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Comp Biochem Physiol B Biochem Mol Biol. 2005 Nov;142(3):335-41. Epub 2005 Sep 15.

Adaptive response of antioxidant enzymes to catalase inhibition by aminotriazole in goldfish liver and kidney.

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Department of Biochemistry, Precarpathian National University named after Vassyl Stefanyk, 57 Shevchenko Str., 76025, Ivano-Frankivsk, Ukraine.


This study was undertaken to clarify the physiological role of catalase in the maintenance of pro/antioxidant balance in goldfish tissues by inhibiting the enzyme in vivo with 3-amino 1,2,4-triazole. Intraperitoneal injection of aminotriazole (0.5 mg/g wet mass) caused a decrease in liver catalase activity by 83% after 24 h that was sustained after 168 h post-injection. In kidney catalase activity was reduced by approximately 50% and 70% at the two time points, respectively. Levels of protein carbonyls were unchanged in liver but rose by 2-fold in kidney after 168 h. Levels of thiobarbituric acid-reactive substances were elevated in both tissues after 24 h but were reversed by 168 h. Glutathione peroxidase and glutathione-S-transferase activities increased in kidney after aminotriazole treatment whereas activities of glutathione peroxidase and glutathione reductase in liver decreased after 24 h but rebounded by 168 h. Liver glucose-6-phosphate dehydrogenase activity was reduced at both time points. Activities of these three enzymes in liver correlated inversely with the levels of lipid damage products (R2=0.65-0.81) suggesting that they may have been oxidatively inactivated. Glutathione-S-transferase activity also correlated inversely with catalase (R2=0.86). Hence, the response to catalase depletion involves compensatory changes in the activities of enzymes of glutathione metabolism.

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