Effect of protein kinase C activation and depletion on insulin stimulation of glycogen synthesis in cultured hepatoma cells.
Insulin stimulation of glycogen synthesis was nearly abolished in hepatoma cells shortly treated with 4 beta-phorbol 12 beta-myristate, 13 alpha-acetate (protein kinase C activation) but remained unmodified in cells chronically treated with the phorbol ester (protein kinase C depletion). Thus, although exogenous activation of protein kinase C results in an inhibition of insulin action, protein kinase C depletion has no influence on this process. The results suggest that, in hepatoma cells, no endogenous activation of protein kinase C may occur in response to the signal triggered by insulin.
Caron
M
M
Laboratoire de Biochimie, INSERM U.181, Faculté de Médecine Saint-Antoine, Paris, France.
Cherqui
G
G
Wicek
D
D
Capeau
J
J
Bertrand
J
J
Picard
J
J
D000818:Animals; D004789:Enzyme Activation / Q000187:drug effects; D006003:Glycogen / Q000096:biosynthesis*; D007328:Insulin / Q000494:pharmacology*; D008114:Liver Neoplasms, Experimental / Q000378:metabolism*; D015240:Phorbol 12,13-Dibutyrate; D010703:Phorbol Esters / Q000494:pharmacology; D011493:Protein Kinase C / Q000378:metabolism*; D051381:Rats; D013755:Tetradecanoylphorbol Acetate / Q000494:pharmacology; D014407:Tumor Cells, Cultured
D007328:Insulin; D010703:Phorbol Esters; D015240:Phorbol 12,13-Dibutyrate; D006003:Glycogen; D011493:Protein Kinase C; D013755:Tetradecanoylphorbol Acetate