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

Authors :
Magherini, Francesca
Abruzzo, Provvidenza Maria
Puglia, Michele
Bini, Luca
Gamberi, Tania
Esposito, Fabio
Veicsteinas, Arsenio
Marini, Marina
Fiorillo, Claudia
Gulisano, Massimo
Modesti, Alessandra
Source :
Journal of Proteomics. Jan2012, Vol. 75 Issue 3, p978-992. 15p.
Publication Year :
2012

Abstract

Abstract: 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. Unbalanced ROS levels can lead to oxidation of cellular macromolecules and a major class of protein oxidative modification is carbonylation. The aim of this investigation was to study muscle protein expression and carbonylation patterns in trained and untrained animal models. We analyzed two muscles characterized by different metabolisms: tibialis anterior and soleus. Whilst tibialis anterior is mostly composed of fast-twitch fibers, the soleus muscle is mostly composed of slow-twitch fibers. By a proteomic approach we identified 15 protein spots whose expression is influenced by training. Among them in tibialis anterior we observed a down-regulation of several glycolitic enzymes. Concerning carbonylation, we observed the existence of a high basal level of protein carbonylation. Although this level shows some variation among individual animals, several proteins (mostly involved in energy metabolism, muscle contraction, and stress response) appear carbonylated in all animals and in both types of skeletal muscle. Moreover we identified 13 spots whose carbonylation increases after training. [Copyright &y& Elsevier]

Details

Language :
English
ISSN :
18743919
Volume :
75
Issue :
3
Database :
Academic Search Index
Journal :
Journal of Proteomics
Publication Type :
Academic Journal
Accession number :
70044537
Full Text :
https://doi.org/10.1016/j.jprot.2011.10.017