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<a href="http://doi.org/10.1074/jbc.M109.056846" target="_blank" rel="noreferrer noopener">http://doi.org/10.1074/jbc.M109.056846</a>
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Pages
3168-3180
Issue
5
Volume
285
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Title
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Peptide-based Antibodies against Glutathione-binding Domains Suppress Superoxide Production Mediated by Mitochondrial Complex I
Publisher
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Journal of Biological Chemistry
Date
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2010
2010-01
Subject
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oxidative stress; Biochemistry & Molecular Biology; nitric-oxide; proteins; site; generation; s-nitrosylation; postischemic heart; radical formation; bovine heart-mitochondria; nadh-ubiquinone oxidoreductase
Creator
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Chen J F; Chen C L; Rawale S; Chen C A; Zweier J L; Kaumaya P T P; Chen Y R
Description
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Complex I (NQR) is a critical site of superoxide (O-2(radical anion)) production and the major host of redox protein thiols in mitochondria. In response to oxidative stress, NQR-derived protein thiols at the 51- and 75-kDa subunits are known to be reversibly S-glutathionylated. Although several glutathionylated domains from NQR 51 and 75 kDa have been identified, their roles in the regulatory functions remain to be explored. To gain further insights into protein S-glutathionylation of complex I, we used two peptides of S-glutathionylated domain ((200)GAGAYI (C) under bar GEETALIESIEGK(219) of 51-kDa protein and (VDSDTL)-V-361 (C) under bar TEEVFPTAGAGTDLR(382) of 75-kDa protein) as chimeric epitopes incorporating a "promiscuous" T-cell epitope to generate two polyclonal antibodies, AbGSCA206 and AbGSCB367. Binding of AbGSCA206 and AbGSCB367 inhibited NQR-mediated O-2(radical anion). generation by 37 and 57%, as measured by EPR spin-trapping. To further provide an appropriate control, two peptides of non-glutathionylated domain ((21)SGDTTAPKKTSFGSLKDFDR(40) of 51-kDa peptide and (100)WNILTNSEKTKKAREGVMEFL(120) of 75-kDa peptide) were synthesized as chimeric epitopes to generate two polyclonal antibodies, Ab51 and Ab75. Binding of A51 did not affect NQR-mediated O-2(radical anion) generation to a significant level. However, binding of Ab75 inhibited NQR- mediated O-2(radical anion) generation by 35%. None of AbGSCA206, AbGSCB367, Ab51, or Ab75 showed an inhibitory effect on the electron transfer activity of NQR, suggesting that antibody binding to the glutathione-binding domain decreased electron leakage from the hydrophilic domain of NQR. When heart tissue homogenates were immunoprecipitated with Ab51 or Ab75 and probed with an antibody against glutathione, protein S-glutathionylation was enhanced in post-ischemic myocardium at the NQR 51-kDa subunit, but not at the 75-kDa subunit, indicating that the 51-kDa subunit of flavin subcomplex is more sensitive to oxidative stress resulting from myocardial infarction.
Identifier
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<a href="http://doi.org/10.1074/jbc.M109.056846" target="_blank" rel="noreferrer noopener">10.1074/jbc.M109.056846</a>
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Journal Article or Conference Abstract Publication
2010
Biochemistry & Molecular Biology
bovine heart-mitochondria
Chen C A
Chen C L
Chen J F
Chen Y R
generation
Journal Article or Conference Abstract Publication
Journal of Biological Chemistry
Kaumaya P T P
nadh-ubiquinone oxidoreductase
nitric-oxide
Oxidative Stress
postischemic heart
Proteins
radical formation
Rawale S
s-nitrosylation
site
Zweier J L