TITLE

Quantitative Proteomic Profiling of Muscle Type-Dependent and Age-Dependent Protein Carbonylation in Rat Skeletal Muscle Mitochondria

AUTHOR(S)
Feng, Juan; Hongwei Xie; Meany, Danni L.; Thompson, LaDora V.; Arriaga, Edgar A.; Griffin, Timothy J.
PUB. DATE
November 2008
SOURCE
Journals of Gerontology Series A: Biological Sciences & Medical ;Nov2008, Vol. 63 Issue 11, p1137
SOURCE TYPE
Academic Journal
DOC. TYPE
Article
ABSTRACT
Carbonylation is a highly prevalent protein modification in skeletal muscle mitochondria, possibly contributing to its functional decline with age. Using quantitative proteomics, we identified mitochondrial proteins susceptible to carbonylation in a muscle type (slow- vs fast- twitch)-dependent and age-dependent manner from Fischer 344 rat skeletal muscle. Fast-twitch muscle contained twice as many carbonylated mitochondrial proteins than did slow-twitch muscle, with 22 proteins showing significant changes in carbonylation state with age, the majority of these increasing in their amount of carbonylation. Ingenuity pathway analysis revealed that these proteins belong to functional classes and pathways known to be impaired in muscle aging, including cellular function and maintenance, fatty acid metabolism, and citrate cycle. Although our studies do not conclusively link protein carbonylation to these functional changes in aging muscle, they provide a unique catalogue of promising protein targets deserving further investigation because of their potential role in aging muscle decline.
ACCESSION #
35725374

 

Related Articles

  • Redox State and Mitochondrial Respiratory Chain Function in Skeletal Muscle of LGMD2A Patients. Nilsson, Mats I.; Macneil, Lauren G.; Kitaoka, Yu; Alqarni, Fatimah; Suri, Rahul; Akhtar, Mahmood; Haikalis, Maria E.; Dhaliwal, Pavneet; Saeed, Munim; Tarnopolsky, Mark A. // PLoS ONE;Jul2014, Vol. 9 Issue 7, p1 

    Background: Calpain-3 deficiency causes oxidative and nitrosative stress-induced damage in skeletal muscle of LGMD2A patients, but mitochondrial respiratory chain function and anti-oxidant levels have not been systematically assessed in this clinical population previously. Methods: We identified...

  • Application of redox proteomics to skeletal muscle aging and exercise. McDonagh, Brian; Sakellariou, Giorgos K.; Jackson, Malcolm J. // Biochemical Society Transactions;Aug2014, Vol. 42 Issue 4, p965 

    Skeletal muscle represents a physiologically relevant model for the application of redox proteomic techniques to dissect its response to exercise and aging. Contracting skeletal muscles generate ROS (reactive oxygen species) and RNS (reactive nitrogen species) necessary for the regulation of...

  • MIA40 is an oxidoreductase that catalyzes oxidative protein folding in mitochondria. Banci, Lucia; Bertini, Ivano; Cefaro, Chiara; Ciofi-Baffoni, Simone; Gallo, Angelo; Martinelli, Manuele; Sideris, Dionisia P; Katrakili, Nitsa; Tokatlidis, Kostas // Nature Structural & Molecular Biology;Feb2009, Vol. 16 Issue 2, p198 

    MIA40 has a key role in oxidative protein folding in the mitochondrial intermembrane space. We present the solution structure of human MIA40 and its mechanism as a catalyst of oxidative folding. MIA40 has a 66-residue folded domain made of an α-helical hairpin core stabilized by two...

  • Structural and Functional Diversity of Glutaredoxins in Yeast. Herrero, Enrique; Bell�, Gemma; Casas, Celia // Current Protein & Peptide Science;Dec2010, Vol. 11 Issue 8, p659 

    No abstract available.

  • Systematic Exploration of Thioredoxin Target Proteins in Plant Mitochondria. Yoshida, Keisuke; Noguchi, Ko; Motohashi, Ken; Hisabori, Toru // Plant & Cell Physiology;Jun2013, Vol. 54 Issue 6, p875 

    The thioredoxin (Trx) system is known to play a pivotal role in cellular redox regulation, but its target proteins in plant mitochondria remain largely uncharacterized. In this study, we systemically screened Trx target candidates in plant mitochondria. Mitochondrial protein extracts were...

  • Proteomic Strategies for the Analysis of Carbonyl Groups on Proteins. Irazusta, Ver�nica; Moreno-Cerme�o, Armando; Cabiscol, Elisa; Tamarit, Jordi; Ros, Joaquim // Current Protein & Peptide Science;Dec2010, Vol. 11 Issue 8, p652 

    No abstract available.

  • Redox proteomics: basic principles and future perspectives for the detection of protein oxidation in plants. Rinalducci, Sara; Murgiano, Leonardo; Zolla, Lello // Journal of Experimental Botany;Oct2008, Vol. 59 Issue 14, p3781 

    The production and scavenging of chemically reactive species, such as ROS/RNS, are central to a broad range of biotic and abiotic stress and physiological responses in plants. Among the techniques developed for the identification of oxidative stress-induced modifications on proteins, the...

  • Development and application of site-specific proteomic approach for study protein S-nitrosylation. Liu, Miao; Talmadge, James; Ding, Shi-Jian // Amino Acids;May2012, Vol. 42 Issue 5, p1541 

    Protein S-nitrosylation is the covalent redox-related modification of cysteine sulfhydryl groups with nitric oxide, creating a regulatory impact similar to phosphorylation. Recent studies have reported a growing number of proteins to be S-nitrosylated in vivo resulting in altered functions....

  • Redox regulation of OxyR requires specific disulfide bond formation involving a rapid kinetic reaction path. Cheolju Lee; Soon Mi Lee; Mukhopadhyay, Partha; Seung Jun Kim; Sang Chul Lee; Woo-Sung Ahn; Myeong-Hee Yu; Storz, Gisela; Seong Eon Ryu // Nature Structural & Molecular Biology;Dec2004, Vol. 11 Issue 12, p1179 

    The Escherichia coli OxyR transcription factor is activated by cellular hydrogen peroxide through the oxidation of reactive cysteines. Although there is substantial evidence for specific disulfide bond formation in the oxidative activation of OxyR, the presence of the disulfide bond has remained...

Share

Read the Article

Courtesy of THE LIBRARY OF VIRGINIA

Sorry, but this item is not currently available from your library.

Try another library?
Sign out of this library

Other Topics