Irreversible plasma and muscle protein oxidation and physical exercise.


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
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

Pagination

126-138

Auteurs

Giulia Gorini (G)

a Department of Biomedical, Experimental and Clinical Sciences "Mario Serio" , University of Florence , Florence , Italy.

Tania Gamberi (T)

a Department of Biomedical, Experimental and Clinical Sciences "Mario Serio" , University of Florence , Florence , Italy.

Tania Fiaschi (T)

a Department of Biomedical, Experimental and Clinical Sciences "Mario Serio" , University of Florence , Florence , Italy.

Michele Mannelli (M)

a Department of Biomedical, Experimental and Clinical Sciences "Mario Serio" , University of Florence , Florence , Italy.

Alessandra Modesti (A)

a Department of Biomedical, Experimental and Clinical Sciences "Mario Serio" , University of Florence , Florence , Italy.

Francesca Magherini (F)

a Department of Biomedical, Experimental and Clinical Sciences "Mario Serio" , University of Florence , Florence , Italy.

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Classifications MeSH