Myofibrillar Proteolysis in Chick Myotubes during Oxidative Stress

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Changes in protein conformation and proteolysis in chick myotubes in response to the induction of oxidative stress by H_2O_2 treatment were studied. Myotubes were treated for 1 h with H_2O_2. After this treatment, the H_2O_2 was removed and the cells were cultured in serum-free medium for 6 and 24 h. Protein carbonyl content, as an index of protein modification, was increased at 6 and 24 h after H_2O_2 treatment. N^τ-methylhistidine release, as an index of myofibrillar proteolysis, was also increased at 6 and 24 h after H_2O_2 treatment. Calpain and cathepsin (B+L and D) activities were increased at 24 but not 6 h after H_2O_2 treatment. Proteasome activity was increased at 6 and 24 h after H_2O_2 treatment. These results indicate that oxidative stress increased proteasome activity and caused an increase in myofibrillar proteolysis during short-term incubation, whereas it increased calpain, proteasome and cathepsin activities during long-term incubation, finally resulting in an increase of myofibrillar proteolysis in chick myotubes.
日本ビタミン学会の論文