Multiple kinases phosphorylate the pancreatic cholecystokinin receptor in an agonist-dependent manner.

摘要: The cholecystokinin (CCK) receptor on the rat pancreatic acinar cell is a guanine nucleotide-binding protein (G protein)-coupled receptor, which was recently demonstrated to be phosphorylated in response agonist stimulation (Klueppelberg et al., J. Biol. Chem. 266: 17744-17746, 1991). In this work, we establish that variety of homologous and heterologous secretagogues these phosphorylation events represent action by more than one kinase. One subgroup kinases includes or isotype kinase C (PKC), capable playing role desensitization. A second acts CCK defined its resistance 10 microM staurosporine, shown inhibit all PKC cells. activity group observed only occupation high concentrations native hormone, raising possibility "receptor-specific kinase." Similar prototypical kinase, beta-adrenergic (beta-ARK), inhibited permeabilized cells heparin. Furthermore, like enzyme activity, beta-ARK resistant staurosporine. Based G protein-coupled activation at agonist, pattern inhibition, believe staurosporine-insensitive represents either closely related member receptor-specific family.