Effect of ethanol on the microsomal glutathione S-transferase activity in glutathione-depleted rat liver.
Depletion of hepatic glutathione in male rats by starvation caused a significant increase in microsomal glutathione S-transferase activity, which was not affected by acute ethanol pretreatment. An additional depletion in fasted rats by diethylmaleate (0.5 g/kg) caused a further increase in the enzyme activity, but this increase was delayed in ethanol intoxicated rats. Although ethanol caused a small increase in hepatic microsomal lipid peroxidation in control animals, this effect of ethanol was not observed in diethylmaleate treated rats and thus was apparently not responsible for the delay in enzyme activation. It is suggested that the activation of microsomal glutathione S-transferase activity towards 1-chloro-2,4-dinitrobenzene in glutathione-depleted rat liver may be produced by changes in thiol/disulfid ratio and/or some reactive oxygen species.
D000818:Animals; D000431:Ethanol / Q000494:pharmacology*; D005978:Glutathione / Q000172:deficiency*; D005982:Glutathione Transferase / Q000032:analysis*; D066298:In Vitro Techniques; D008054:Lipid Peroxides / Q000378:metabolism; D008297:Male; D008862:Microsomes, Liver / Q000187:drug effects / Q000201:enzymology*; D051381:Rats
D008054:Lipid Peroxides; D000431:Ethanol; D005982:Glutathione Transferase; D005978:Glutathione