Characterization of dehydroascorbate-mediated modification of glutaredoxin by mass spectrometry.
Identifieur interne : 000569 ( Main/Exploration ); précédent : 000568; suivant : 000570Characterization of dehydroascorbate-mediated modification of glutaredoxin by mass spectrometry.
Auteurs : Aurore Flandrin [Canada, France] ; Sebastien Allouche [Canada, France] ; Yoann Rolland [Canada, France] ; François-Olivier Mcduff [Canada] ; J. Richard Wagner [Canada] ; Klaus Klarskov [Canada]Source :
- Journal of mass spectrometry : JMS [ 1096-9888 ] ; 2015.
Descripteurs français
- KwdFr :
- Acide déhydroascorbique (composition chimique), Chromatographie en phase liquide (MeSH), Escherichia coli (génétique), Glutarédoxines (composition chimique), Glutarédoxines (génétique), Humains (MeSH), Mesure d'échange de deutérium (MeSH), Protéines recombinantes (composition chimique), Spectrométrie de masse ESI (méthodes).
- MESH :
- composition chimique : Acide déhydroascorbique, Glutarédoxines, Protéines recombinantes.
- génétique : Escherichia coli, Glutarédoxines.
- méthodes : Spectrométrie de masse ESI.
- Chromatographie en phase liquide, Humains, Mesure d'échange de deutérium.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Dehydroascorbic Acid, Glutaredoxins, Recombinant Proteins.
- genetics : Escherichia coli, Glutaredoxins.
- methods : Spectrometry, Mass, Electrospray Ionization.
- Chromatography, Liquid, Deuterium Exchange Measurement, Humans.
Abstract
Ascorbate is as a potent antioxidant in vivo protecting the organism against oxidative stress. In this process, ascorbate is oxidized in two steps to dehydroascorbate (DHA), which if not efficiently reduced back to ascorbate decomposes irreversibly to a complex mixture of products. We demonstrate that a component of this mixture specifically reacts with the thiol group of cysteine residues at physiological pH to give a protein adduct involving the addition of a 5-carbon fragment of DHA (+112 Da). Incubations of glutaredoxin-1 expressed in Escherichia coli and dehydroascorbate revealed abundant adducts of +112, +224 and +336 Da due to the addition of one, two and three conjugation products of DHA, respectively. ESI-MS of carbamidomethylated glutaredoxin-1 before incubation with DHA, deuterium exchange together with tandem mass spectrometry analysis and LC-ESIMS/MS of modified peptides confirmed structure and sites of modification in the protein. Modification of protein thiols by a DHA-derived product can be involved in oxidative stress-mediated cellular toxicity.
DOI: 10.1002/jms.3706
PubMed: 26634969
Affiliations:
Links toward previous steps (curation, corpus...)
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Richard Wagner</name><affiliation wicri:level="1"><nlm:affiliation>Département de Médecine Nucléaire et Radiobiologie, Faculté de Médecine et des Sciences de la Santé, Université de Sherbrooke, Sherbrooke, QC, Canada.</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>Département de Médecine Nucléaire et Radiobiologie, Faculté de Médecine et des Sciences de la Santé, Université de Sherbrooke, Sherbrooke, QC</wicri:regionArea><wicri:noRegion>QC</wicri:noRegion></affiliation></author><author><name sortKey="Klarskov, Klaus" sort="Klarskov, Klaus" uniqKey="Klarskov K" first="Klaus" last="Klarskov">Klaus Klarskov</name><affiliation wicri:level="1"><nlm:affiliation>Département de Pharmacologie et Physiologie, Faculté de Médecine et des Sciences de la Santé, Université de Sherbrooke, Sherbrooke, QC, Canada.</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>Département de Pharmacologie et Physiologie, Faculté de Médecine et des Sciences de la Santé, Université de Sherbrooke, Sherbrooke, QC</wicri:regionArea><wicri:noRegion>QC</wicri:noRegion></affiliation></author></analytic><series><title level="j">Journal of mass spectrometry : JMS</title><idno type="eISSN">1096-9888</idno><imprint><date when="2015" type="published">2015</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Chromatography, Liquid (MeSH)</term><term>Dehydroascorbic Acid (chemistry)</term><term>Deuterium Exchange Measurement (MeSH)</term><term>Escherichia coli (genetics)</term><term>Glutaredoxins (chemistry)</term><term>Glutaredoxins (genetics)</term><term>Humans (MeSH)</term><term>Recombinant Proteins (chemistry)</term><term>Spectrometry, Mass, Electrospray Ionization (methods)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Acide déhydroascorbique (composition chimique)</term><term>Chromatographie en phase liquide (MeSH)</term><term>Escherichia coli (génétique)</term><term>Glutarédoxines (composition chimique)</term><term>Glutarédoxines (génétique)</term><term>Humains (MeSH)</term><term>Mesure d'échange