Catalase inhibition by amino triazole induces oxidative stress in goldfish brain

被引:79
作者
Bagnyukova, TV
Vasylkiv, OY
Storey, KB
Lushchak, VI
机构
[1] Vassyl Stefanyk Precarpathian Natl Univ, Inst Nat Sci, Dept Biochem, UA-76025 Ivano Frankivsk, Ukraine
[2] Carleton Univ, Dept Biol, Ottawa, ON K1S 5B6, Canada
基金
加拿大自然科学与工程研究理事会;
关键词
goldfish; catalase; 3-amino 1,2,4-ttiazole; glutathione peroxidase; carbonylprotein;
D O I
10.1016/j.brainres.2005.06.002
中图分类号
Q189 [神经科学];
学科分类号
071006 ;
摘要
The effects of in vivo inhibition of catalase by 3-amino 1,2,4-triazole (AMT) on the levels of damage products resulting from reactive oxygen species attack on proteins and lipids as well as on the activities of five antioxidant and associated enzymes were studied in the brain of goldfish, Carassius auratus. Intraperitoneal injection of AMT at a concentration of 0.1 mg/g wet weight caused a gradual decrease in brain catalase activity over 72 h, whereas higher AMT concentrations (0.5 or 1.0 mg/g) reduced catalase activity by about two-thirds within 5-10 h. AMT effects on antioxidant enzyme activities and oxidative stress markers were studied in detail using fish treated with 0.5 mg/g AMT for 24 or 168 h. The levels of thiobarbituric acid-reactive substances (a lipid damage product) increased 6,5-fold by 24 h after AMT injection but fell again after 168 h. The content of carbonylproteins (CP) also rose within 24 h (by similar to 2-fold) and remained 1.5-fold higher compared with respective sham-injected fish after 168 h. CP levels correlated inversely with catalase activity (R-2 = 0.93) suggesting that catalase may protect proteins in vivo against oxidative modification. The activities of both glutathione peroxidase and glulathione-S-transferase increased by similar to 50 % and 80 %, respectively, in brain of AMT-treated fish and this might represent it compensatory response to lowered catalase activity. Possible functions of catalase in the maintenance of prooxidant/antioxidant balance in goldfish brain are discussed. (c) 2005 Published by Elsevier B.V.
引用
收藏
页码:180 / 186
页数:7
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