Inhibition of the catalytic activity of alcohol dehydrogenase by nitric oxide is associated with S nitrosylation and the release of zinc

Biochemistry
D Gergel, A I Cederbaum

Abstract

Nitric oxide (NO) reacts with the sulfhydryl groups of proteins to form nitroso thiols. Alcohol dehydrogenase (ADH) plays an important role in the metabolism of ethanol. Chronic alcohol administration stimulates NO formation in the liver, and production of NO is increased in alcohol liver injury. The effect of exogenous and endogenous NO on rat or horse ADH activity was evaluated. Incubation of intact rat hepatocytes or cytosol isolated from hepatocytes with S-nitroso-N-acetylpenicillamine (SNAP), a nitric oxide donor, resulted in a decrease in ADH activity. Endogenous NO synthesis was induced in rat hepatocytes by incubation with a mixture of cytokines and endotoxin in the presence of L-arginine. As NO production in hepatocytes increased over a 24 h time period, a significant decrease in ADH activity was observed. This effect was blocked by the competitive inhibitor of NO synthesis, N omega-nitro-L-arginine methyl ester, indicating that ADH was also inactivated by endogenously generated NO. The decreased activity of ADH was not related to lowering of the ADH content as shown by Western blot analysis. To evaluate the mechanism of inhibition, purified ADH from equine liver was incubated with gaseous NO or NO released from NO don...Continue Reading

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