After alcohol exposure through a standard Lieber and De Carli diet for 28 days, a severe atrophy in the rat uteirne horn was observed, accompanied by significant alterations in its epithelial cells. Microsomal pathway of acetaldehyde production was slightly increased. Hydroxyl radicals were detected in the cytosolic fraction, and this was attributed to participation of xanthine oxidoreductase. They were also observed in the microsomal fraction in the presence of NADPH generating system. No generation of 1-hydroxyethyl was evidenced. The t-butylhydroperoxide-induced chemiluminescence analysis of uterine horn homogenates revealed a significant increase in the chemiluminiscence emission due to ethanol exposure. In the animals repeatedly exposed to alcohol, sulfhydryl content from uterine horn proteins was decreased, but no significant changes were observed in the protein carbonyl content from the same samples. Minor but significant decreasing changes were observed in the GSH content accompanied by a tendency to decrease in the GSH/GSSG ratio. A highly significant finding was the diminished activity content of glutathione peroxidase. Results suggest that acetaldehyde accumulation plus the oxidative stress may play an additional effect to the alcohol-promoted hormonal changes in the uterus reported by others after chronic exposure to alcohol. 1. Introduction In previous studies from our laboratory we reported that the rat uterine horn has different metabolic pathways able to generate acetaldehyde from ethanol accompanied by a low capacity to destroy it through aldehyde dehydrogenase (ALDH). That led to long lasting increases in acetaldehyde levels in the uterus during ethanol exposure [1]. The identified enzymes involved in acetaldehyde production included alcohol dehydrogenase (ADH) and xanthine oxidoreductase (XO) in the cytosolic fraction and the flavoenzyme NADPH oxidase and catalase in the microsomal fraction [1]. The ALDH activity present in the mitochondrial fraction was almost negligible and not detectable at all in the microsomal or cytosolic fraction. That was envisaged to be a reasonable explanation for the observed acetaldehyde increased levels observed [1]. However, other enzymatic systems and cofactors such as GSH and glutathione transferase (GST) that are also able to handle acetaldehyde to eliminate it were not determined in those studies. Notwithstanding, acetaldehyde is not the only harmful metabolite produced during interaction of ethanol with enzymes and cellular fractions in different tissues. In effect, previous studies from our and
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