EFFECTS OF ETHANOL-METABOLISM ON PKC ACTIVITY IN ISOLATED RAT HEPATOCYTES

Isolated rat hepatocytes were exposed to increasing concentrations of ethanol. During exposure of cells to ethanol a moderate but significan t modification in the level of hepatic PKC c-isoforms has been observe d, The ethanol-induced effect on liver protein kinase C was reversed b y 4-methylpyrazole, an inhibitor of alcohol dehydrogenase, indicating that the conversion of ethanol to acetaldehyde may be involved in the enzyme inactivation. The involvement of the alcohol metabolite in PKC modifications was confirmed by the exposure of hepatocytes or partiall y purified liver enzyme to acetaldehyde concentrations of pathological interest.