Postischemic deactivation of cardiac aldose reductase: role of glutathione S-transferase P and glutaredoxin in regeneration of reduced thiols from sulfenic acids.
Identifieur interne : 000A08 ( Main/Exploration ); précédent : 000A07; suivant : 000A09Postischemic deactivation of cardiac aldose reductase: role of glutathione S-transferase P and glutaredoxin in regeneration of reduced thiols from sulfenic acids.
Auteurs : Karin Wetzelberger [États-Unis] ; Shahid P. Baba ; Mahesh Thirunavukkarasu ; Ye-Shih Ho ; Nilanjana Maulik ; Oleg A. Barski ; Daniel J. Conklin ; Aruni BhatnagarSource :
- The Journal of biological chemistry [ 1083-351X ] ; 2010.
Descripteurs français
- KwdFr :
- Acides sulféniques (métabolisme), Aldose reductase (métabolisme), Animaux (MeSH), Cystéine (métabolisme), Glutarédoxines (métabolisme), Glutathione transferase (métabolisme), Ischémie myocardique (enzymologie), Ischémie myocardique (métabolisme), Mâle (MeSH), Oxydoréduction (MeSH), Souris (MeSH), Souris de lignée C57BL (MeSH), Thiols (métabolisme).
- MESH :
- enzymologie : Ischémie myocardique.
- métabolisme : Acides sulféniques, Aldose reductase, Cystéine, Glutarédoxines, Glutathione transferase, Ischémie myocardique, Thiols.
- Animaux, Mâle, Oxydoréduction, Souris, Souris de lignée C57BL.
English descriptors
- KwdEn :
- Aldehyde Reductase (metabolism), Animals (MeSH), Cysteine (metabolism), Glutaredoxins (metabolism), Glutathione Transferase (metabolism), Male (MeSH), Mice (MeSH), Mice, Inbred C57BL (MeSH), Myocardial Ischemia (enzymology), Myocardial Ischemia (metabolism), Oxidation-Reduction (MeSH), Sulfenic Acids (metabolism), Sulfhydryl Compounds (metabolism).
- MESH :
- chemical , metabolism : Aldehyde Reductase, Cysteine, Glutaredoxins, Glutathione Transferase, Sulfenic Acids, Sulfhydryl Compounds.
- enzymology : Myocardial Ischemia.
- metabolism : Myocardial Ischemia.
- Animals, Male, Mice, Mice, Inbred C57BL, Oxidation-Reduction.
Abstract
Aldose reductase (AR) is a multifunctional enzyme that catalyzes the reduction of glucose and lipid peroxidation-derived aldehydes. During myocardial ischemia, the activity of AR is increased due to the oxidation of its cysteine residues to sulfenic acids. It is not known, however, whether the activated, sulfenic form of the protein (AR-SOH) is converted back to its reduced, unactivated state (AR-SH). We report here that in perfused mouse hearts activation of AR during 15 min of global ischemia is completely reversed by 30 min of reperfusion. During reperfusion, AR-SOH was converted to a mixed disulfide (AR-SSG). Deactivation of AR and the appearance of AR-SSG during reperfusion were delayed in hearts of mice lacking glutathione S-transferase P (GSTP). In vitro, GSTP accelerated glutathiolation and inactivation of AR-SOH. Reduction of AR-SSG to AR-SH was facilitated by glutaredoxin (GRX). Ischemic activation of AR was increased in GRX-null hearts but was attenuated in the hearts of cardiospecific GRX transgenic mice. Incubation of AR-SSG with GRX led to the regeneration of the reduced form of the enzyme. In ischemic cardiospecific AR transgenic hearts, AR was co-immunoprecipitated with GSTP, whereas in reperfused hearts, the association of AR with GRX was increased. These findings suggest that upon reperfusion of the ischemic heart AR-SOH is converted to AR-SSG via GSTP-assisted glutathiolation. AR-SSG is then reduced by GRX to AR-SH. Sequential catalysis by GSTP and GRX may be a general redox switching mechanism that regulates the reduction of protein sulfenic acids to cysteines.
