Characterization of mammalian glutaredoxin isoforms as S-denitrosylases.
Identifieur interne : 000188 ( Main/Exploration ); précédent : 000187; suivant : 000189Characterization of mammalian glutaredoxin isoforms as S-denitrosylases.
Auteurs : Xiaoyuan Ren [Suède] ; Rajib Sengupta [Suède, Inde] ; Jun Lu [Suède, République populaire de Chine] ; Jon O. Lundberg [Suède] ; Arne Holmgren [Suède]Source :
- FEBS letters [ 1873-3468 ] ; 2019.
Descripteurs français
- KwdFr :
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Caspase 3, Cathepsin B, Glutaredoxins, Nitric Oxide, Oxygenases, Protein Isoforms.
- HEK293 Cells, Homeostasis, Humans, Signal Transduction.
Abstract
Glutaredoxins (Grx) are involved in many reactions including defense against oxidative stress. However, the role of the Grx system under nitrosative stress has barely been investigated. In this study, we found that human Grxs denitrosylated both low and high molecular weight S-nitrosothiols. Some S-nitrosylated proteins, stable in the presence of a physiological concentration of glutathione (GSH), were denitrosylated by Grxs. Caspase 3 and cathepsin B were identified as substrates of Grx1-catalysed denitrosylation. In addition, mono-thiol Grxs, such as Grx5, exhibited denitrosylase activity coupled with GSH via a monothiol mechanism. Our study demonstrates the ability of Grxs to act as S-denitrosylases and pinpoint a new mechanism for denitrosylation.
DOI: 10.1002/1873-3468.13454
PubMed: 31125428
Affiliations:
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Lundberg</name><affiliation wicri:level="3"><nlm:affiliation>Department of Physiology and Pharmacology, Karolinska Institutet, Stockholm, Sweden.</nlm:affiliation><country xml:lang="fr">Suède</country><wicri:regionArea>Department of Physiology and Pharmacology, Karolinska Institutet, Stockholm</wicri:regionArea><placeName><settlement type="city">Stockholm</settlement><region nuts="2">Svealand</region></placeName></affiliation></author><author><name sortKey="Holmgren, Arne" sort="Holmgren, Arne" uniqKey="Holmgren A" first="Arne" last="Holmgren">Arne Holmgren</name><affiliation wicri:level="3"><nlm:affiliation>Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden.</nlm:affiliation><country xml:lang="fr">Suède</country><wicri:regionArea>Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm</wicri:regionArea><placeName><settlement type="city">Stockholm</settlement><region nuts="2">Svealand</region></placeName></affiliation></author></analytic><series><title level="j">FEBS letters</title><idno type="eISSN">1873-3468</idno><imprint><date when="2019" type="published">2019</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Caspase 3 (metabolism)</term><term>Cathepsin B (metabolism)</term><term>Glutaredoxins (metabolism)</term><term>HEK293 Cells (MeSH)</term><term>Homeostasis (MeSH)</term><term>Humans (MeSH)</term><term>Nitric Oxide (metabolism)</term><term>Oxygenases (metabolism)</term><term>Protein Isoforms (metabolism)</term><term>Signal Transduction (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Caspase-3 (métabolisme)</term><term>Cathepsine B (métabolisme)</term><term>Cellules HEK293 (MeSH)</term><term>Glutarédoxines (métabolisme)</term><term>Homéostasie (MeSH)</term><term>Humains (MeSH)</term><term>Isoformes de protéines (métabolisme)</term><term>Monoxyde d'azote (métabolisme)</term><term>Oxygénases (métabolisme)</term><term>Transduction du signal (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Caspase 3</term><term>Cathepsin B</term><term>Glutaredoxins</term><term>Nitric Oxide</term><term>Oxygenases</term><term>Protein Isoforms</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Caspase-3</term><term>Cathepsine B</term><term>Glutarédoxines</term><term>Isoformes de protéines</term><term>Monoxyde d'azote</term><term>Oxygénases</term></keywords><keywords scheme="MESH" xml:lang="en"><term>HEK293 Cells</term><term>Homeostasis</term><term>Humans</term><term>Signal Transduction</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cellules HEK293</term><term>Homéostasie</term><term>Humains</term><term>Transduction du signal</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Glutaredoxins (Grx) are involved in many reactions including defense against oxidative stress. However, the role of the Grx system under nitrosative stress has barely been investigated. In this study, we found that human Grxs denitrosylated both low and high molecular weight S-nitrosothiols. Some S-nitrosylated proteins, stable in the presence of a physiological concentration of glutathione (GSH), were denitrosylated by Grxs. Caspase 3 and cathepsin B were identified as substrates of Grx1-catalysed denitrosylation. In addition, mono-thiol Grxs, such as Grx5, exhibited denitrosylase activity coupled with GSH via a monothiol mechanism. Our study demonstrates the ability of Grxs to act as S-denitrosylases and pinpoint a new mechanism for denitrosylation.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">31125428</PMID><DateCompleted><Year>2020</Year><Month>06</Month><Day>15</Day></DateCompleted><DateRevised><Year>2020</Year><Month>06</Month><Day>15</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1873-3468</ISSN><JournalIssue CitedMedium="Internet"><Volume>593</Volume><Issue>14</Issue><PubDate><Year>2019</Year><Month>07</Month></PubDate></JournalIssue><Title>FEBS letters</Title><ISOAbbreviation>FEBS Lett</ISOAbbreviation></Journal><ArticleTitle>Characterization of mammalian glutaredoxin isoforms as S-denitrosylases.