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- W1985651693 abstract "Treatment of Swiss 3T3 cells with bombesin rapidly induced tyrosine phosphorylation of the p130 Crk-associated substrate (p130cas). Vasopressin, endothelin, bradykinin, lysophosphatidic acid, sphingosylphosphorylcholine, and phorbol 12,13-dibutyrate also stimulated p130cas tyrosine phosphorylation. Bombesin-induced p130cas tyrosine phosphorylation could be dissociated from both protein kinase C activation and Ca2+ mobilization from intracellular stores. In contrast, cytochalasin D, which disrupts the network of actin microfilaments, completely prevented tyrosine phosphorylation of p130cas by bombesin. Platelet-derived growth factor, at low concentrations (1-5 ng/ml), also induced tyrosine phosphorylation of p130cas via a pathway that depended on the integrity of the actin cytoskeleton. The phosphatidylinositol 3′-kinase inhibitors wortmannin and LY294002 prevented tyrosine phosphorylation of p130cas in response to platelet-derived growth factor but not in response to neuropeptides, lysophosphatidic acid, sphingosylphosphorylcholine, or phorbol 12,13-dibutyrate. All agonists that induced p130cas tyrosine phosphorylation also promoted the formation of a p130cas·Crk complex in intact Swiss 3T3 cells. Thus, our results identified distinct signal transduction pathways that lead to tyrosine phosphorylation of p130cas in the same cells and suggest that p130cas could play a role in mitogen-mediated signal transduction. Treatment of Swiss 3T3 cells with bombesin rapidly induced tyrosine phosphorylation of the p130 Crk-associated substrate (p130cas). Vasopressin, endothelin, bradykinin, lysophosphatidic acid, sphingosylphosphorylcholine, and phorbol 12,13-dibutyrate also stimulated p130cas tyrosine phosphorylation. Bombesin-induced p130cas tyrosine phosphorylation could be dissociated from both protein kinase C activation and Ca2+ mobilization from intracellular stores. In contrast, cytochalasin D, which disrupts the network of actin microfilaments, completely prevented tyrosine phosphorylation of p130cas by bombesin. Platelet-derived growth factor, at low concentrations (1-5 ng/ml), also induced tyrosine phosphorylation of p130cas via a pathway that depended on the integrity of the actin cytoskeleton. The phosphatidylinositol 3′-kinase inhibitors wortmannin and LY294002 prevented tyrosine phosphorylation of p130cas in response to platelet-derived growth factor but not in response to neuropeptides, lysophosphatidic acid, sphingosylphosphorylcholine, or phorbol 12,13-dibutyrate. All agonists that induced p130cas tyrosine phosphorylation also promoted the formation of a p130cas·Crk complex in intact Swiss 3T3 cells. Thus, our results identified distinct signal transduction pathways that lead to tyrosine phosphorylation of p130cas in the same cells and suggest that p130cas could play a role in mitogen-mediated signal transduction." @default.
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- W1985651693 date "1997-04-01" @default.
- W1985651693 modified "2023-10-11" @default.
- W1985651693 title "Tyrosine Phosphorylation of p130 by Bombesin, Lysophosphatidic Acid, Phorbol Esters, and Platelet-derived Growth Factor" @default.
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- W1985651693 doi "https://doi.org/10.1074/jbc.272.14.9363" @default.
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