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Proteomic and Carbonylation Profile Analysis of Rat Skeletal Muscles following Acute Swimming Exercise

Previous studies by us and other groups characterized protein expression variation following long-term moderate training, whereas the effects of single bursts of exercise are less known. Making use of a proteomic approach, we investigated the effects of acute swimming exercise (ASE) on protein expre...

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Autores principales: Magherini, Francesca, Gamberi, Tania, Pietrovito, Laura, Fiaschi, Tania, Bini, Luca, Esposito, Fabio, Marini, Marina, Abruzzo, Provvidenza Maria, Gulisano, Massimo, Modesti, Alessandra
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3742498/
https://www.ncbi.nlm.nih.gov/pubmed/23967250
http://dx.doi.org/10.1371/journal.pone.0071839
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author Magherini, Francesca
Gamberi, Tania
Pietrovito, Laura
Fiaschi, Tania
Bini, Luca
Esposito, Fabio
Marini, Marina
Abruzzo, Provvidenza Maria
Gulisano, Massimo
Modesti, Alessandra
author_facet Magherini, Francesca
Gamberi, Tania
Pietrovito, Laura
Fiaschi, Tania
Bini, Luca
Esposito, Fabio
Marini, Marina
Abruzzo, Provvidenza Maria
Gulisano, Massimo
Modesti, Alessandra
author_sort Magherini, Francesca
collection PubMed
description Previous studies by us and other groups characterized protein expression variation following long-term moderate training, whereas the effects of single bursts of exercise are less known. Making use of a proteomic approach, we investigated the effects of acute swimming exercise (ASE) on protein expression and carbonylation patterns in two hind limb muscles: the Extensor Digitorum Longus (EDL) and the Soleus, mostly composed of fast-twitch and slow-twitch fibres, respectively. Carbonylation is one of the most common oxidative modifications of proteins and a marker of oxidative stress. In fact, several studies suggest that physical activity and the consequent increase in oxygen consumption can lead to increase in reactive oxygen and nitrogen species (RONS) production, hence the interest in examining the impact of RONS on skeletal muscle proteins following ASE. Results indicate that protein expression is unaffected by ASE in both muscle types. Unexpectedly, the protein carbonylation level was reduced following ASE. In particular, the analysis found 31 and 5 spots, in Soleus and EDL muscles respectively, whose carbonylation is reduced after ASE. Lipid peroxidation levels in Soleus were markedly reduced as well. Most of the decarbonylated proteins are involved either in the regulation of muscle contractions or in the regulation of energy metabolism. A number of hypotheses may be advanced to account for such results, which will be addressed in future studies.
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spelling pubmed-37424982013-08-21 Proteomic and Carbonylation Profile Analysis of Rat Skeletal Muscles following Acute Swimming Exercise Magherini, Francesca Gamberi, Tania Pietrovito, Laura Fiaschi, Tania Bini, Luca Esposito, Fabio Marini, Marina Abruzzo, Provvidenza Maria Gulisano, Massimo Modesti, Alessandra PLoS One Research Article Previous studies by us and other groups characterized protein expression variation following long-term moderate training, whereas the effects of single bursts of exercise are less known. Making use of a proteomic approach, we investigated the effects of acute swimming exercise (ASE) on protein expression and carbonylation patterns in two hind limb muscles: the Extensor Digitorum Longus (EDL) and the Soleus, mostly composed of fast-twitch and slow-twitch fibres, respectively. Carbonylation is one of the most common oxidative modifications of proteins and a marker of oxidative stress. In fact, several studies suggest that physical activity and the consequent increase in oxygen consumption can lead to increase in reactive oxygen and nitrogen species (RONS) production, hence the interest in examining the impact of RONS on skeletal muscle proteins following ASE. Results indicate that protein expression is unaffected by ASE in both muscle types. Unexpectedly, the protein carbonylation level was reduced following ASE. In particular, the analysis found 31 and 5 spots, in Soleus and EDL muscles respectively, whose carbonylation is reduced after ASE. Lipid peroxidation levels in Soleus were markedly reduced as well. Most of the decarbonylated proteins are involved either in the regulation of muscle contractions or in the regulation of energy metabolism. A number of hypotheses may be advanced to account for such results, which will be addressed in future studies. Public Library of Science 2013-08-13 /pmc/articles/PMC3742498/ /pubmed/23967250 http://dx.doi.org/10.1371/journal.pone.0071839 Text en © 2013 Magherini et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Magherini, Francesca
Gamberi, Tania
Pietrovito, Laura
Fiaschi, Tania
Bini, Luca
Esposito, Fabio
Marini, Marina
Abruzzo, Provvidenza Maria
Gulisano, Massimo
Modesti, Alessandra
Proteomic and Carbonylation Profile Analysis of Rat Skeletal Muscles following Acute Swimming Exercise
title Proteomic and Carbonylation Profile Analysis of Rat Skeletal Muscles following Acute Swimming Exercise
title_full Proteomic and Carbonylation Profile Analysis of Rat Skeletal Muscles following Acute Swimming Exercise
title_fullStr Proteomic and Carbonylation Profile Analysis of Rat Skeletal Muscles following Acute Swimming Exercise
title_full_unstemmed Proteomic and Carbonylation Profile Analysis of Rat Skeletal Muscles following Acute Swimming Exercise
title_short Proteomic and Carbonylation Profile Analysis of Rat Skeletal Muscles following Acute Swimming Exercise
title_sort proteomic and carbonylation profile analysis of rat skeletal muscles following acute swimming exercise
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3742498/
https://www.ncbi.nlm.nih.gov/pubmed/23967250
http://dx.doi.org/10.1371/journal.pone.0071839
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