Dehydroascorbic acid S-Thiolation of peptides and proteins: Role of homocysteine and glutathione.
Identifieur interne : 000180 ( Main/Exploration ); précédent : 000179; suivant : 000181Dehydroascorbic acid S-Thiolation of peptides and proteins: Role of homocysteine and glutathione.
Auteurs : Grace Ahuié Kouakou [Canada] ; Hugo Gagnon [Canada] ; Vincent Lacasse [Canada] ; J Richard Wagner [Canada] ; Stephen Naylor [États-Unis] ; Klaus Klarskov [Canada]Source :
- Free radical biology & medicine [ 1873-4596 ] ; 2019.
Descripteurs français
- KwdFr :
- Acide déhydroascorbique (composition chimique), Antioxydants (composition chimique), Cystéine (composition chimique), Dimérisation (MeSH), Disulfures (composition chimique), Domaine catalytique (MeSH), Glutarédoxines (composition chimique), Glutathion (composition chimique), Homocystéine (composition chimique), Humains (MeSH), Hémoglobines (composition chimique), Oxydoréduction (MeSH), Peptides (composition chimique), Stress oxydatif (MeSH), Thiols (composition chimique).
- MESH :
- composition chimique : Acide déhydroascorbique, Antioxydants, Cystéine, Disulfures, Glutarédoxines, Glutathion, Homocystéine, Hémoglobines, Peptides, Thiols.
- Dimérisation, Domaine catalytique, Humains, Oxydoréduction, Stress oxydatif.
English descriptors
- KwdEn :
- Antioxidants (chemistry), Catalytic Domain (MeSH), Cysteine (chemistry), Dehydroascorbic Acid (chemistry), Dimerization (MeSH), Disulfides (chemistry), Glutaredoxins (chemistry), Glutathione (chemistry), Hemoglobins (chemistry), Homocysteine (chemistry), Humans (MeSH), Oxidation-Reduction (MeSH), Oxidative Stress (MeSH), Peptides (chemistry), Sulfhydryl Compounds (chemistry).
- MESH :
- chemical , chemistry : Antioxidants, Cysteine, Dehydroascorbic Acid, Disulfides, Glutaredoxins, Glutathione, Hemoglobins, Homocysteine, Peptides, Sulfhydryl Compounds.
- Catalytic Domain, Dimerization, Humans, Oxidation-Reduction, Oxidative Stress.
Abstract
Ascorbic acid (vitamin C) plays a significant role in the prevention of oxidative stress. In this process, ascorbate is oxidized to dehydroascorbate (DHA). We have investigated the impact of DHA on peptide/protein intramolecular disulfide formation as well as S-glutathionylation and S-homocysteinylation. S-glutathionylation of peptides/proteins is a reversible, potential regulatory mechanism in oxidative stress. Although the exact role of protein S-homocysteinylation is unknown, it has been proposed to be of importance in pathobiological processes such as onset of cardiovascular disease. Using an in vitro model system, we demonstrate that DHA causes disulfide bond formation within the active site of recombinant human glutaredoxin (Grx-1). DHA also facilities the formation of S-glutathionylation and S-homocysteinylation of a model peptide (AcFHACAAK) as well as Grx-1. We discuss the possible mechanisms of peptide/protein S-thiolation, which can occur either via thiol exchange or a thiohemiketal intermediate. A thiohemiketal DHA-peptide adduct was detected by mass spectrometry and its location on the peptide/protein cysteinyl thiol group was unambiguously confirmed by tandem mass spectrometry. This demonstrates that peptide/protein S-thiolation mediated by DHA is not limited to thiol exchange reactions but also takes place directly via the formation of a thiohemiketal peptide intermediate. Finally, we investigated a potential reducing role of glutathione (GSH) in the presence of S-homocysteinylated peptide/protein adducts. S-homocysteinylated AcFHACAAK, human hemoglobin α-chain and Grx-1 were incubated with GSH. Both peptide and proteins were reduced, and homocysteine replaced with GS-adducts by thiol exchange, as a function of time.
