Gel-free proteomic methodologies to study reversible cysteine oxidation and irreversible protein carbonyl formation

被引:15
作者
Boronat, S. [1 ]
Garcia-Santamarina, S. [2 ]
Hidalgo, E. [1 ]
机构
[1] Univ Pompeu Fabra, Dept Ciencies Expt & Salut, Oxidat Stress & Cell Cycle Grp, E-08003 Barcelona, Spain
[2] Duke Univ, Sch Med, Dept Pharmacol & Canc Biol, Durham, NC 27710 USA
关键词
Cys oxidation; H2O2; reactivity; protein carbonyl formation; redox proteomics; redox regulation; CODED AFFINITY TAG; HISTIDINE-CONTAINING PEPTIDES; METAL-CATALYZED OXIDATION; TANDEM MASS-SPECTROMETRY; LOW-DENSITY LIPOPROTEINS; S-NITROSYLATED PROTEINS; SULFENIC ACID FORMATION; REDOX PROTEOMICS; REDUCTIVE LIGATION; QUANTITATIVE-ANALYSIS;
D O I
10.3109/10715762.2015.1009053
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Oxidative modifications in proteins have been traditionally considered as hallmarks of damage by oxidative stress and aging. However, oxidants can generate a huge variety of reversible and irreversible modifications in amino acid side chains as well as in the protein backbones, and these post-translational modifications can contribute to the activation of signal transduction pathways, and also mediate the toxicity of oxidants. Among the reversible modifications, the most relevant ones are those arising from cysteine oxidation. Thus, formation of sulfenic acid or disulfide bonds is known to occur in many enzymes as part of their catalytic cycles, and it also participates in the activation of signaling cascades. Furthermore, these reversible modifications have been usually attributed with a protective role, since they may prevent the formation of irreversible damage by scavenging reactive oxygen species. Among irreversible modifications, protein carbonyl formation has been linked to damage and death, since it cannot be repaired and can lead to protein loss-of-function and to the formation of protein aggregates. This review is aimed at researchers interested on the biological consequences of oxidative stress, both at the level of signaling and toxicity. Here we are providing a concise overview on current mass-spectrometry-based methodologies to detect reversible cysteine oxidation and irreversible protein carbonyl formation in proteomes. We do not pretend to impose any of the different methodologies, but rather to provide an objective catwalk on published gel-free approaches to detect those two types of modifications, from a biologist's point of view.
引用
收藏
页码:494 / 510
页数:17
相关论文
共 150 条
[51]   Identification of S-nitrosylation motifs by site-specific mapping of the S-nitrosocysteine proteome in human vascular smooth muscle cells [J].
Greco, Todd M. ;
Hodara, Roberto ;
Parastatidis, Loannis ;
Heijnen, Harry F. G. ;
Dennehy, Michelle K. ;
Liebler, Daniel C. ;
Ischiropoulos, Harry .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2006, 103 (19) :7420-7425
[52]   Oxidative stress and covalent modification of protein with bioactive aldehydes [J].
Grimsrud, Paul A. ;
Xie, Hongwei ;
Griffin, Timothy J. ;
Bernlohr, David A. .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2008, 283 (32) :21837-21841
[53]   Resin-assisted enrichment of thiols as a general strategy for proteomic profiling of cysteine-based reversible modifications [J].
Guo, Jia ;
Gaffrey, Matthew J. ;
Su, Dian ;
Liu, Tao ;
Camp, David G., II ;
Smith, Richard D. ;
Qian, Wei-Jun .
NATURE PROTOCOLS, 2014, 9 (01) :64-75
[54]   To tag or not to tag: A comparative evaluation of immunoaffinity-labeling and tandem mass spectrometry for the identification and localization of posttranslational protein carbonylation by 4-hydroxy-2-nonenal, an end-product of lipid peroxidation [J].
Guo, Jia ;
Prokai, Laszlo .
JOURNAL OF PROTEOMICS, 2011, 74 (11) :2360-2369
[55]   Protein targets for carbonylation by 4-hydroxy-2-nonenal in rat liver mitochondria [J].
Guo, Jia ;
Prokai-Tatrai, Katalin ;
Vien Nguyen ;
Rauniyar, Navin ;
Ughy, Bettina ;
Prokai, Laszlo .
JOURNAL OF PROTEOMICS, 2011, 74 (11) :2370-2379
[56]   Quantitative analysis of complex protein mixtures using isotope-coded affinity tags [J].
Gygi, SP ;
Rist, B ;
Gerber, SA ;
Turecek, F ;
Gelb, MH ;
Aebersold, R .
NATURE BIOTECHNOLOGY, 1999, 17 (10) :994-999
[57]   Carbonyl-Reactive Tandem Mass Tags for the Proteome-Wide Quantification of N-Linked Glycans [J].
Hahne, Hannes ;
Neubert, Patrick ;
Kuhn, Karsten ;
Etienne, Chris ;
Bomgarden, Ryan ;
Rogers, John C. ;
Kuster, Bernhard .
ANALYTICAL CHEMISTRY, 2012, 84 (08) :3716-3724
[58]   Design, synthesis, and application of a hydrazide-functionalized isotope-coded affinity tag for the quantification of oxylipid-protein conjugates [J].
Han, Bingnan ;
Stevens, Jan F. ;
Maier, Claudia S. .
ANALYTICAL CHEMISTRY, 2007, 79 (09) :3342-3354
[59]   A comparative 'bottom up' proteomics strategy for the site-specific identification and quantification of protein modifications by electrophilic lipids [J].
Han, Bingnan ;
Hare, Michael ;
Wickramasekara, Samanthi ;
Fang, Yi ;
Maier, Claudia S. .
JOURNAL OF PROTEOMICS, 2012, 75 (18) :5724-5733
[60]   A PROCEDURE FOR QUANTITATIVE-DETERMINATION OF TRIS(2-CARBOXYETHYL)PHOSPHINE, AN ODORLESS REDUCING AGENT MORE STABLE AND EFFECTIVE THAN DITHIOTHREITOL [J].
HAN, JC ;
HAN, GY .
ANALYTICAL BIOCHEMISTRY, 1994, 220 (01) :5-10