Document Detail


Novel oxidative modifications in redox-active cysteine residues.
MedLine Citation:
PMID:  21148632     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Redox-active cysteine, a highly reactive sulfhydryl, is one of the major targets of ROS. Formation of disulfide bonds and other oxidative derivatives of cysteine including sulfenic, sulfinic, and sulfonic acids, regulates the biological function of various proteins. We identified novel low-abundant cysteine modifications in cellular GAPDH purified on 2-dimensional gel electrophoresis (2D-PAGE) by employing selectively excluded mass screening analysis for nano ultraperformance liquid chromatography-electrospray-quadrupole-time of flight tandem mass spectrometry, in conjunction with MODi and MODmap algorithm. We observed unexpected mass shifts (Δm=-16, -34, +64, +87, and +103 Da) at redox-active cysteine residue in cellular GAPDH purified on 2D-PAGE, in oxidized NDP kinase A, peroxiredoxin 6, and in various mitochondrial proteins. Mass differences of -16, -34, and +64 Da are presumed to reflect the conversion of cysteine to serine, dehydroalanine (DHA), and Cys-SO2-SH respectively. To determine the plausible pathways to the formation of these products, we prepared model compounds and examined the hydrolysis and hydration of thiosulfonate (Cys-S-SO2-Cys) either to DHA (Δm=-34 Da) or serine along with Cys-SO2-SH (Δm=+64 Da). We also detected acrylamide adducts of sulfenic and sulfinic acids (+87 and +103 Da). These findings suggest that oxidations take place at redox-active cysteine residues in cellular proteins, with the formation of thiosulfonate, Cys-SO2-SH, and DHA, and conversion of cysteine to serine, in addition to sulfenic, sulfinic and sulfonic acids of reactive cysteine.
Authors:
Jaeho Jeong; Yongsik Jung; Seungjin Na; Jihye Jeong; Eunsun Lee; Mi-Sun Kim; Sun Choi; Dong-Hae Shin; Eunok Paek; Hee-Yoon Lee; Kong-Joo Lee
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2010-12-10
Journal Detail:
Title:  Molecular & cellular proteomics : MCP     Volume:  10     ISSN:  1535-9484     ISO Abbreviation:  Mol. Cell Proteomics     Publication Date:  2011 Mar 
Date Detail:
Created Date:  2011-03-02     Completed Date:  2011-06-16     Revised Date:  2013-07-03    
Medline Journal Info:
Nlm Unique ID:  101125647     Medline TA:  Mol Cell Proteomics     Country:  United States    
Other Details:
Languages:  eng     Pagination:  M110.000513     Citation Subset:  IM    
Affiliation:
The Center for Cell Signaling & Drug Discovery Research, College of Pharmacy, Division of Life & Pharmaceutical Sciences, Department of Bioinspired Science, Ewha Womans University, Seoul, Korea 120-750.
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MeSH Terms
Descriptor/Qualifier:
Alanine / analogs & derivatives,  metabolism
Amino Acid Sequence
Animals
Catalytic Domain
Cysteine / metabolism*
Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating) / chemistry,  metabolism
HEK293 Cells
Humans
Mass Spectrometry
Mice
Mitochondrial Proteins / chemistry,  metabolism
Molecular Sequence Data
Mutant Proteins / chemistry,  metabolism
Nucleoside-Diphosphate Kinase / chemistry,  metabolism
Oxidation-Reduction
Peptides / chemistry,  metabolism
Peroxiredoxin VI / chemistry,  metabolism
Protein Processing, Post-Translational*
Recombinant Proteins / chemistry,  metabolism
Serine / metabolism
Sulfenic Acids / metabolism
Sulfinic Acids / metabolism
Chemical
Reg. No./Substance:
0/Mitochondrial Proteins; 0/Mutant Proteins; 0/Peptides; 0/Recombinant Proteins; 0/Sulfenic Acids; 0/Sulfinic Acids; 1948-56-7/dehydroalanine; 52-90-4/Cysteine; 56-41-7/Alanine; 56-45-1/Serine; EC 1.11.1.15/Peroxiredoxin VI; EC 1.11.1.15/Prdx6 protein, mouse; EC 1.2.1.12/Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating); EC 2.7.4.6/Nucleoside-Diphosphate Kinase
Comments/Corrections

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