Carbachol stimulates TYR phosphorylation and association of PKCdelta and PYK2 in pancreas.
Carbachol treatment resulted in increased phosphorylation on tyrosine of PKCdelta immunoprecipitated from rat pancreatic acinar cells. The Ca2+-dependent tyrosine kinase PYK2 coimmunoprecipitated with PKCdelta from carbachol-exposed cells and also exhibited increased tyrosine phosphorylation. Tyrosine phosphorylation of both PKCdelta and PYK2 was concentration-dependent with respect to carbachol, and rapid, reaching maximal ... levels by 5 min of treatment. Exposure of acinar cells to phorbol myristate acetate (PMA), a phorbol ester activator of PKCdelta, also resulted in increased phosphorylation of PKCdelta and PYK2 isolated using anti-PKCdelta immunoprecipitation. These results are suggestive of a physical and functional interaction between PKCdelta and PYK2 following muscarinic stimulation in the pancreatic acinar cell.
Mesh Terms:
Animals, Carbachol, Cells, Cultured, Focal Adhesion Kinase 2, Isoenzymes, Macromolecular Substances, Muscarinic Agonists, Pancreas, Phosphorylation, Phosphotyrosine, Protein Kinase C, Protein Kinase C-delta, Protein-Tyrosine Kinases, Rats, Rats, Wistar, Tetradecanoylphorbol Acetate
Animals, Carbachol, Cells, Cultured, Focal Adhesion Kinase 2, Isoenzymes, Macromolecular Substances, Muscarinic Agonists, Pancreas, Phosphorylation, Phosphotyrosine, Protein Kinase C, Protein Kinase C-delta, Protein-Tyrosine Kinases, Rats, Rats, Wistar, Tetradecanoylphorbol Acetate
Biochem. Biophys. Res. Commun.
Date: Apr. 13, 2001
PubMed ID: 11352632
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