DOI: 10.1016/j.freeradbiomed.2019.06.022
PubMed: 31228548
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Electronic address: klaus.klarskov@usherbrooke.ca.</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</wicri:regionArea><wicri:noRegion>Université de Sherbrooke</wicri:noRegion></affiliation></author></analytic><series><title level="j">Free radical biology & medicine</title><idno type="eISSN">1873-4596</idno><imprint><date when="2019" type="published">2019</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Antioxidants (chemistry)</term><term>Catalytic Domain (MeSH)</term><term>Cysteine (chemistry)</term><term>Dehydroascorbic Acid (chemistry)</term><term>Dimerization (MeSH)</term><term>Disulfides (chemistry)</term><term>Glutaredoxins (chemistry)</term><term>Glutathione (chemistry)</term><term>Hemoglobins (chemistry)</term><term>Homocysteine (chemistry)</term><term>Humans (MeSH)</term><term>Oxidation-Reduction (MeSH)</term><term>Oxidative Stress (MeSH)</term><term>Peptides (chemistry)</term><term>Sulfhydryl Compounds (chemistry)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Acide déhydroascorbique (composition chimique)</term><term>Antioxydants (composition chimique)</term><term>Cystéine (composition chimique)</term><term>Dimérisation (MeSH)</term><term>Disulfures (composition chimique)</term><term>Domaine catalytique (MeSH)</term><term>Glutarédoxines (composition chimique)</term><term>Glutathion (composition chimique)</term><term>Homocystéine (composition chimique)</term><term>Humains (MeSH)</term><term>Hémoglobines (composition chimique)</term><term>Oxydoréduction (MeSH)</term><term>Peptides (composition chimique)</term><term>Stress oxydatif (MeSH)</term><term>Thiols (composition chimique)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Antioxidants</term><term>Cysteine</term><term>Dehydroascorbic Acid</term><term>Disulfides</term><term>Glutaredoxins</term><term>Glutathione</term><term>Hemoglobins</term><term>Homocysteine</term><term>Peptides</term><term>Sulfhydryl Compounds</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Acide déhydroascorbique</term><term>Antioxydants</term><term>Cystéine</term><term>Disulfures</term><term>Glutarédoxines</term><term>Glutathion</term><term>Homocystéine</term><term>Hémoglobines</term><term>Peptides</term><term>Thiols</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Catalytic Domain</term><term>Dimerization</term><term>Humans</term><term>Oxidation-Reduction</term><term>Oxidative Stress</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Dimérisation</term><term>Domaine catalytique</term><term>Humains</term><term>Oxydoréduction</term><term>Stress oxydatif</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Ascorbic acid (vitamin C) plays a significant role in the prevention of oxidative stress. In this process, ascorbate is oxidized to dehydroascorbate (DHA). We have investigated the impact of DHA on peptide/protein intramolecular disulfide formation as well as S-glutathionylation and S-homocysteinylation. S-glutathionylation of peptides/proteins is a reversible, potential regulatory mechanism in oxidative stress. Although the exact role of protein S-homocysteinylation is unknown, it has been proposed to be of importance in pathobiological processes such as onset of cardiovascular disease. Using an in vitro model system, we demonstrate that DHA causes disulfide bond formation within the active site of recombinant human glutaredoxin (Grx-1). DHA also facilities the formation of S-glutathionylation and S-homocysteinylation of a model peptide (AcFHACAAK) as well as Grx-1. We discuss the possible mechanisms of peptide/protein S-thiolation, which can occur either via thiol exchange or a thiohemiketal intermediate. A thiohemiketal DHA-peptide adduct was detected by mass spectrometry and its location on the peptide/protein cysteinyl thiol group was unambiguously confirmed by tandem mass spectrometry. This demonstrates that peptide/protein S-thiolation mediated by DHA is not limited to thiol exchange reactions but also takes place directly via the formation of a thiohemiketal peptide intermediate. Finally, we investigated a potential reducing role of glutathione (GSH) in the presence of S-homocysteinylated peptide/protein adducts. S-homocysteinylated AcFHACAAK, human hemoglobin α-chain and Grx-1 were incubated with GSH. Both peptide and proteins were reduced, and homocysteine replaced with GS-adducts by thiol exchange, as a function of time.