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J. Biol. Chem., Vol. 269, Issue 44, 27372-27377, 11, 1994
YH Chen, J Pouyssegur, SA Courtneidge and E Van Obberghen-Schilling
Thrombin stimulates G protein-coupled signaling pathways in target cells by
proteolytic cleavage of its seven transmembrane domain receptor. Protein
tyrosine phosphorylation is also stimulated by the protease via poorly
defined mechanisms. In human platelets, thrombin has been shown to activate
the nonreceptor tyrosine kinase Src. To elucidate the signal transduction
pathways involved in transmission of thrombin's cellular effects, we have
examined the ability of thrombin to activate Src family tyrosine kinases in
a growth-responsive line of lung fibroblasts (CCL39 cells). We report here
that thrombin induces a rapid (< or = 30 s) and transient increase in
the kinase activity of Src and Fyn as determined by autophosphorylation in
immune complex kinase assays. Activation is mediated by the G
protein-coupled thrombin receptor since a synthetic peptide agonist of the
receptor mimics thrombin action. The involvement of one or more G proteins
in this response was confirmed by the observation that thrombin's effect is
partially sensitive to pertussis toxin. Furthermore, both alpha 2-
adrenergic and muscarinic m1 receptors are able to increase Src kinase
activity via pertussis toxin-sensitive and -insensitive G proteins,
respectively. These findings suggest that nonreceptor tyrosine kinases of
the Src family may represent a novel effector system linking G
protein-coupled receptors to downstream activation of Ras and the
mitogen-activated protein kinase cascade.
Activation of Src family kinase activity by the G protein-coupled thrombin receptor in growth-responsive fibroblasts
Centre de Biochimie, CNRs UMR134, Nice, France.
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