Bombesin, vasopressin, and endothelin stimulation of tyrosine phosphorylation in Swiss 3T3 cells. Identification of a novel tyrosine kinase as a major substrate.

  title={Bombesin, vasopressin, and endothelin stimulation of tyrosine phosphorylation in Swiss 3T3 cells. Identification of a novel tyrosine kinase as a major substrate.},
  author={I. Zachary and J. Sinnett-Smith and E. Rozengurt},
  journal={The Journal of biological chemistry},
  volume={267 27},
Neuropeptide-stimulated tyrosine phosphorylation of specific components in Swiss 3T3 cells was investigated using monoclonal antibodies directed against the src transformation-associated substrates p125 focal adhesion kinase (FAK), a novel type of cytosolic tyrosine kinase, and p130. Treatment of Swiss 3T3 cells with the mitogenic peptides bombesin, vasopressin, and endothelin caused a striking increase in the tyrosine phosphorylation of p125FAK, as judged either by anti-phosphotyrosine (anti… Expand
Tyrosine phosphorylation of p130(cas) by bombesin, lysophosphatidic acid, phorbol esters, and platelet-derived growth factor. Signaling pathways and formation of a p130(cas)-Crk complex.
Two distinct signal transduction pathways that lead to tyrosine phosphorylation of p130(cas) in the same cells are identified and it is suggested that p130 (cas) could play a role in mitogen-mediated signalTransduction. Expand
Bombesin, Bradykinin, Vasopressin, and Phorbol Esters Rapidly and Transiently Activate Src Family Tyrosine Kinases in Swiss 3T3 Cells
Two separate pathways that lead to protein tyrosine phosphorylation in neuropeptide-stimulated Swiss 3T3 cells are dissected, which are not dependent either on protein kinase C or Ca2+. Expand
Bombesin, Vasopressin, Lysophosphatidic Acid, and Sphingosylphosphorylcholine Induce Focal Adhesion Kinase Activation in Intact Swiss 3T3 Cells*
The results demonstrate that agonists that act via 7-transmembrane domain receptors stimulate FAK kinase activation, and indicate that FAK activation requires an intact actin cytoskeleton. Expand
Tyrosine phosphorylation of p125fak, p130cas, and paxillin does not require extracellular signal‐regulated kinase activation in swiss 3T3 cells stimulated by bombesin or platelet‐derived growth factor
The experiments presented here were designed to examine the contribution of the extracellular signal‐regulated mitogen‐activated protein kinases (ERKs) to the tyrosine phosphorylation of the focalExpand
Dissociation of focal adhesion kinase and paxillin tyrosine phosphorylation induced by bombesin and lysophosphatidic acid from epidermal growth factor receptor transactivation in Swiss 3T3 cells
The results clearly dissociate EGFR transactivation from the tyrosine phosphorylation of FAK and paxillin induced by multiple GPCR agonists. Expand
Requirement for Phosphatidylinositol 3′-Kinase Activity in Platelet-derived Growth Factor-stimulated Tyrosine Phosphorylation of p125 Focal Adhesion Kinase and Paxillin (*)
A PI 3′-kinase-dependent signal transduction pathway in the action of PDGF, which leads to the phosphorylation of p125 and paxillin is identified. Expand
Bombesin and gastrin releasing peptide increase tyrosine phosphorylation of focal adhesion kinase and paxillin in non-small cell lung cancer cells.
Results suggest that p125(FAK) is an important enzyme for NSCLC proliferation and treatment of NCI-H1299 cells with FAK antisense resulted in decreased FAK tyrosine kinase activity and proliferation. Expand
Phosphorylation of p130Cas by angiotensin II is dependent on c-Src, intracellular Ca2+, and protein kinase C.
These results are the first to demonstrate that the tyrosine phosphorylation of p130Cas by Ang II is transduced by the Src, intracellular Ca2+, protein kinase C signaling pathway. Expand
Vasopressin stimulates tyrosine phosphorylation by activation of pkc in the rat smooth muscle cell line, a‐10
Results indicate that PKC is upstream of the phosphorylation, a motion which is supported by the fact that the AVP‐stimulatedosphorylation was downregulated by phorbol esters. Expand
CCK causes rapid tyrosine phosphorylation of p125FAK focal adhesion kinase and paxillin in rat pancreatic acini.
It is demonstrated that in rat pancreatic acini, CCK causes rapid TYR PHOSP of both p125 focal adhesion kinase and paxillin, mediated by both the high affinity and low affinity CCK receptor states. Expand