PMID: 9547350Apr 21, 1998Paper

A G protein beta gamma dimer-mediated pathway contributes to mitogen-activated protein kinase activation by thyrotropin-releasing hormone receptors in transfected COS-7 cells

Molecular Pharmacology
T PalomeroPilar de la Peña

Abstract

Activation of mitogen-activated protein kinase (MAPK) is induced by adding thyrotropin-releasing hormone (TRH) to COS-7 cells cotransfected with TRH receptors and an epitope-tagged MAPK. Long term treatment of the cells with pertussis toxin has no effect on TRH-induced MAPK activation. Incubation of the cells with the protein kinase C (PKC) inhibitor GF109203X causes an almost complete inhibition of MAPK activation by the PKC activator phorbol-12-myristate-13-acetate. In contrast, only approximately 50% of the TRH-induced MAPK activity is inhibited by GF109203X, indicating that activation of MAPK by TRH is only partially dependent on PKC. The inhibitory effect of GF109203X is additive with that of p21(N17ras), a dominant negative mutant of p21(ras) that exerts little effect on PKC-dependent MAPK activation by phorbol-12-myristate-13-acetate. The TRH-induced activation of MAPK also is inhibited partially by overexpression of transducin alpha subunits (alpha t), an agent known to sequester free G protein beta gamma dimers. However, the inhibitory potency of alpha t on TRH-induced activation is about half of that obtained in cells transfected with m2 muscarinic receptors, which activate MAPK exclusively through beta gamma dimers. ...Continue Reading

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Citations

Mar 15, 2012·Pflügers Archiv : European journal of physiology·Luis CarreteroPedro Domínguez
Oct 1, 2015·BioMed Research International·Susana Garcia-Recio, Pedro Gascón
Apr 11, 2006·American Journal of Physiology. Endocrinology and Metabolism·LuGuang LuoJohn Z Q Luo
Apr 13, 1999·The American Journal of Physiology·C W EmalaC A Hirshman

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