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In this study, the effects of catalase (CAT) inhibitor aminotriazole (ATZ) on alcohol-induced acute liver injury were investigated to explore the potential roles of CAT in alcoholic liver injury. Acute liver injury was induced by intraperitoneal injection of alcohol in Sprague Dawley (SD) rats, and various doses of ATZ (100-400 mg/kg) or vehicle were administered intraperitoneally at 30 min before alcohol exposure. After 24 h of alcohol exposure, the levels of aspartate transaminase (AST), alanine transaminase (ALT) and lactate dehydrogenase (LDH) in plasma were determined. The degree of hepatic histopathological abnormality was observed by HE staining. The activity of hepatic CAT, hydrogen peroxide (H₂O₂) level and malondialdehyde (MDA) content in liver tissue were measured by corresponding kits. The levels of tumor necrosis factor-α (TNF-α) and interleukin-6 (IL-6) in plasma were determined by ELISA method. The results showed that treatment with ATZ dose-dependently suppressed the elevation of ALT, AST and LDH levels induced by alcohol exposure, and that ATZ alleviated alcohol-induced histopathological alterations. Furthermore, ATZ inhibited the activity of CAT, reduced hepatic levels of H₂O₂and MDA in alcohol exposed rats. ATZ also decreased the levels of plasma TNF-α and IL-6 in rats with alcohol exposure. These results indicated that ATZ attenuated alcohol-induced acute liver injury in rats, suggesting that CAT might play important pathological roles in the pathogenesis of alcoholic liver injury.

Objective: To study the possible mechanism of H2O2-producing lactobacilli inhibited neisseria gonorrhoeae growth., Methods: H2O2-producing lactobacilli were coincubated with neisseria gonorrhoeae in vitro, LB+ cell were disrupted by sonication, the protein in the lactobacilli lysate was separated by filtration through different MW sizes membranes and was examined for the ability to inhibit N. gonorrhoeae catalase activity., Results: When coincubation medium was at pH 5.0, there was a significant decrease in the gonococcal catalase activity, the lysates of LB+ also effectively inhibited gonococcal catalase activity. This inhibition was retained upon heating of lysate to 100 degrees C for 15 minutes but was lost with proteinase K treatment., Conclusions: The LB+ may inhibit growth of gonococci by production of catalase inhibitors.