PROTEIN CARBONYLATION AS A MAJOR HALLMARK OF OXIDATIVE DAMAGE: UPDATE OF ANALYTICAL STRATEGIES

被引:393
作者
Fedorova, Maria [1 ,2 ]
Bollineni, Ravi Chand [1 ,2 ]
Hoffmann, Ralf [1 ,2 ]
机构
[1] Univ Leipzig, Inst Bioanalyt Chem, Fac Chem & Mineral, D-04103 Leipzig, Germany
[2] Univ Leipzig, Ctr Biotechnol & Biomed BBZ, D-04103 Leipzig, Germany
关键词
TANDEM MASS-SPECTROMETRY; 2-DIMENSIONAL LIQUID-CHROMATOGRAPHY; HISTIDINE-CONTAINING PEPTIDES; STRESS-INDUCED CARBONYLATION; METAL-CATALYZED OXIDATION; LOSS-DRIVEN MS3; OXIDIZED PROTEINS; REACTIVE OXYGEN; LIPID-PEROXIDATION; PROTEOMIC IDENTIFICATION;
D O I
10.1002/mas.21381
中图分类号
O433 [光谱学];
学科分类号
0703 ; 070302 ;
摘要
Protein carbonylation, one of the most harmful irreversible oxidative protein modifications, is considered as a major hallmark of oxidative stress-related disorders. Protein carbonyl measurements are often performed to assess the extent of oxidative stress in the context of cellular damage, aging and several age-related disorders. A wide variety of analytical techniques are available to detect and quantify protein-bound carbonyls generated by metal-catalyzed oxidation, lipid peroxidation or glycation/glycoxidation. Here we review current analytical approaches for protein carbonyl detection with a special focus on mass spectrometry-based techniques. The utility of several carbonyl-derivatization reagents, enrichment protocols and especially advanced mass spectrometry techniques are compared and discussed in detail. Furthermore, the mechanisms and biology of protein carbonylation are summarized based on recent high-throughput proteomics data. Copyright © 2013 Wiley Periodicals, Inc.
引用
收藏
页码:79 / 97
页数:19
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