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">31228548</PMID><DateCompleted><Year>2020</Year><Month>07</Month><Day>13</Day></DateCompleted><DateRevised><Year>2020</Year><Month>07</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1873-4596</ISSN><JournalIssue CitedMedium="Internet"><Volume>141</Volume><PubDate><Year>2019</Year><Month>09</Month></PubDate></JournalIssue><Title>Free radical biology & medicine</Title><ISOAbbreviation>Free Radic Biol Med</ISOAbbreviation></Journal><ArticleTitle>Dehydroascorbic acid S-Thiolation of peptides and proteins: Role of homocysteine and glutathione.</ArticleTitle><Pagination><MedlinePgn>233-243</MedlinePgn></Pagination><ELocationID EIdType="pii" ValidYN="Y">S0891-5849(19)30576-3</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.freeradbiomed.2019.06.022</ELocationID><Abstract><AbstractText>Ascorbic acid (vitamin C) plays a significant role in the prevention of oxidative stress. In this process, ascorbate is oxidized to dehydroascorbate (DHA). We have investigated the impact of DHA on peptide/protein intramolecular disulfide formation as well as S-glutathionylation and S-homocysteinylation. S-glutathionylation of peptides/proteins is a reversible, potential regulatory mechanism in oxidative stress. Although the exact role of protein S-homocysteinylation is unknown, it has been proposed to be of importance in pathobiological processes such as onset of cardiovascular disease. Using an in vitro model system, we demonstrate that DHA causes disulfide bond formation within the active site of recombinant human glutaredoxin (Grx-1). DHA also facilities the formation of S-glutathionylation and S-homocysteinylation of a model peptide (AcFHACAAK) as well as Grx-1. We discuss the possible mechanisms of peptide/protein S-thiolation, which can occur either via thiol exchange or a thiohemiketal intermediate. A thiohemiketal DHA-peptide adduct was detected by mass spectrometry and its location on the peptide/protein cysteinyl thiol group was unambiguously confirmed by tandem mass spectrometry. This demonstrates that peptide/protein S-thiolation mediated by DHA is not limited to thiol exchange reactions but also takes place directly via the formation of a thiohemiketal peptide intermediate. Finally, we investigated a potential reducing role of glutathione (GSH) in the presence of S-homocysteinylated peptide/protein adducts. S-homocysteinylated AcFHACAAK, human hemoglobin α-chain and Grx-1 were incubated with GSH. Both peptide and proteins were reduced, and homocysteine replaced with GS-adducts by thiol exchange, as a function of time.</AbstractText><CopyrightInformation>Copyright © 2019 Elsevier Inc. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Ahuié Kouakou</LastName><ForeName>Grace</ForeName><Initials>G</Initials><AffiliationInfo><Affiliation>Département de Pharmacologie et Physiologie, Faculté de Médecine et des Sciences de la Santé, Université de Sherbrooke, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Gagnon</LastName><ForeName>Hugo</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>PhenoSwitch Bioscience, 975 Rue Léon-Trépanier, Sherbrooke, QC J1G 5J6, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lacasse</LastName><ForeName>Vincent</ForeName><Initials>V</Initials><AffiliationInfo><Affiliation>Département de Pharmacologie et Physiologie, Faculté de Médecine et des Sciences de la Santé, Université de Sherbrooke, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wagner</LastName><ForeName>J Richard</ForeName><Initials>JR</Initials><AffiliationInfo><Affiliation>Département de Médecine Nucléaire et radiobiologie, Faculté de Médecine et des Sciences de la Santé, Université de Sherbrooke, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Naylor</LastName><ForeName>Stephen</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>ReNeuroGen LLC, 2160 San Fernando Drive, Elm Grove, WI, 53122, USA.</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, Canada. Electronic address: klaus.klarskov@usherbrooke.ca.