Abstract
In our recent study was shown a significant recovery of damaged skeletal muscle of mice with X-linked muscular dystrophy (mdx) following low-intensity endurance exercise, probably by reducing the degeneration of dystrophic muscle. Consequently, in the present work, we aimed to identify proteins involved in the observed reduction in degenerating fibres. To this end, we used proteomic analysis to evaluate changes in the protein profile of quadriceps dystrophic muscles of exercised compared with sedentary mdx mice. Four protein spots were found to be significantly changed and were identified as three isoforms of carbonic anhydrase 3 (CA3) and superoxide dismutase [Cu-Zn] (SODC). Protein levels of CA3 isoforms were significantly up-regulated in quadriceps of sedentary mdx mice and were completely restored to wild-type (WT) mice values, both sedentary and exercised, in quadriceps of exercised mdx mice. Protein levels of SODC were down-regulated in quadriceps of sedentary mdx mice and were significantly restored to WT mice values, both sedentary and exercised, in quadriceps of exercised mdx mice. Western blot data were in agreement with those obtained using proteomic analysis and revealed the presence of one more CA3 isoform that was significantly changed. Based on data found in the present study, it seems that low-intensity endurance exercise may in part contribute to reduce cell degeneration process in mdx muscles, by counteracting oxidative stress.
Highlights
Duchenne muscular dystrophy (DMD) is a lethal X-linked muscle disease due to a defect in the sub-sarcolemmal protein dystrophin, which leads to membrane fragility, muscle necrosis, motor weakness, myofibre death and replacement of skeletal muscle by fibrous and fatty connective tissue, due to failed regeneration [1]
Over the last few years, MS-based proteomics has been successfully applied to investigate normal and pathologically-altered skeletal muscle tissue [3], including the proteomic profiling of muscle tissues from mdx mice that has revealed differential degrees of perturbed protein expression patterns in dystrophin-deficient fibres [4]. Many of these proteomic analyses on muscles of mice with X-linked muscular dystrophy and DMD have been performed with the aim of unravelling the molecular pathogenesis of muscular dystrophy [5] and these analyses discovered several proteins
Quadriceps proteins purified from sedentary wild-type mice (WT-Sed), WT-Ex, sedentary mice with X-linked muscular dystrophy (MDX-Sed) and exercised mice with X-linked muscular dystrophy (MDX-Ex) mice were analysed by 2D gel electrophoresis (2DE) analysis
Summary
Duchenne muscular dystrophy (DMD) is a lethal X-linked muscle disease due to a defect in the sub-sarcolemmal protein dystrophin, which leads to membrane fragility, muscle necrosis, motor weakness, myofibre death and replacement of skeletal muscle by fibrous and fatty connective tissue, due to failed regeneration [1]. Over the last few years, MS-based proteomics has been successfully applied to investigate normal and pathologically-altered skeletal muscle tissue [3], including the proteomic profiling of muscle tissues from mdx mice that has revealed differential degrees of perturbed protein expression patterns in dystrophin-deficient fibres [4]. Many of these proteomic analyses on muscles of mice with X-linked muscular dystrophy (mdx) and DMD have been performed with the aim of unravelling the molecular pathogenesis of muscular dystrophy [5] and these analyses discovered several proteins c 2015 Authors. This large number of proteins change has hampered the possibility of developing therapeutic approach to muscular dystrophy by targeting proteins modified
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