作者: Akira Takeda , Shuichi Saheki , Takashi Shimazu , Nozomu Takeuchi
DOI: 10.1093/OXFORDJOURNALS.JBCHEM.A122923
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摘要: We previously demonstrated that the 27-kDa major component protein in rat liver gap junctions was phosphorylated by kinase C vitro (Takeda, A. et al. (1987) FEBS Lett. 210, 169-172). In this study, we examined further and phosphorylation of junction hepatocytes metabolically labeling cells with [32P]orthophosphate using a monoclonal antibody to immunoprecipitate protein. The inhibited antibodies recognizing carboxyl- (C-)terminal domain Protease digestion analysis revealed occurred at C-terminal domain. hepatocytes, phorbol esters, 12-O-tetradecanoylphorbol-13-acetate phorbol-12,13-dibutyrate, stimulated phosphorylation, whereas 4 alpha-phorbol-12,13-didecanoate did not. 1-Oleoyl-2-acetyl-sn-glycerol also phosphorylation. addition, norepinephrine pretreatment staurosporine, potent inhibitor C, stimulatory effect norepinephrine. Both chemical cleavage phosphoprotein mainly 10-kDa fragment which recognized. These results indicate phosphorylates protein, not only but