Irreversible plasma and muscle protein oxidation and physical exercise.
Physical exercise
plasma
protein carbonylation
proteomics
skeletal muscle
Journal
Free radical research
ISSN: 1029-2470
Titre abrégé: Free Radic Res
Pays: England
ID NLM: 9423872
Informations de publication
Date de publication:
Feb 2019
Feb 2019
Historique:
pubmed:
5
12
2018
medline:
7
9
2019
entrez:
5
12
2018
Statut:
ppublish
Résumé
The imbalance between the reactive oxygen (ROS) and nitrogen (RNS) species production and their handling by the antioxidant machinery (low molecular weight antioxidant molecules and antioxidant enzymes), also known as oxidative stress, is a condition caused by physiological and pathological processes. Moreover, oxidative stress may be due to an overproduction of free radicals during physical exercise. Excess of radical species leads to the modification of molecules, such as proteins - the most susceptible to oxidative modification - lipids and DNA. With regard to the oxidation of proteins, carbonylation is an oxidative modification that has been widely described. Several studies have detected changes in the total amount of protein carbonyls following different types of physical exercise, but only few of these identified the specific amino acidic residues targets of such oxidation. In this respect, proteomic approaches allow to identify the proteins susceptible to carbonylation and in many cases, it is also possible to identify the specific protein carbonylation sites. This review focuses on the role of protein oxidation, and specifically carbonyl formation, for plasma and skeletal muscle proteins, following different types of physical exercise performed at different intensities. Furthermore, we focused on the proteomic strategies used to identify the specific protein targets of carbonylation. Overall, our analysis suggests that regular physical activity promotes a protection against protein carbonylation, due to the activation of the antioxidant defence or of the turnover of protein carbonyls. However, we can conclude that from the comprehensive bibliography analysed, there is no clearly defined specific physiological role about this post-translational modification of proteins.
Identifiants
pubmed: 30513020
doi: 10.1080/10715762.2018.1542141
doi:
Substances chimiques
Muscle Proteins
0
Types de publication
Journal Article
Review
Langues
eng
Sous-ensembles de citation
IM