Effects Of Prolonged Exercise On The Thioredoxin Reductase In Heart Muscle And Skeletal Muscle Of Rats

Thioredoxins are small ubiquitous proteins with a conserved redox active Cys-Gly-Pro-Cys motif. The proteins function in a wide variety of cellular processes, such as regulating the cellular apoptosis, effecting the DNA binding of NF kappa B. The first elucidated role was as donor of reducing equivalents for ribonucleotide reductase. In higher organisms, the thioredoxin system, composed of thioredoxin, NADPH, and thioredoxin reductase, which catalyze the reduction of hydrogen peroxide and organic peroxides, is widely distributed in nature.Exercise training enhances the anti-oxidative system in some degree, but exhausted exercise impairs it. Experiments have showed that prolonged exercise canenhance the main anti-oxidative system--glutathione system, especially theglutathione reductase, but exhausted exercise impairs it, Which is also proved in my experiment.The results indicated that the activity of thioredoxin reductase is significantly increased after 6 weeks prolonged training(50min/day 60min/day, 70min/day, 80min/day 90min/day 90min/day), but no change in mRNA level, with DTNB and RT-PCR. On the contrary, exhausted exercise impairs the activity of thioredoxin reductase significantly.