1
40
3
-
Text
A resource consisting primarily of words for reading. Examples include books, letters, dissertations, poems, newspapers, articles, archives of mailing lists. Note that facsimiles or images of texts are still of the genre Text.
URL Address
<a href="http://doi.org/10.1021/bi9018237" target="_blank" rel="noreferrer noopener">http://doi.org/10.1021/bi9018237</a>
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Article information provided for research and reference use only. All rights are retained by the journal listed under publisher and/or the creator(s).
Pages
2529-2539
Issue
11
Volume
49
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Dublin Core
The Dublin Core metadata element set is common to all Omeka records, including items, files, and collections. For more information see, http://dublincore.org/documents/dces/.
Title
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Peroxynitrite-Mediated Oxidative Modifications of Complex II: Relevance in Myocardial Infarction
Publisher
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Biochemistry
Date
A point or period of time associated with an event in the lifecycle of the resource
2010
2010-03
Subject
The topic of the resource
Biochemistry & Molecular Biology; cytochrome-c; fatty-acids; identification; membrane; mitochondrial; modulation; nitric-oxide; postischemic heart; succinate-ubiquinone; thiyl
Creator
An entity primarily responsible for making the resource
Zhang L W; Chen C L; Kang P T; Garg V; Hu K L; Green-Church K B; Chen Y R
Description
An account of the resource
Increased O-2(center dot-) and NO production is a key mechanism of mitochondrial dysfunction in mycocardial ischemia/reperfusion injury. In complex impairment and enhanced tyrosine nitration of the 70 kDa FAD-binding protein occur in the post-ischemic myocardium and are thought to be mediated by peroxynitrite (OONO-) ill vivo [Chen, Y.-R., et ill. (2008) J. Biol. Chem. 283, 27991-28003]. To gain deeper insights into the redox protein thiols involved ill OONO--mediated Oxidative post-translational modifications relevant ill myocardial infarction, We subjected Isolated myocardial complex 11 to ill vltro protein nitration with OONO-. This resulted ill site-specific nitration at the 70 kDa polypeptide and impairment of complex II-derived electron transfer activity. Under reducing conditions, the gel band of the 70 kDa POlyPePtldC MIS subjected to in-gel trypsin/chymotrypsin digestion and then LC-MS/MS analysis Nitration Of Y-56 and Y-142 was previosly reported. Further analysis revealed that C-267, C-476 and C-537 are involved ill OONO--mediated S-sulfonation. To identify the disulfide formation mediated by OONO-, nitrated complex 11 was alkylated with iodoacetamide. In-gel proteolytic digestion and LC-MS/MS analysis were conducted under nonreducing conditions. The MS/MS data were examined with MassMatrix, indicating that three cysteine pairs, C-306-C-312,C-439-C-444, and C-288-C-575, were involved in OONO--mediated disulfide formation. Immuno-spin trapping with an anti-DMPO antibody and subsequent MS Was used to define Oxidative modification with protein radical formation. An OONO--dependent DMPO adduct was detected. and further LC-MS/MS analysis indicated C-288 and C-655 were involved in DMPO binding. These I-CSLIltS offered a complete profile of OONO--mediated Oxidative modifications that may be relevant Ill the disease model of myocardial infarction.
Identifier
An unambiguous reference to the resource within a given context
<a href="http://doi.org/10.1021/bi9018237" target="_blank" rel="noreferrer noopener">10.1021/bi9018237</a>
Format
The file format, physical medium, or dimensions of the resource
Journal Article
2010
BIOCHEMISTRY
Biochemistry & Molecular Biology
Chen C L
Chen Y R
cytochrome-c
fatty-acids
Garg V
Green-Church K B
Hu K L
identification
Journal Article
Kang P T
membrane
Mitochondrial
modulation
nitric-oxide
postischemic heart
succinate-ubiquinone
thiyl
Zhang L W
-
Text
A resource consisting primarily of words for reading. Examples include books, letters, dissertations, poems, newspapers, articles, archives of mailing lists. Note that facsimiles or images of texts are still of the genre Text.
URL Address
<a href="http://doi.org/10.1016/j.bbabio.2011.03.001" target="_blank" rel="noreferrer noopener">http://doi.org/10.1016/j.bbabio.2011.03.001</a>
Rights
Article information provided for research and reference use only. All rights are retained by the journal listed under publisher and/or the creator(s).
Pages
491-502
Issue
5
Volume
1807
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The Dublin Core metadata element set is common to all Omeka records, including items, files, and collections. For more information see, http://dublincore.org/documents/dces/.
