Ethanol administration generates oxidative stress in the pancreas and liver, but fails to induce heat-shock proteins in rats.

Background: Heat-shock proteins (HSP) play an essential role in the sequestration and reparation of denatured cellular proteins. Because ethanol treatment can result in oxidative stress-induced protein damage, it is possible that expression of HSP is altered after ethanol consumption. Dose-response and time-course studies were performed to investigate whether acute and chronic intragastric ethanol administration can induce tissue damage, oxidative stress and expression of the heat-shock proteins HSP60 and HSP72 in the pancreas and liver of male Wistar rats.

Methods: Laboratory and morphological analysis of pancreatic and liver damage were investigated. The degree of oxidative stress was assessed by measurement of the reduced glutathione content, lipid peroxidation and protein oxidation. The levels of HSP were examined by western blot analysis.

Results: Ethanol administration dose- and time-dependently elevated the serum ethanol concentration and hepatic enzyme activities. Chronic ethanol treatment also resulted in morphological damage of the liver. We observed that acute and chronic ethanol consumption had markedly different effects on the oxidative parameters in the pancreas and liver. Acute ethanol administration caused oxidative stress in the liver, whereas there was no such effect in the pancreas. In contrast, chronic ethanol feeding resulted in oxidative stress in both the pancreas and the liver. Furthermore, neither acute nor chronic ethanol intake induced the synthesis of HSP, a major defense system against cellular damage in the examined organs.

Conclusion: Ethanol administration generates oxidative stress in the pancreas and liver, but fails to induce HSP in rats.