de deutérium (MeSH)</term><term>Protéines recombinantes (composition chimique)</term><term>Spectrométrie de masse ESI (méthodes)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Dehydroascorbic Acid</term><term>Glutaredoxins</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Acide déhydroascorbique</term><term>Glutarédoxines</term><term>Protéines recombinantes</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Escherichia coli</term><term>Glutaredoxins</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Escherichia coli</term><term>Glutarédoxines</term></keywords><keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Spectrometry, Mass, Electrospray Ionization</term></keywords><keywords scheme="MESH" qualifier="méthodes" xml:lang="fr"><term>Spectrométrie de masse ESI</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Chromatography, Liquid</term><term>Deuterium Exchange Measurement</term><term>Humans</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Chromatographie en phase liquide</term><term>Humains</term><term>Mesure d'échange de deutérium</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Ascorbate is as a potent antioxidant in vivo protecting the organism against oxidative stress. In this process, ascorbate is oxidized in two steps to dehydroascorbate (DHA), which if not efficiently reduced back to ascorbate decomposes irreversibly to a complex mixture of products. We demonstrate that a component of this mixture specifically reacts with the thiol group of cysteine residues at physiological pH to give a protein adduct involving the addition of a 5-carbon fragment of DHA (+112 Da). Incubations of glutaredoxin-1 expressed in Escherichia coli and dehydroascorbate revealed abundant adducts of +112, +224 and +336 Da due to the addition of one, two and three conjugation products of DHA, respectively. ESI-MS of carbamidomethylated glutaredoxin-1 before incubation with DHA, deuterium exchange together with tandem mass spectrometry analysis and LC-ESIMS/MS of modified peptides confirmed structure and sites of modification in the protein. Modification of protein thiols by a DHA-derived product can be involved in oxidative stress-mediated cellular toxicity.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">26634969</PMID><DateCompleted><Year>2016</Year><Month>09</Month><Day>21</Day></DateCompleted><DateRevised><Year>2015</Year><Month>12</Month><Day>04</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1096-9888</ISSN><JournalIssue CitedMedium="Internet"><Volume>50</Volume><Issue>12</Issue><PubDate><Year>2015</Year><Month>Dec</Month></PubDate></JournalIssue><Title>Journal of mass spectrometry : JMS</Title><ISOAbbreviation>J Mass Spectrom</ISOAbbreviation></Journal><ArticleTitle>Characterization of dehydroascorbate-mediated modification of glutaredoxin by mass spectrometry.</ArticleTitle><Pagination><MedlinePgn>1358-66</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1002/jms.3706</ELocationID><Abstract><AbstractText>Ascorbate is as a potent antioxidant in vivo protecting the organism against oxidative stress. In this process, ascorbate is oxidized in two steps to dehydroascorbate (DHA), which if not efficiently reduced back to ascorbate decomposes irreversibly to a complex mixture of products. We demonstrate that a component of this mixture specifically reacts with the thiol group of cysteine residues at physiological pH to give a protein adduct involving the addition of a 5-carbon fragment of DHA (+112 Da). Incubations of glutaredoxin-1 expressed in Escherichia coli and dehydroascorbate revealed abundant adducts of +112, +224 and +336 Da due to the addition of one, two and three conjugation products of DHA, respectively. ESI-MS of carbamidomethylated glutaredoxin-1 before incubation with DHA, deuterium exchange together with tandem mass spectrometry analysis and LC-ESIMS/MS of modified peptides confirmed structure and sites of modification in the protein. Modification of protein thiols by a DHA-derived product can be involved in oxidative stress-mediated cellular toxicity.</AbstractText><CopyrightInformation>Copyright © 2015 John Wiley & Sons, Ltd.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Flandrin</LastName><ForeName>Aurore</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Département de Pharmacologie et Physiologie, Faculté de Médecine et des Sciences de la Santé, Université de Sherbrooke, Sherbrooke, QC, Canada.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>École nationale supérieure des ingénieurs en arts chimiques et technologiques, Toulouse, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Allouche</LastName><ForeName>Sebastien</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Département de Pharmacologie et Physiologie, Faculté de Médecine et des Sciences de la Santé, Université de Sherbrooke, Sherbrooke, QC, Canada.