DOI: 10.1074/jbc.M110.146423
PubMed: 20538586
PubMed Central: PMC2924019
Affiliations:
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Baba</name></author><author><name sortKey="Thirunavukkarasu, Mahesh" sort="Thirunavukkarasu, Mahesh" uniqKey="Thirunavukkarasu M" first="Mahesh" last="Thirunavukkarasu">Mahesh Thirunavukkarasu</name></author><author><name sortKey="Ho, Ye Shih" sort="Ho, Ye Shih" uniqKey="Ho Y" first="Ye-Shih" last="Ho">Ye-Shih Ho</name></author><author><name sortKey="Maulik, Nilanjana" sort="Maulik, Nilanjana" uniqKey="Maulik N" first="Nilanjana" last="Maulik">Nilanjana Maulik</name></author><author><name sortKey="Barski, Oleg A" sort="Barski, Oleg A" uniqKey="Barski O" first="Oleg A" last="Barski">Oleg A. Barski</name></author><author><name sortKey="Conklin, Daniel J" sort="Conklin, Daniel J" uniqKey="Conklin D" first="Daniel J" last="Conklin">Daniel J. Conklin</name></author><author><name sortKey="Bhatnagar, Aruni" sort="Bhatnagar, Aruni" uniqKey="Bhatnagar A" first="Aruni" last="Bhatnagar">Aruni Bhatnagar</name></author></analytic><series><title level="j">The Journal of biological chemistry</title><idno type="eISSN">1083-351X</idno><imprint><date when="2010" type="published">2010</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Aldehyde Reductase (metabolism)</term><term>Animals (MeSH)</term><term>Cysteine (metabolism)</term><term>Glutaredoxins (metabolism)</term><term>Glutathione Transferase (metabolism)</term><term>Male (MeSH)</term><term>Mice (MeSH)</term><term>Mice, Inbred C57BL (MeSH)</term><term>Myocardial Ischemia (enzymology)</term><term>Myocardial Ischemia (metabolism)</term><term>Oxidation-Reduction (MeSH)</term><term>Sulfenic Acids (metabolism)</term><term>Sulfhydryl Compounds (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Acides sulféniques (métabolisme)</term><term>Aldose reductase (métabolisme)</term><term>Animaux (MeSH)</term><term>Cystéine (métabolisme)</term><term>Glutarédoxines (métabolisme)</term><term>Glutathione transferase (métabolisme)</term><term>Ischémie myocardique (enzymologie)</term><term>Ischémie myocardique (métabolisme)</term><term>Mâle (MeSH)</term><term>Oxydoréduction (MeSH)</term><term>Souris (MeSH)</term><term>Souris de lignée C57BL (MeSH)</term><term>Thiols (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Aldehyde Reductase</term><term>Cysteine</term><term>Glutaredoxins</term><term>Glutathione Transferase</term><term>Sulfenic Acids</term><term>Sulfhydryl Compounds</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Ischémie myocardique</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Myocardial Ischemia</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Myocardial Ischemia</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Acides sulféniques</term><term>Aldose reductase</term><term>Cystéine</term><term>Glutarédoxines</term><term>Glutathione transferase</term><term>Ischémie myocardique</term><term>Thiols</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Male</term><term>Mice</term><term>Mice, Inbred C57BL</term><term>Oxidation-Reduction</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Mâle</term><term>Oxydoréduction</term><term>Souris</term><term>Souris de lignée C57BL</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Aldose reductase (AR) is a multifunctional enzyme that catalyzes the reduction of glucose and lipid peroxidation-derived aldehydes. During myocardial ischemia, the activity of AR is increased due to the oxidation of its cysteine residues to sulfenic acids. It is not known, however, whether the activated, sulfenic form of the protein (AR-SOH) is converted back to its reduced, unactivated state (AR-SH). We report here that in perfused mouse hearts activation of AR during 15 min of global ischemia is completely reversed by 30 min of reperfusion. During reperfusion, AR-SOH was converted to a mixed disulfide (AR-SSG). Deactivation of AR and the appearance of AR-SSG during reperfusion were delayed in hearts of mice lacking glutathione S-transferase P (GSTP). In vitro, GSTP accelerated glutathiolation and inactivation of