Effect of protein kinase C activation and depletion on insulin stimulation of glycogen synthesis in cultured hepatoma cells |
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Authors: | M. Caron G. Cherqui D. Wicek J. Capeau J. Bertrand J. Picard |
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Affiliation: | (1) Laboratoire de Biochimie, INSERM U. 181, Faculté de Médecine Saint-Antoine, 27 rue Chaligny, F-75571 Paris Cédex 12, France |
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Abstract: | Summary Insulin stimulation of glycogen synthesis was nearly abolished in hepatoma cells shortly treated with 4 ß-phorbol 12 -myristate, 13 -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. |
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Keywords: | Glycogen synthesis insulin protein kinase C Zajdela hepatoma cells |
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