FORUM: Redox Proteomics: from Protein Modifications to Cellular Dysfunction and Disease.
Protein carbonylation and muscle function in COPD and other conditions
Article first published online: 24 OCT 2013
© 2013 Wiley Periodicals, Inc.
Mass Spectrometry Reviews
Special Issue: Special Issue on Redox Proteomics Part 3
Volume 33, Issue 3, pages 219–236, May/June 2014
How to Cite
Barreiro, E. (2014), Protein carbonylation and muscle function in COPD and other conditions. Mass Spectrom. Rev., 33: 219–236. doi: 10.1002/mas.21394
- Issue published online: 28 MAR 2014
- Article first published online: 24 OCT 2013
- Manuscript Revised: 17 JUN 2013
- Manuscript Accepted: 17 JUN 2013
- Manuscript Received: 21 JAN 2013
- CIBERES. Grant Numbers: FIS 11/02029, FIS 12/02534, 2009-SGR-393, SAF 2011-26908, SEPAR 2010, FUCAP 2011, FUCAP 2012
- Marató TV3. Grant Number: MTV3-07-1010
- protein carbonylation;
- muscle function;
- disuse muscle atrophy;
- cancer cachexia;
Skeletal muscle, the most abundant tissue in mammals, is essential for any activity in life. Muscle dysfunction is a common systemic manifestation in highly prevalent conditions such as chronic obstructive pulmonary disease (COPD), cancer cachexia, and sepsis. It has a significant impact on exercise tolerance, thus worsening the patients' quality of life and survival. Among several factors, oxidative stress is a major player in the etiology of skeletal muscle dysfunction associated with those conditions. Whereas low levels of oxidants are absolutely required for normal cell adaptation, high levels of reactive oxygen species (ROS) alter the function and structure of molecules such as proteins, DNA, and lipids. Specifically, protein carbonylation, a common variety of protein oxidation, was shown to alter the function of key enzymes and structural proteins involved in muscle contractile performance. Moreover, increased levels of ROS may also activate proteolytic systems, thus leading to enhanced protein breakdown in several models. In the current review, the specific modifications induced by carbonylation in protein structure and function in muscles have been described. Furthermore, the potential role of ROS in the activation of proteolytic systems in skeletal muscles is also discussed. The review summarizes the effects of protein carbonylation on muscles in several models and conditions such as COPD, disuse muscle atrophy, cancer cachexia, sepsis, and aging. Future research should focus on the elucidation of the specific protein sites modified by ROS in these muscles using redox proteomics analyses and on the assessment of the consequent alterations in protein function and stability. © 2013 Wiley Periodicals, Inc. Mass Spec Rev 33: 219–236, 2014.