TAILIEUCHUNG - Báo cáo khoa học: Cholecystokinin rapidly stimulates CrkII function in vivo in rat pancreatic acini Formation of CrkII–protein complexes

Crk belongs to a family of adapter proteins whose structure allows interaction with tyrosine-phosphorylated proteins and is therefore an important modulator of downstream signals, representing a convergence of the actions of numerous stimuli. Recently, it was demonstrated that chole-cystokinin (CCK) induced tyrosine phosphorylation of proteins related to fiber stress formation in rat pancreatic acini. | Eur. J. Biochem. 270 4706-4713 2003 FEBS 2003 doi Cholecystokinin rapidly stimulates Crkll function in vivo in rat pancreatic acini Formation of Crkll-protein complexes Alberto G. Andreolotti1 Maria J. Bragado2 Jose A. Tapia3 Robert T. Jensen3 and Luis J. Garcia-Marin1 1 Departamento de Fisiologia Universidad de Extremadura Caceres Spain 2Departamento de Bioquimica Biologia Molecular y Genetica Universidad de Extremadura Caceres Spain 3Digestive Diseases Branch National Institute of Diabetes and Digestive and Kidney Diseases of the National Institutes of Health Bethesda MD USA Crk belongs to a family of adapter proteins whose structure allows interaction with tyrosine-phosphorylated proteins and is therefore an important modulator of downstream signals representing a convergence of the actions of numerous stimuli. Recently it was demonstrated that cholecystokinin CCK induced tyrosine phosphorylation of proteins related to fiber stress formation in rat pancreatic acini. Here we investigated whether CCK reeeplor rcii antion signals through CrklI and forms complexes with tyrosine-phosphorylated proteins in rat pancreatic acini. We demonstrated that CCKpromoted the transient formation of CrkII-paxillin and CrkII-p130Cas complexes with maximal effect at 1 min. Additionally CCK decreased the elec trophoretic mobility of CrkII. This decrease was time- and concentration-dependent and inversely related with its function. Carbachol and bombesin also decreased CrkII electrophoretic mobility whereas epidermal growth factor vasoactive intestinal peptide secretin or pituitary adenylate cyclase-activating polypeptide had no effect. CCK-induced CrkII electrophoretic shift was dependent on the Src family of tyrosine kinases and occurred in the intact animal suggesting a physiological role of CrkII mediating CCK ruciio ns in the exocrine pancreas in vivo. Keywords Crk protein complex CCK transduction pathways pancreatic acini. Cholecystokinin CCK is

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