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>École nationale supérieure des ingénieurs en arts chimiques et technologiques, Toulouse, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Rolland</LastName><ForeName>Yoann</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>Département de Pharmacologie et Physiologie, Faculté de Médecine et des Sciences de la Santé, Université de Sherbrooke, Sherbrooke, QC, Canada.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>École nationale supérieure des ingénieurs en arts chimiques et technologiques, Toulouse, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>McDuff</LastName><ForeName>François-Olivier</ForeName><Initials>FO</Initials><AffiliationInfo><Affiliation>Département de Pharmacologie et Physiologie, Faculté de Médecine et des Sciences de la Santé, Université de Sherbrooke, Sherbrooke, QC, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Richard Wagner</LastName><ForeName>J</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Département de Médecine Nucléaire et Radiobiologie, Faculté de Médecine et des Sciences de la Santé, Université de Sherbrooke, Sherbrooke, QC, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Klarskov</LastName><ForeName>Klaus</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Département de Pharmacologie et Physiologie, Faculté de Médecine et des Sciences de la Santé, Université de Sherbrooke, Sherbrooke, QC, Canada.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>J Mass Spectrom</MedlineTA><NlmUniqueID>9504818</NlmUniqueID><ISSNLinking>1076-5174</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C516005">GLRX protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>Y2Z3ZTP9UM</RegistryNumber><NameOfSubstance UI="D003683">Dehydroascorbic Acid</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D002853" MajorTopicYN="N">Chromatography, Liquid</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003683" MajorTopicYN="N">Dehydroascorbic Acid</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D041961" MajorTopicYN="N">Deuterium Exchange Measurement</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004926" MajorTopicYN="N">Escherichia coli</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D021241" MajorTopicYN="N">Spectrometry, Mass, Electrospray Ionization</DescriptorName><QualifierName UI="Q000379" MajorTopicYN="Y">methods</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">dehydroascorbate</Keyword><Keyword MajorTopicYN="N">electrospray ionization mass spectrometry</Keyword><Keyword MajorTopicYN="N">glutaredoxin-1</Keyword><Keyword MajorTopicYN="N">liquid chromatography</Keyword><Keyword MajorTopicYN="N">protein S-ascorbylation</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2015</Year><Month>06</Month><Day>23</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2015</Year><Month>08</Month><Day>25</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2015</Year><Month>09</Month><Day>15</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2015</Year><Month>12</Month><Day>5</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate 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Klaus" sort="Klarskov, Klaus" uniqKey="Klarskov K" first="Klaus" last="Klarskov">Klaus Klarskov</name><name sortKey="Mcduff, Francois Olivier" sort="Mcduff, Francois Olivier" uniqKey="Mcduff F" first="François-Olivier" last="Mcduff">François-Olivier Mcduff</name><name sortKey="Richard Wagner, J" sort="Richard Wagner, J" uniqKey="Richard Wagner J" first="J" last="Richard Wagner">J. Richard Wagner</name><name sortKey="Rolland, Yoann" sort="Rolland, Yoann" uniqKey="Rolland Y" first="Yoann" last="Rolland">Yoann Rolland</name></country><country name="France"><region name="Occitanie (région administrative)"><name sortKey="Flandrin, Aurore" sort="Flandrin, Aurore" uniqKey="Flandrin A" first="Aurore" last="Flandrin">Aurore Flandrin</name></region><name sortKey="Allouche, Sebastien" sort="Allouche, Sebastien" uniqKey="Allouche S" first="Sebastien" last="Allouche">Sebastien Allouche</name><name sortKey="Rolland, Yoann" sort="Rolland, Yoann" uniqKey="Rolland Y" first="Yoann" last="Rolland">Yoann Rolland</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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|wiki= Bois
|area= GlutaredoxinV1
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|clé= pubmed:26634969
|texte= Characterization of dehydroascorbate-mediated modification of glutaredoxin by mass spectrometry.
}}
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