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Originally published In Press as doi:10.1074/jbc.M203639200 on June 5, 2002

J. Biol. Chem., Vol. 277, Issue 35, 32099-32108, August 30, 2002
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Involvement of Both Gq/11 and Gs Proteins in Gonadotropin-releasing Hormone Receptor-mediated Signaling in Lbeta T2 Cells*

Fujun LiuDagger , Isao UsuiDagger , Lui Guojing Evans§, Darrell A. Austin§, Pamela L. Mellon||, Jerrold M. OlefskyDagger , and Nicholas J. G. WebsterDagger §||**

From the Departments of Dagger  Medicine and  Reproductive Medicine, and the || UCSD Cancer Center, University of California, San Diego, California 92093 and the § Medical Research Service and San Diego Veterans Healthcare System, San Diego, California 92161

The hypothalamic hormone gonadotropin-releasing hormone (GnRH) stimulates the synthesis and release of the pituitary gonadotropins. GnRH acts through a plasma membrane receptor that is a member of the G protein-coupled receptor (GPCR) family. These receptors interact with heterotrimeric G proteins to initiate downstream signaling. In this study, we have investigated which G proteins are involved in GnRH receptor-mediated signaling in Lbeta T2 pituitary gonadotrope cells. We have shown previously that GnRH activates ERK and induces the c-fos and LHbeta genes in these cells. Signaling via the Gi subfamily of G proteins was excluded, as neither ERK activation nor c-Fos and LHbeta induction was impaired by treatment with pertussis toxin or a cell-permeable peptide that sequesters Gbeta gamma -subunits. GnRH signaling was partially mimicked by adenoviral expression of a constitutively active mutant of Galpha q (Q209L) and was blocked by a cell-permeable peptide that uncouples Galpha q from GPCRs. Furthermore, chronic activation of Galpha q signaling induced a state of GnRH resistance. A cell-permeable peptide that uncouples Galpha s from receptors was also able to inhibit ERK, c-Fos, and LHbeta , indicating that both Gq/11 and Gs proteins are involved in signaling. Consistent with this, GnRH caused GTP loading on Gs and Gq/11 and increased intracellular cAMP. Artificial elevation of cAMP with forskolin activated ERK and caused a partial induction of c-Fos. Finally, treatment of Galpha q (Q209L)-infected cells with forskolin enhanced the induction of c-Fos showing that the two pathways are independent and additive. Taken together, these results indicate that the GnRH receptor activates both Gq and Gs signaling to regulate gene expression in Lbeta T2 cells.

* This work was supported by a U54 Center Grant HD-12303 from the National Institutes of Health.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 should be addressed: Dept. of Medicine 0673, University of California, San Diego, 9500 Gilman Dr., La Jolla, CA 92093-0673. E-mail: nwebster@ucsd.edu.

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