Hepatic glutathione levels in D-penicillamine-fed ethanol-dependent rats.
Ethanol oxidation is accomplished primarily by alcohol dehydrogenase. However, a microsomal system involving hydrogen peroxide formation operates at elevated ethanol concentrations. Removal of the resultant hydrogen peroxide may depend on the activity of glutathione peroxidase. In the study, we have examined the effect of chronic ethanol exposure on hepatic glutatione levels and found that ethanol exposure resulted in elevations of hepatic reduced and oxidized glutathione. The dietary inclusion of the sulfhydryl amino acid, D-penicillamine, increased hepatic reduced glutathione (GSH) in both ethanol-dependent and control rats. However, D-penicillamine did not have a differential effect on hepatic GSH when comparing ethanol-dependent and control animals. Following two weeks exposure, the exclusion of ethanol and/or D-penicillamine from the diet for 24 hours resulted in a significant decrease in hepatic GSH.
D000437:Alcoholism / Q000378:metabolism*; D000818:Animals; D004032:Diet; D005978:Glutathione / Q000378:metabolism*; D006801:Humans; D008099:Liver / Q000378:metabolism*; D008297:Male; D010084:Oxidation-Reduction; D010396:Penicillamine / Q000494:pharmacology*; D051381:Rats
D005978:Glutathione; D010396:Penicillamine