TY - JOUR
T1 - Proteomic analysis and protein carbonylation profile in trained and untrained rat muscles
AU - Magherini, Francesca
AU - Abruzzo, Provvidenza Maria
AU - Puglia, Michele
AU - Bini, Luca
AU - Gamberi, Tania
AU - Esposito, Fabio
AU - Veicsteinas, Arsenio
AU - Marini, Marina
AU - Fiorillo, Claudia
AU - Gulisano, Massimo
AU - Modesti, Alessandra
PY - 2012/1/4
Y1 - 2012/1/4
N2 - 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.
AB - 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.
KW - Carbonylation
KW - Exercise training
KW - Muscle
KW - Oxidative stress
KW - Oxyblots
KW - Two dimensional gel electrophoresis
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U2 - 10.1016/j.jprot.2011.10.017
DO - 10.1016/j.jprot.2011.10.017
M3 - Article
C2 - 22062160
AN - SCOPUS:84355166450
VL - 75
SP - 978
EP - 992
JO - Journal of Proteomics
JF - Journal of Proteomics
SN - 1874-3919
IS - 3
ER -