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pubmed-article:11343700pubmed:abstractTextWe present evidence that gastrin, binding to a G protein-coupled receptor, activates the p38-mitogen-activated protein kinase (MAPK) pathway. Blockage of protein kinase C (PKC) by GF109203X, depletion of intracellular calcium by thapsigargin or inhibition of Src family kinases by PP2 prevented p38-MAPK activation and the Src kinase activity stimulated by gastrin. Inhibition of the PI 3-kinase by wortmannin or LY294002 did not affect these responses. In addition, the p38-MAPK inhibitor, SB203580, repressed gastrin-induced [(3)H]thymidine incorporation, indicating a major role of p38-MAPK in the growth-promoting effect of gastrin. Our results demonstrate that gastrin-induced DNA synthesis requires p38-MAPK activation through mechanisms that involve calcium mobilization, PKC and Src family kinases.lld:pubmed
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pubmed-article:11343700pubmed:articleTitleGastrin-induced DNA synthesis requires p38-MAPK activation via PKC/Ca(2+) and Src-dependent mechanisms.lld:pubmed
pubmed-article:11343700pubmed:affiliationGroupe de Recherche de Biologie et Pathologie Digestives, INSERM U.531, CHU Rangueil, 1 avenue J. Poulhes, Institut Louis Bugnard, Bat. L3, 31403 Toulouse, France.lld:pubmed
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