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• W2018407245 abstract "Gonadotropin-releasing hormone (GnRH)-induced Gq-mediated stimulation of mitogen-activated protein kinases (MAPKs), including extracellularly regulated kinases 1 and 2 (ERK1/2), in GT1–7 neuronal cells, occurs via transactivation of the epidermal growth factor receptor (EGF-R) in a protein kinase C (PKC) dependent fashion. In this study, we determined whether other prosurvival proteins, including p90 ribosomal S6 kinase (RSK-1), cyclic AMP response element binding protein (CREB) and the antiapoptotic protein BAD, are also phosphorylated by GnRH in immortalized hypothalamic cells (GT1–7). Since the GnRH-R is coupled to Gs/adenylyl cyclase as well as Gq/PKC in these cells, and cAMP is known to stimulate MAPK signaling in neurons, we also examined the role of cAMP in mediating these effects. Cell culture and immunoblot analysis. GT1–7 cells were grown in F12/DEMEM culture medium. Serum-deprived cells were stimulated with GnRH, EGF, forskolin, epinephrine and phorbol 12-myristate 12-acetate (PMA) in the presence and absence of selective inhibitors. After collection in Laemmeli buffer, cell lysates were subjected to immunoblot analysis to determine the phosphorylation of CREB, RSK-1 and BAD proteins. Stimulation of GT1–7 cells with GnRH caused rapid activation of ERK1/2, RSK-1, CREB and BAD. These actions of GnRH were attenuated by the selective EGF-R antagonist, AG1478, in a concentration-dependent manner. Activation of PKC by PMA, and of EGF-R by EGF, also caused rapid phosphorylation of these proteins. The selective phosphoinositide 3-kinase (PI3K) inhibitor, wortmannin, decreased GnRH-, PMA- and EGF-induced phosphorylation of ERK1/2, RSK-1, CREB and BAD in a concentration-dependent manner. Epinephrine-induced activation of Gs-coupled adrenoceptors in GT1–7 cells also caused phosphorylation of ERK1/2, RSK-1 and CREB through activation of the EGF-R and PI3K. Blockade of cAMP/PKA with H-89 abolished the effects of epinephrine, and decreased those of GnRH, indicating partial involvement of Gs/cAMP/PKA signaling in GnRH action in these cells. Agonist-induced stimulation of these prosurvival proteins was abolished by the MEK inhibitor, UO126, indicating the involvement of the MEK/ERK cascade in these responses. These data demonstrate that stimulation of Gq/PKC by GnRH, and of Gs/adenylyl cyclase/cAMP by epinephrine and forskolin, causes activation of ERK1/2, RSK-1 and CREB through transactivation of the EGF-R and PI3K in GT1–7 cells. The signals emanating from these agonists appear to converge at MEK in the ERK signaling cascade." @default.
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• W2018407245 date "2004-09-01" @default.
• W2018407245 modified "2023-09-27" @default.
• W2018407245 title "Dependence of GnRH-induced CREB phosphorylation in hypothalamic neurons upon transactivation of the EGF receptor and activation of the phosphoinositide 3-kinase pathway" @default.
• W2018407245 doi "https://doi.org/10.1016/j.fertnstert.2004.07.833" @default.
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