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a Department of Physiology and Pharmacology, Oregon Health Sciences University, Portland, Oregon 97201
b Oregon Regional Primate Research Center, Beaverton, Oregon 97006
c University of Wyoming, Department of Molecular Biology, Laramie, Wyoming 82071
There is evidence in several cell systems suggesting that the GnRH receptor couples to multiple G proteins. Presently there are no published studies showing GnRH receptor coupling to Gi
, Gs, and Gq/11 in a single cell type. To examine this possibility we measured palmitoylation of G proteins in response to GnRH receptor occupancy, since this event is a measure of G-protein activation by cognate receptors. GnRH stimulated time (0–120 min)- and dose (10-12–10-6 g/ml)-dependent palmitoylation of both Gi and Gs. Palmitoylation is G-protein activation dependent; accordingly, pertussis toxin (100 ng/ml; PTX), phorbol myristic acid (100 ng/ml), and Antide (50 nM; a GnRH antagonist) did not stimulate palmitoylation of Gi or Gs above basal levels. However, cholera toxin (5 µg/ml), an activator of Gs, stimulated palmitoylation of Gs but not Gi. We used a lactotrope-derived cell line expressing the GnRH receptor (GGH3) to examine whether the ability of the receptor to couple multiple G proteins is gonadotroph specific. GGH3 cells were transfected with specific cDNA coding for different G proteins, and agonist-stimulated second messenger production was assessed. Buserelin (a GnRH agonist) stimulated increased cAMP release in Gs cDNA-transfected GGH3 cells, whereas in Gi cDNA-transfected cells, both inositol phosphate (IP) production and cAMP release were decreased in response to buserelin. Transfection of Gq, G11, G14, and G15 cDNA into GGH3 cells resulted in an increased IP production in response to buserelin, indicating that GnRH receptor couples to this PTX-insensitive G-protein family. The observations presented in this study provide evidence for GnRH receptor coupling to multiple G proteins in a single cell type.
2 Correspondence. FAX: (503) 690–5569; connm{at}ohsu.edu
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