Tyrphostin inhibits bombesin stimulation of tyrosine phosphorylation, c-fos expression, and DNA synthesis in Swiss 3T3 cells.
作者： M. Seckl , E. Rozengurt
DOI: 10.1016/S0021-9258(18)98386-9
关键词: Protein kinase C 、 Bombesin 、 Biology 、 Forskolin 、 Phorbol 、 Signal transduction 、 Tyrosine phosphorylation 、 Mitogen-activated protein kinase 、 Molecular biology 、 Tyrosine kinase
摘要: Abstract Treatment of quiescent Swiss 3T3 cells with 20 microM ([(3,4,5-trihydroxyphenyl)methylene]propanedinitrile) (tyrphostin) caused a 76% reduction in the tyrosine phosphorylation M(r) 110,000-130,000 band induced by bombesin. This was accompanied 48% cytosolic kinase p125 focal adhesion kinase. Preincubation tyrphostin did not inhibit either protein A activation forskolin or C (PKC) phorbol 12,13-dibutyrate intact cells. Similarly, neither interfered binding bombesin to its receptor nor prevented bombesin-stimulated Ca2+ mobilization PKC activation. Thus selectively inhibits Consequently, we examined contribution this pathway subsequent induction c-fos and stimulation mitogenesis Tyrphostin both mRNA expression DNA synthesis The incorporation [3H] thymidine inhibited dose-dependent manner (IC50 = microM), effect reversed even at high concentrations These results provide evidence that is mitogenic signal for
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