</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><ArticleDate DateType="Electronic"><Year>2019</Year><Month>06</Month><Day>19</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Free Radic Biol Med</MedlineTA><NlmUniqueID>8709159</NlmUniqueID><ISSNLinking>0891-5849</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000975">Antioxidants</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004220">Disulfides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D006454">Hemoglobins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010455">Peptides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D013438">Sulfhydryl Compounds</NameOfSubstance></Chemical><Chemical><RegistryNumber>0LVT1QZ0BA</RegistryNumber><NameOfSubstance UI="D006710">Homocysteine</NameOfSubstance></Chemical><Chemical><RegistryNumber>GAN16C9B8O</RegistryNumber><NameOfSubstance UI="D005978">Glutathione</NameOfSubstance></Chemical><Chemical><RegistryNumber>K848JZ4886</RegistryNumber><NameOfSubstance UI="D003545">Cysteine</NameOfSubstance></Chemical><Chemical><RegistryNumber>Y2Z3ZTP9UM</RegistryNumber><NameOfSubstance UI="D003683">Dehydroascorbic Acid</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000975" MajorTopicYN="N">Antioxidants</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020134" MajorTopicYN="N">Catalytic Domain</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003545" MajorTopicYN="N">Cysteine</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003683" MajorTopicYN="N">Dehydroascorbic Acid</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D019281" MajorTopicYN="N">Dimerization</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004220" MajorTopicYN="N">Disulfides</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005978" MajorTopicYN="N">Glutathione</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006454" MajorTopicYN="N">Hemoglobins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006710" MajorTopicYN="N">Homocysteine</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018384" MajorTopicYN="N">Oxidative Stress</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010455" MajorTopicYN="N">Peptides</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013438" MajorTopicYN="N">Sulfhydryl Compounds</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">Dehydroascorbate</Keyword><Keyword MajorTopicYN="Y">Glutaredoxin-1</Keyword><Keyword MajorTopicYN="Y">Glutathione</Keyword><Keyword MajorTopicYN="Y">Homocysteine</Keyword><Keyword MajorTopicYN="Y">Mass spectrometry</Keyword><Keyword MajorTopicYN="Y">S-thiolation</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2019</Year><Month>04</Month><Day>05</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2019</Year><Month>06</Month><Day>13</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2019</Year><Month>06</Month><Day>17</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2019</Year><Month>6</Month><Day>23</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2020</Year><Month>7</Month><Day>14</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2019</Year><Month>6</Month><Day>23</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">31228548</ArticleId><ArticleId IdType="pii">S0891-5849(19)30576-3</ArticleId><ArticleId IdType="doi">10.1016/j.freeradbiomed.2019.06.022</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Canada</li><li>États-Unis</li></country></list><tree><country name="Canada"><noRegion><name sortKey="Ahuie Kouakou, Grace" sort="Ahuie Kouakou, Grace" uniqKey="Ahuie Kouakou G" first="Grace" last="Ahuié Kouakou">Grace Ahuié Kouakou</name></noRegion><name sortKey="Gagnon, Hugo" sort="Gagnon, Hugo" uniqKey="Gagnon H" first="Hugo" last="Gagnon">Hugo Gagnon</name><name sortKey="Klarskov, Klaus" sort="Klarskov, Klaus" uniqKey="Klarskov K" first="Klaus" last="Klarskov">Klaus Klarskov</name><name sortKey="Lacasse, Vincent" sort="Lacasse, Vincent" uniqKey="Lacasse V" first="Vincent" last="Lacasse">Vincent Lacasse</name><name sortKey="Wagner, J Richard" sort="Wagner, J Richard" uniqKey="Wagner J" first="J Richard" last="Wagner">J Richard Wagner</name></country><country name="États-Unis"><noRegion><name sortKey="Naylor, Stephen" sort="Naylor, Stephen" uniqKey="Naylor S" first="Stephen" last="Naylor">Stephen Naylor</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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