AR-SOH. Reduction of AR-SSG to AR-SH was facilitated by glutaredoxin (GRX). Ischemic activation of AR was increased in GRX-null hearts but was attenuated in the hearts of cardiospecific GRX transgenic mice. Incubation of AR-SSG with GRX led to the regeneration of the reduced form of the enzyme. In ischemic cardiospecific AR transgenic hearts, AR was co-immunoprecipitated with GSTP, whereas in reperfused hearts, the association of AR with GRX was increased. These findings suggest that upon reperfusion of the ischemic heart AR-SOH is converted to AR-SSG via GSTP-assisted glutathiolation. AR-SSG is then reduced by GRX to AR-SH. Sequential catalysis by GSTP and GRX may be a general redox switching mechanism that regulates the reduction of protein sulfenic acids to cysteines.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">20538586</PMID><DateCompleted><Year>2010</Year><Month>09</Month><Day>30</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1083-351X</ISSN><JournalIssue CitedMedium="Internet"><Volume>285</Volume><Issue>34</Issue><PubDate><Year>2010</Year><Month>Aug</Month><Day>20</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J Biol Chem</ISOAbbreviation></Journal><ArticleTitle>Postischemic deactivation of cardiac aldose reductase: role of glutathione S-transferase P and glutaredoxin in regeneration of reduced thiols from sulfenic acids.</ArticleTitle><Pagination><MedlinePgn>26135-48</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1074/jbc.M110.146423</ELocationID><Abstract><AbstractText>Aldose reductase (AR) is a multifunctional enzyme that catalyzes the reduction of glucose and lipid peroxidation-derived aldehydes. During myocardial ischemia, the activity of AR is increased due to the oxidation of its cysteine residues to sulfenic acids. It is not known, however, whether the activated, sulfenic form of the protein (AR-SOH) is converted back to its reduced, unactivated state (AR-SH). We report here that in perfused mouse hearts activation of AR during 15 min of global ischemia is completely reversed by 30 min of reperfusion. During reperfusion, AR-SOH was converted to a mixed disulfide (AR-SSG). Deactivation of AR and the appearance of AR-SSG during reperfusion were delayed in hearts of mice lacking glutathione S-transferase P (GSTP). In vitro, GSTP accelerated glutathiolation and inactivation of AR-SOH. Reduction of AR-SSG to AR-SH was facilitated by glutaredoxin (GRX). Ischemic activation of AR was increased in GRX-null hearts but was attenuated in the hearts of cardiospecific GRX transgenic mice. Incubation of AR-SSG with GRX led to the regeneration of the reduced form of the enzyme. In ischemic cardiospecific AR transgenic hearts, AR was co-immunoprecipitated with GSTP, whereas in reperfused hearts, the association of AR with GRX was increased. These findings suggest that upon reperfusion of the ischemic heart AR-SOH is converted to AR-SSG via GSTP-assisted glutathiolation. AR-SSG is then reduced by GRX to AR-SH. Sequential catalysis by GSTP and GRX may be a general redox switching mechanism that regulates the reduction of protein sulfenic acids to cysteines.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Wetzelberger</LastName><ForeName>Karin</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Diabetes and Obesity Center, University of Louisville, Louisville, Kentucky 40202, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Baba</LastName><ForeName>Shahid P</ForeName><Initials>SP</Initials></Author><Author ValidYN="Y"><LastName>Thirunavukkarasu</LastName><ForeName>Mahesh</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Ho</LastName><ForeName>Ye-Shih</ForeName><Initials>YS</Initials></Author><Author ValidYN="Y"><LastName>Maulik</LastName><ForeName>Nilanjana</ForeName><Initials>N</Initials></Author><Author ValidYN="Y"><LastName>Barski</LastName><ForeName>Oleg A</ForeName><Initials>OA</Initials></Author><Author ValidYN="Y"><LastName>Conklin</LastName><ForeName>Daniel J</ForeName><Initials>DJ</Initials></Author><Author ValidYN="Y"><LastName>Bhatnagar</LastName><ForeName>Aruni</ForeName><Initials>A</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>P20 