Title
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Excess no predisposes mitochondrial succinate-cytochrome c reductase to produce hydroxyl radical
Publisher
An entity responsible for making the resource available
Biochimica Et Biophysica Acta-Bioenergetics
Date
A point or period of time associated with an event in the lifecycle of the resource
2011
2011-05
Subject
The topic of the resource
Mitochondria; Biophysics; oxygen; Biochemistry & Molecular Biology; nitric-oxide synthase; reactive; smooth-muscle-cells; endothelial-cells; reperfusion injury; EPR; postischemic heart; complex-ii; Electron transport chain; electron-transport; Hydroxyl radical; NO; oxygen-free radicals; SCR; spin trapping; superoxide generation
Creator
An entity primarily responsible for making the resource
Chen J F; Chen C L; Alevriadou B R; Zweier J L; Chen Y R
Description
An account of the resource
Mitochondria-derived oxygen-free radical(s) are important mediators of oxidative cellular injury. It is widely hypothesized that excess NO enhances O(2)(center dot-) generated by mitochondria under certain pathological conditions. In the mitochondrial electron transport chain, succinate-cytochrome c reductase (SCR) catalyzes the electron transfer reaction from succinate to cytochrome c. To gain the insights into the molecular mechanism of how NO overproduction may mediate the oxygen-free radical generation by SCR, we employed isolated SCR, cardiac myoblast H9c2, and endothelial cells to study the interaction of NO with SCR in vitro and ex vivo. Under the conditions of enzyme turnover in the presence of NO donor (DEANO), SCR gained pro-oxidant function for generating hydroxyl radical as detected by EPR spin trapping using DEPMPO. The EPR signal associated with DEPMPO/(center dot)OH adduct was nearly completely abolished in the presence of catalase or an iron chelator and partially inhibited by SOD, suggesting the involvement of the iron-H(2)O(2)-dependent Fenton reaction or O(2)(center dot-)-dependent Haber-Weiss mechanism. Direct EPR measurement of SCR at 77 K indicated the formation of a nonheme iron-NO complex, implying that electron leakage to molecular oxygen was enhanced at the FAD cofactor, and that excess NO predisposed SCR to produce (center dot)OH. In H9c2 cells, SCR-dependent oxygen-free radical generation was stimulated by NO released from DEANO or produced by the cells following exposure to hypoxia/reoxygenation. With shear exposure that led to overproduction of NO by the endothelium, SCR-mediated oxygen-free radical production was also detected in cultured vascular endothelial cells. (C) 2011 Elsevier B.V. All rights reserved.
Identifier
An unambiguous reference to the resource within a given context
<a href="http://doi.org/10.1016/j.bbabio.2011.03.001" target="_blank" rel="noreferrer noopener">10.1016/j.bbabio.2011.03.001</a>
Format
The file format, physical medium, or dimensions of the resource
Journal Article or Conference Abstract Publication
2011
Alevriadou B R
Biochemistry & Molecular Biology
Biochimica Et Biophysica Acta-Bioenergetics
Biophysics
Chen C L
Chen J F
Chen Y R
complex-ii
Electron transport chain
electron-transport
endothelial-cells
EPR
Hydroxyl radical
Journal Article or Conference Abstract Publication
Mitochondria
nitric-oxide synthase
NO
Oxygen
oxygen-free radicals
postischemic heart
reactive
Reperfusion Injury
SCR
smooth-muscle-cells
spin trapping
superoxide generation
Zweier J L
-
Text
A resource consisting primarily of words for reading. Examples include books, letters, dissertations, poems, newspapers, articles, archives of mailing lists. Note that facsimiles or images of texts are still of the genre Text.
URL Address
<a href="http://doi.org/10.1074/jbc.M109.056846" target="_blank" rel="noreferrer noopener">http://doi.org/10.1074/jbc.M109.056846</a>
Rights
Article information provided for research and reference use only. All rights are retained by the journal listed under publisher and/or the creator(s).
Pages
3168-3180
Issue
5
Volume
285
Search for Full-text
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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
A point or period of time associated with an event in the lifecycle of the resource
2010
2010-01
Subject
The topic of the resource
oxidative stress; Biochemistry & Molecular Biology; nitric-oxide; proteins; site; generation; s-nitrosylation; postischemic heart; radical formation; bovine heart-mitochondria; nadh-ubiquinone oxidoreductase
Creator
An entity primarily responsible for making the resource
Chen J F; Chen C L; Rawale S; Chen C A; Zweier J L; Kaumaya P T P; Chen Y R
Description
An account of the resource
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
An unambiguous reference to the resource within a given context
<a href="http://doi.org/10.1074/jbc.M109.056846" target="_blank" rel="noreferrer noopener">10.1074/jbc.M109.056846</a>
Format
The file format, physical medium, or dimensions of the resource
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