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This version published online on April 7, 2005
Endocrinology, doi:10.1210/en.2005-0093
A more recent version of this article appeared on July 1, 2005
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Submitted on January 24, 2005
Accepted on April 1, 2005

LH-induced ERK Activation Differently Modulates Progesterone and Androstenedione Production in Bovine Theca Cells

Kimihisa Tajima*, Kumiko Yoshii, Shin Fukuda, Makoto Orisaka, Kaoru Miyamoto, Abraham Amsterdam, and Fumikazu Kotsuji

Department of Obstetrics and Gynecology (K.T., K.Y., S.F., M.O., F.K.). and Biochemistry (K.M.), Faculty of Medical Sciences, University of Fukui, 23 Shimoaizuki, Matsuoka, Fukui 910-1193, Japan; and Departments of Molecular Cell Biology (A.A.), Weizmann Institute of Science, Rehovot 71600, Israel

* To whom correspondence should be addressed. E-mail: kimihisa{at}fmsrsa.fukui-med.ac.jp.

It has been reported that gonadotropins promoted phosphorylation of extracellular-signal regulated kinase (ERK/MAPK) in granulosa cells. However, little is known about the effects of gonadotropin on ERK activity in theca cells. This study explores how LH/forskolin controls ERK phosphorylation in cultured bovine theca cells. Effects of ERK on steroidogenesis were also investigated. Phosphorylation of ERK in bovine theca cells was augmented by LH and forskolin in 5 min; it decreased thereafter below basal levels in 20 min. Nevertheless, phosphorylation of the ERK kinase, MEK, was unaffected. Addition of H89 (a PKA inhibitor) significantly reduced the effect of LH/forskolin on ERK phosphorylation. A potent MEK inhibitor PD98059 eliminated ERK phosphorylation and augmented progesterone production concomitantly with the elevation of intracellular steroidogenic acute regulatory protein (StAR) mRNA in LH/forskolin-stimulated theca cells. In contrast to progesterone production, androgen production was diminished significantly by inhibition of ERK with decreased intracellular P450c17 mRNA levels. Taking these results together, we conclude that LH/cAMP leads to phosphorylation of ERK in a biphasic manner through MEK-independent pathway in bovine theca cells. PKA-induced phosphatase could possibly contribute to the phosphorylation process. Furthermore, modulation of ERK phosphorylation involves control of thecal steroidogenesis via modulation of the expression of StAR and P450c17.
Key words: Theca cells • steroidogenesis • StAR • P450c17 • ERK




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