RR024489</GrantID><Acronym>RR</Acronym><Agency>NCRR NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>HL78825</GrantID><Acronym>HL</Acronym><Agency>NHLBI NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01 HL059378</GrantID><Acronym>HL</Acronym><Agency>NHLBI NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01 HL089380</GrantID><Acronym>HL</Acronym><Agency>NHLBI NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>HL89380</GrantID><Acronym>HL</Acronym><Agency>NHLBI NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>HL55477</GrantID><Acronym>HL</Acronym><Agency>NHLBI NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>P01 HL078825</GrantID><Acronym>HL</Acronym><Agency>NHLBI NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>HL59378</GrantID><Acronym>HL</Acronym><Agency>NHLBI NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>RR024489</GrantID><Acronym>RR</Acronym><Agency>NCRR NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>HL893802S1</GrantID><Acronym>HL</Acronym><Agency>NHLBI NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01 HL055477</GrantID><Acronym>HL</Acronym><Agency>NHLBI NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D052061">Research Support, N.I.H., Extramural</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2010</Year><Month>06</Month><Day>10</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Biol Chem</MedlineTA><NlmUniqueID>2985121R</NlmUniqueID><ISSNLinking>0021-9258</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D013434">Sulfenic Acids</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D013438">Sulfhydryl Compounds</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.1.1.21</RegistryNumber><NameOfSubstance UI="D000449">Aldehyde Reductase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.5.1.18</RegistryNumber><NameOfSubstance UI="D005982">Glutathione Transferase</NameOfSubstance></Chemical><Chemical><RegistryNumber>K848JZ4886</RegistryNumber><NameOfSubstance UI="D003545">Cysteine</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000449" MajorTopicYN="N">Aldehyde Reductase</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003545" MajorTopicYN="N">Cysteine</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005982" MajorTopicYN="N">Glutathione Transferase</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008297" MajorTopicYN="N">Male</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D051379" MajorTopicYN="N">Mice</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008810" MajorTopicYN="N">Mice, Inbred C57BL</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017202" MajorTopicYN="N">Myocardial Ischemia</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013434" MajorTopicYN="N">Sulfenic Acids</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013438" MajorTopicYN="N">Sulfhydryl Compounds</DescriptorName><QualifierName 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Baba</name><name sortKey="Barski, Oleg A" sort="Barski, Oleg A" uniqKey="Barski O" first="Oleg A" last="Barski">Oleg A. Barski</name><name sortKey="Bhatnagar, Aruni" sort="Bhatnagar, Aruni" uniqKey="Bhatnagar A" first="Aruni" last="Bhatnagar">Aruni Bhatnagar</name><name sortKey="Conklin, Daniel J" sort="Conklin, Daniel J" uniqKey="Conklin D" first="Daniel J" last="Conklin">Daniel J. Conklin</name><name sortKey="Ho, Ye Shih" sort="Ho, Ye Shih" uniqKey="Ho Y" first="Ye-Shih" last="Ho">Ye-Shih Ho</name><name sortKey="Maulik, Nilanjana" sort="Maulik, Nilanjana" uniqKey="Maulik N" first="Nilanjana" last="Maulik">Nilanjana Maulik</name><name sortKey="Thirunavukkarasu, Mahesh" sort="Thirunavukkarasu, Mahesh" uniqKey="Thirunavukkarasu M" first="Mahesh" last="Thirunavukkarasu">Mahesh Thirunavukkarasu</name></noCountry><country name="États-Unis"><noRegion><name sortKey="Wetzelberger, Karin" sort="Wetzelberger, Karin" uniqKey="Wetzelberger K" first="Karin" last="Wetzelberger">Karin Wetzelberger</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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