</ArticleTitle><Pagination><MedlinePgn>1799-1806</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1002/1873-3468.13454</ELocationID><Abstract><AbstractText>Glutaredoxins (Grx) are involved in many reactions including defense against oxidative stress. However, the role of the Grx system under nitrosative stress has barely been investigated. In this study, we found that human Grxs denitrosylated both low and high molecular weight S-nitrosothiols. Some S-nitrosylated proteins, stable in the presence of a physiological concentration of glutathione (GSH), were denitrosylated by Grxs. Caspase 3 and cathepsin B were identified as substrates of Grx1-catalysed denitrosylation. In addition, mono-thiol Grxs, such as Grx5, exhibited denitrosylase activity coupled with GSH via a monothiol mechanism. Our study demonstrates the ability of Grxs to act as S-denitrosylases and pinpoint a new mechanism for denitrosylation.</AbstractText><CopyrightInformation>© 2019 Federation of European Biochemical Societies.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Ren</LastName><ForeName>Xiaoyuan</ForeName><Initials>X</Initials><Identifier Source="ORCID">0000-0001-5644-9008</Identifier><AffiliationInfo><Affiliation>Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Sengupta</LastName><ForeName>Rajib</ForeName><Initials>R</Initials><AffiliationInfo><Affiliation>Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Amity Institute of Biotechnology, Amity University, Kolkata, India.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lu</LastName><ForeName>Jun</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>School of Pharmaceutical Sciences, Southwest University, Chongqing, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lundberg</LastName><ForeName>Jon O</ForeName><Initials>JO</Initials><AffiliationInfo><Affiliation>Department of Physiology and Pharmacology, Karolinska Institutet, Stockholm, Sweden.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Holmgren</LastName><ForeName>Arne</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><Agency>Swedish Cancer Society</Agency><Country>International</Country></Grant><Grant><Agency>Swedish Research Council</Agency><Country>International</Country></Grant><Grant><Agency>Karolinska Institutet</Agency><Country>International</Country></Grant></GrantList><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>02</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>FEBS Lett</MedlineTA><NlmUniqueID>0155157</NlmUniqueID><ISSNLinking>0014-5793</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D020033">Protein Isoforms</NameOfSubstance></Chemical><Chemical><RegistryNumber>31C4KY9ESH</RegistryNumber><NameOfSubstance UI="D009569">Nitric Oxide</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.13.-</RegistryNumber><NameOfSubstance UI="D010105">Oxygenases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.22.-</RegistryNumber><NameOfSubstance UI="D053148">Caspase 3</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.22.1</RegistryNumber><NameOfSubstance UI="D002401">Cathepsin B</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D053148" MajorTopicYN="N">Caspase 3</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002401" MajorTopicYN="N">Cathepsin B</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="D057809" MajorTopicYN="N">HEK293 Cells</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006706" MajorTopicYN="N">Homeostasis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009569" MajorTopicYN="N">Nitric Oxide</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010105" MajorTopicYN="N">Oxygenases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020033" MajorTopicYN="N">Protein Isoforms</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015398" MajorTopicYN="N">Signal Transduction</DescriptorName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">S-denitrosylation</Keyword><Keyword MajorTopicYN="Y">apoptosis</Keyword><Keyword MajorTopicYN="Y">glutaredoxins</Keyword><Keyword MajorTopicYN="Y">glutathione</Keyword><Keyword MajorTopicYN="Y">thioredoxin</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2019</Year><Month>04</Month><Day>04</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2019</Year><Month>05</Month><Day>21</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2019</Year><Month>05</Month><Day>21</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2019</Year><Month>5</Month><Day>28</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2020</Year><Month>6</Month><Day>17</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2019</Year><Month>5</Month><Day>25</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">31125428</ArticleId><ArticleId IdType="doi">10.1002/1873-3468.13454</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Inde</li><li>République populaire de Chine</li><li>Suède</li></country><region><li>Svealand</li></region><settlement><li>Stockholm</li></settlement></list><tree><country name="Suède"><region name="Svealand"><name sortKey="Ren, Xiaoyuan" sort="Ren, Xiaoyuan" uniqKey="Ren X" first="Xiaoyuan" last="Ren">Xiaoyuan Ren</name></region><name sortKey="Holmgren, Arne" sort="Holmgren, Arne" uniqKey="Holmgren A" first="Arne" last="Holmgren">Arne Holmgren</name><name sortKey="Lu, Jun" sort="Lu, Jun" uniqKey="Lu J" first="Jun" last="Lu">Jun Lu</name><name sortKey="Lundberg, Jon O" sort="Lundberg, Jon O" uniqKey="Lundberg J" first="Jon O" last="Lundberg">Jon O. Lundberg</name><name sortKey="Sengupta, Rajib" sort="Sengupta, Rajib" uniqKey="Sengupta R" first="Rajib" last="Sengupta">Rajib Sengupta</name></country><country name="Inde"><noRegion><name sortKey="Sengupta, Rajib" sort="Sengupta, Rajib" uniqKey="Sengupta R" first="Rajib" last="Sengupta">Rajib Sengupta</name></noRegion></country><country name="République populaire de Chine"><noRegion><name sortKey="Lu, Jun" sort="Lu, Jun" uniqKey="Lu J" first="Jun" last="Lu">Jun Lu</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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