Lipid peroxide and antioxidant enzymes in muscle and nonmuscle of dystrophic mouse.

To determine whether abnormality in redox metabolism occurs specifically in certain individual dystrophic muscles, thiobarbituric acid reactivity, free radical scavengers, and oxidative marker enzymes were measured in the liver, kidney, erythrocytes, heart, and four different individual skeletal muscles from C57BL/6J dy/dy mice. Superoxide dismutases were assayed by specific radioimmunoassays, which enabled the study of a small individual murine muscle. Glutathione peroxidase and catalase were increased markedly in each individual dystrophic skeletal muscle studied and less markedly in the heart. Manganosuperoxide dismutase and thiobarbituric acid reactivity were decreased to a similar extent in each dystrophic skeletal muscle. Cuprozinc superoxide dismutase was decreased in the soleus muscle. Only a minimal biochemical change occurred in nonmuscles. Fumarase activity correlated closely with the level of manganosuperoxide dismutase. These results suggest that muscle protein breakdown occurs independently of lipid peroxidation despite the presence of tissue-specific abnormality of redox metabolism in dystrophic muscle.