF2) 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 PGF2 induction of 20
-HSD, a steroidogenic enzyme
involved in the catabolism of progesterone. In this report we
established, using luteinized granulosa cells, that PGF2
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 PGF2 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
PGF2. However, mutation of the AP1 sites as well as a
dominant-negative JunD abolished nur77 induction by
PGF2. PGF2 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.
PGF2-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 PGF2. Finally, we demonstrated that this molecular mechanism also mediates
20-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.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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