CCK causes rapid tyrosine phosphorylation of p125FAK focal adhesion kinase and paxillin in rat pancreatic acini.

@article{Garca1997CCKCR,
  title={CCK causes rapid tyrosine phosphorylation of p125FAK focal adhesion kinase and paxillin in rat pancreatic acini.},
  author={L. J. Garc{\'i}a and J. Rosado and T. Tsuda and R. Jensen},
  journal={Biochimica et biophysica acta},
  year={1997},
  volume={1358 2},
  pages={
          189-99
        }
}
Recent studies show CCK stimulates tyrosine phosphorylation (TYR PHOSP) of a number of proteins and evidence from the pancreas and other cellular systems suggest this could be important in mediating some of CCK's growth and secretory effects. In other tissues various neuropeptides such as bombesin can cause tyrosine phosphorylation of p125 focal adhesion kinase (p125FAK) and paxillin which are important in mediating their growth effects. The purpose of the present study was to determine the… Expand
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Are tyrosine phosphorylation of p125(FAK) and paxillin or the small GTP binding protein, rho, needed for CCK-stimulated pancreatic amylase secretion?
TLDR
The results show that tyrosine phosphorylation of p125FAK and paxillin is not required for CCK-8 stimulation of enzyme secretion, and suggest Rho is involved in the CCK’s stimulation of amylase release by a parallel pathway to its involvement in this role. Expand
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Bombesin and gastrin releasing peptide increase tyrosine phosphorylation of focal adhesion kinase and paxillin in non-small cell lung cancer cells.
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Phosphospecific Site Tyrosine Phosphorylation of p125FAK and Proline-rich Kinase 2 Is Differentially Regulated by Cholecystokinin Receptor Type A Activation in Pancreatic Acini*
TLDR
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Activation of m3 muscarinic receptors induces rapid tyrosine phosphorylation of p125(FAK), p130(cas), and paxillin in rat pancreatic acini.
TLDR
Results suggest that activation of m3 muscarinic receptors in rat pancreatic acini increases tyrosine phosphorylation of p125(FAK) and its substrates, p130(cas) and paxillin by diacylglycerol-activated PKC- and calcium- dependent, and independent pathways. Expand
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P125FAK and paxillin are identified as components of the intracellular pathways stimulated after EGF receptor occupation in rat pancreatic acini. Expand
A Role for the p38 Mitogen-activated Protein Kinase/Hsp 27 Pathway in Cholecystokinin-induced Changes in the Actin Cytoskeleton in Rat Pancreatic Acini*
TLDR
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TLDR
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Regulation of the Actin Cytoskeleton by p125 Focal Adhesion Kinase in Rat Pancreatic Acinar Cells
Background/Aims: Activation of p125 focal adhesion kinase by cholecystokinin (CCK)-8 has recently been demonstrated in pancreatic acinar cells. The purpose of this study is to examine downstreamExpand
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TLDR
Results show that multiple mechanisms are involved in BK-stimulated tyrosine phosphorylation of p125FAK, paxillin, Ras-GAP-associated p125, and src transformation- associated p130 and half-maximal effects occurring at 1-10 nM BK. Expand
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The finding that one of these substrates is a tyrosine kinase suggests the existence of a novel signal transduction pathway in the action of mitogenic neuropeptides. Expand
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TLDR
It is demonstrated that neither the PKC nor Ca2+ pathways are responsible for the rapid stimulation of p125FAK tyrosine phosphorylation by neuropeptide growth factors, and the integrity of the actin cytoskeleton is essential for the effects of both PDB and bombesin. Expand
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TLDR
The results suggest that CCK-B/gastrin receptors might transmit mitogenic signals by cross-talking with the tyrosine kinase cascades. Expand
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TLDR
Results provide direct evidence for neuropeptide activation of a tyrosine kinase in cell-free preparations and identify a novel event in the action of this class of growth factors in intact Swiss 3T3 cells. Expand
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TLDR
It is shown that an increase in tyrosine phosphorylation of a 120-kDa group of proteins is an early protein kinase C-independent cellular signal elicited by both bradykinin and bombesin. Expand
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TLDR
Evidence is provided that acinar cell tyrosine phosphorylation is stimulated by agonists acting via calcium- dependent and protein kinase C-dependent pathways, with only the calcium-dependent tyrosin phosphorylated cascade involved in triggering hormone-induced amylase release. Expand
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TLDR
It is proposed that the inhibitory limb in the bell-shaped dose-response curve of PDGF and the novel cross-talk between PD GF and bombesin on tyrosine phosphorylation may be explained by the ability ofPDGF at 30 ng/ml to disrupt the actin cytoskeleton. Expand
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TLDR
Evidence that tyrosine phosphorylation is a mitogenic signal for bombesin is provided by treatment of intact Swiss 3T3 cells with 20 microM tyrphostin. Expand
Jun Kinases Are Rapidly Activated by Cholecystokinin in Rat Pancreas both in Vitro and in Vivo(*)
TLDR
JNKs and mitogen-activated protein kinases are rapidly activated in rat pancreatic acini stimulated by both cholecystokinin and anisomycin as well as in pancreatic tissue during in vivo stimulation with CER. Expand
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