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Papers In Press, published online ahead of print November 21, 2001
Department of Physiology and Biophysics, University of Illinois at Chicago, Chicago, IL 60612
Corresponding Author: ggibori{at}uic.edu
We have previously demonstrated that PGF2a 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 PGF2a induction of 20a-HSD, a steroidogenic enzyme involved in the catabolism of progesterone. In this report we established, using luteinized granulosa cells, that PGF2a 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 PGF2a-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 PGF2a. However, mutation of the AP1 sites as well as a dominant-negative JunD abolished nur77 induction by PGF2a. PGF2a 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. PGF2a-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 PGF2a. Finally, we demonstrated that this molecular mechanism also mediates 20a-hsd induction.
J. Biol. Chem, 10.1074/jbc.M110936200
Submitted on November 15, 2001
Revised on November 21, 2001
Accepted on November 21, 2001
A calcium/calmodulin dependent activation of ERK1/2 mediates JunD phosphorylation and induction of nur77 and 20a-hsd genes by PGF2a in ovarian cells
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