Proteomic analysis and protein carbonylation profile in trained and untrained rat muscles

Magherini, Francesca; Abruzzo, Provvidenza Maria; Puglia, Michele; Bini, Luca; Gamberi, Tania; Esposito, Fabio; Veicsteinas, Arsenio; Marini, Marina; Fiorillo, Claudia; Gulisano, Massimo; Modesti, Alessandra

doi:10.1016/j.jprot.2011.10.017

Cited by 33 publications

(43 citation statements)

References 53 publications

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“…Carbonyls groups were derivatized into their DNP adducts using DNPH and these were detected by carbonylated protein Western blot. In wild-type muscle, total protein carbonylation levels increased 1 h after exercise (P o 0.05) and remained elevated 2 days after, as observed in previous studies [42]. Interestingly, in mdx muscle, total protein carbonylation level was not significantly different after exercise (Fig.…”

Section: Total Protein Carbonylation Level After Low Intensity Swimmingsupporting

confidence: 85%

Low intensity training of mdx mice reduces carbonylation and increases expression levels of proteins involved in energy metabolism and muscle contraction

Hyzewicz

Tanihata

Kuraoka

et al. 2015

Free Radical Biology and Medicine

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High intensity training induces muscle damage in dystrophin-deficient mdx mice, an animal model for Duchenne muscular dystrophy. However, low intensity training (LIT) rescues the mdx phenotype and even reduces the level of protein carbonylation, a marker of oxidative damage. Until now, beneficial effects of LIT were mainly assessed at the physiological level. We investigated the effects of LIT at the molecular level on 8-week-old wild-type and mdx muscle using 2D Western blot and protein-protein interaction analysis. We found that the fast isoforms of troponin T and myosin binding protein C as well as glycogen phosphorylase were overcarbonylated and downregulated in mdx muscle. Some of the mitochondrial enzymes of the citric acid cycle were overcarbonylated, whereas some proteins of the respiratory chain were downregulated. Of functional importance, ATP synthase was only partially assembled, as revealed by Blue Native PAGE analysis. LIT decreased the carbonylation level and increased the expression of fast isoforms of troponin T and of myosin binding protein C, and glycogen phosphorylase. In addition, it increased the expression of aconitate hydratase and NADH dehydrogenase, and fully restored the ATP synthase complex. Our study demonstrates that the benefits of LIT are associated with lowered oxidative damage as revealed by carbonylation and higher expression of proteins involved in energy metabolism and muscle contraction. Potentially, these results will help to design therapies for DMD based on exercise mimicking drugs.

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Section: Total Protein Carbonylation Level After Low Intensity Swimmingsupporting

confidence: 85%

Low intensity training of mdx mice reduces carbonylation and increases expression levels of proteins involved in energy metabolism and muscle contraction

Hyzewicz

Tanihata

Kuraoka

et al. 2015

Free Radical Biology and Medicine

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“…It has been recently demonstrated that enolase isoforms interact with microtubules during muscle satellite cell differentiation contributing to the regulation of the cytoskeletal filaments dynamism that occurs during the transition from myoblasts to myotubes. 47,48 NLR family pyrin domaincontaining protein 10 (NLRP 10), heterogeneous nuclear ribonucleoprotein K (HNRNP K) and galectin-3 following the PANTHER classification system were assigned to the ''induction of apoptosis'' class but they are also involved in other important processes. .…”

Section: Molecular Biosystems Papermentioning

confidence: 99%

Effect of IR laser on myoblasts: a proteomic study

et al. 2013

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Laser therapy is used in physical medicine and rehabilitation to accelerate muscle recovery and in sports medicine to prevent damages produced by metabolic disturbances and inflammatory reactions after heavy exercise. The aim of this research was to get insight into possible benefits deriving from the application of an advanced IR laser system to counteract deficits of muscle energy metabolism and stimulate the recovery of hypotrophic tissue. We studied the effect of IR laser treatment on proliferation, differentiation, cytoskeleton organization and global protein expression in C2C12 myoblasts. We found that laser treatment induced a decrease in the cell proliferation rate without affecting cell viability, while leading to cytoskeletal rearrangement and expression of the early differentiation marker MyoD. The differential proteome analysis revealed the up-regulation and/or modulation of many proteins known to be involved in cell cycle regulation, cytoskeleton organization and differentiation.

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“…This increase is consistent with that observed in other studies where a different animal model was used. 22,23 One possible explanation of this difference can be based on the fact that H and TA mitochondria are involved in Figure 8. MS/MS fragmentation spectra showing the occurrence of oxidation (Leu-HydroxiLeu) on ATP synthase and several different oxidation sites on aconitate hydratase.…”

Section: ■ Discussion and Conclusionmentioning

confidence: 99%

Profiling Carbonylated Proteins in Heart and Skeletal Muscle Mitochondria from Trained and Untrained Mice

Carpentieri¹,

Gamberi

Modesti

et al. 2016

J. Proteome Res.

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Understanding the relationship between physical exercise, reactive oxygen species, and skeletal muscle modification is important in order to better identify the benefits or the damages that appropriate or inappropriate exercise can induce. Heart and skeletal muscles have a high density of mitochondria with robust energetic demands, and mitochondria plasticity has an important role in both the cardiovascular system and skeletal muscle responses. The aim of this study was to investigate the influence of regular physical activity on the oxidation profiles of mitochondrial proteins from heart and tibialis anterior muscles. To this end, we used the mouse as animal model. Mice were divided into two groups: untrained and regularly trained. The carbonylated protein pattern was studied by two-dimensional gel electrophoresis followed by Western blot with anti-dinitrophenyl hydrazone antibodies. Mass spectrometry analysis allowed the identification of several different protein oxidation sites, including methionine, cysteine, proline, and leucine residues. A large number of oxidized proteins were found in both untrained and trained animals. Moreover, mitochondria from skeletal muscles and heart showed almost the same carbonylation pattern. Interestingly, exercise training seems to increase the carbonylation level mainly of mitochondrial proteins from skeletal muscle.

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Proteomic analysis and protein carbonylation profile in trained and untrained rat muscles

Cited by 33 publications

References 53 publications

Low intensity training of mdx mice reduces carbonylation and increases expression levels of proteins involved in energy metabolism and muscle contraction

Low intensity training of mdx mice reduces carbonylation and increases expression levels of proteins involved in energy metabolism and muscle contraction

Effect of IR laser on myoblasts: a proteomic study

Profiling Carbonylated Proteins in Heart and Skeletal Muscle Mitochondria from Trained and Untrained Mice

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