Emerging mechanisms of glutathione-dependent chemistry in biology and disease.
Identifieur interne : 000769 ( Main/Exploration ); précédent : 000768; suivant : 000770Emerging mechanisms of glutathione-dependent chemistry in biology and disease.
Auteurs : Yvonne M W. Janssen-Heininger [États-Unis] ; James D. Nolin ; Sidra M. Hoffman ; Jos L. Van Der Velden ; Jane E. Tully ; Karolyn G. Lahue ; Sarah T. Abdalla ; David G. Chapman ; Niki L. Reynaert ; Albert Van Der Vliet ; Vikas AnathySource :
- Journal of cellular biochemistry [ 1097-4644 ] ; 2013.
Descripteurs français
- KwdFr :
- MESH :
- métabolisme : Biotine, Glutarédoxines, Glutathion, Thiols.
- Animaux, Humains, Oxydoréduction.
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Biotin, Glutaredoxins, Glutathione, Sulfhydryl Compounds.
- Animals, Humans, Oxidation-Reduction.
Abstract
Glutathione has traditionally been considered as an antioxidant that protects cells against oxidative stress. Hence, the loss of reduced glutathione and formation of glutathione disulfide is considered a classical parameter of oxidative stress that is increased in diseases. Recent studies have emerged that demonstrate that glutathione plays a more direct role in biological and pathophysiological processes through covalent modification to reactive cysteines within proteins, a process known as S-glutathionylation. The formation of an S-glutathionylated moiety within the protein can lead to structural and functional modifications. Activation, inactivation, loss of function, and gain of function have all been attributed to S-glutathionylation. In pathophysiological settings, S-glutathionylation is tightly regulated. This perspective offers a concise overview of the emerging field of protein thiol redox modifications. We will also cover newly developed methodology to detect S-glutathionylation in situ, which will enable further discovery into the role of S-glutathionylation in biology and disease.
DOI: 10.1002/jcb.24551
PubMed: 23554102
PubMed Central: PMC3857728
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Van Der Velden</name></author><author><name sortKey="Tully, Jane E" sort="Tully, Jane E" uniqKey="Tully J" first="Jane E" last="Tully">Jane E. Tully</name></author><author><name sortKey="Lahue, Karolyn G" sort="Lahue, Karolyn G" uniqKey="Lahue K" first="Karolyn G" last="Lahue">Karolyn G. Lahue</name></author><author><name sortKey="Abdalla, Sarah T" sort="Abdalla, Sarah T" uniqKey="Abdalla S" first="Sarah T" last="Abdalla">Sarah T. Abdalla</name></author><author><name sortKey="Chapman, David G" sort="Chapman, David G" uniqKey="Chapman D" first="David G" last="Chapman">David G. Chapman</name></author><author><name sortKey="Reynaert, Niki L" sort="Reynaert, Niki L" uniqKey="Reynaert N" first="Niki L" last="Reynaert">Niki L. Reynaert</name></author><author><name sortKey="Van Der Vliet, Albert" sort="Van Der Vliet, Albert" uniqKey="Van Der Vliet A" first="Albert" last="Van Der Vliet">Albert Van Der Vliet</name></author><author><name sortKey="Anathy, Vikas" sort="Anathy, Vikas" uniqKey="Anathy V" first="Vikas" last="Anathy">Vikas Anathy</name></author></analytic><series><title level="j">Journal of cellular biochemistry</title><idno type="eISSN">1097-4644</idno><imprint><date when="2013" type="published">2013</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals (MeSH)</term><term>Biotin (metabolism)</term><term>Glutaredoxins (metabolism)</term><term>Glutathione (metabolism)</term><term>Humans (MeSH)</term><term>Oxidation-Reduction (MeSH)</term><term>Sulfhydryl Compounds (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term><term>Biotine (métabolisme)</term><term>Glutarédoxines (métabolisme)</term><term>Glutathion (métabolisme)</term><term>Humains (MeSH)</term><term>Oxydoréduction (MeSH)</term><term>Thiols (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Biotin</term><term>Glutaredoxins</term><term>Glutathione</term><term>Sulfhydryl Compounds</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Biotine</term><term>Glutarédoxines</term><term>Glutathion</term><term>Thiols</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Humans</term><term>Oxidation-Reduction</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Humains</term><term>Oxydoréduction</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Glutathione has traditionally been considered as an antioxidant that protects cells against oxidative stress. Hence, the loss of reduced glutathione and formation of glutathione disulfide is considered a classical parameter of oxidative stress that is increased in diseases. Recent studies have emerged that demonstrate that glutathione plays a more direct role in biological and pathophysiological processes through covalent modification to reactive cysteines within proteins, a process known as S-glutathionylation. The formation of an S-glutathionylated moiety within the protein can lead to structural and functional modifications. Activation, inactivation, loss of function, and gain of function have all been attributed to S-glutathionylation. In pathophysiological settings, S-glutathionylation is tightly regulated. This perspective offers a concise overview of the emerging field of protein thiol redox modifications. We will also cover newly developed methodology to detect S-glutathionylation in situ, which will enable further discovery into the role of S-glutathionylation in biology and disease.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">23554102</PMID><DateCompleted><Year>2013</Year><Month>10</Month><Day>29</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1097-4644</ISSN><JournalIssue CitedMedium="Internet"><Volume>114</Volume><Issue>9</Issue><PubDate><Year>2013</Year><Month>Sep</Month></PubDate></JournalIssue><Title>Journal of cellular biochemistry</Title><ISOAbbreviation>J Cell Biochem</ISOAbbreviation></Journal><ArticleTitle>Emerging mechanisms of glutathione-dependent chemistry in biology and disease.</ArticleTitle><Pagination><MedlinePgn>1962-8</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1002/jcb.24551</ELocationID><Abstract><AbstractText>Glutathione has traditionally been considered as an antioxidant that protects cells against oxidative stress. Hence, the loss of reduced glutathione and formation of glutathione disulfide is considered a classical parameter of oxidative stress that is increased in diseases. Recent studies have emerged that demonstrate that glutathione plays a more direct role in biological and pathophysiological processes through covalent modification to reactive cysteines within proteins, a process known as S-glutathionylation. The formation of an S-glutathionylated moiety within the protein can lead to structural and functional modifications. Activation, inactivation, loss of function, and gain of function have all been attributed to S-glutathionylation. In pathophysiological settings, S-glutathionylation is tightly regulated. This perspective offers a concise overview of the emerging field of protein thiol redox modifications. We will also cover newly developed methodology to detect S-glutathionylation in situ, which will enable further discovery into the role of S-glutathionylation in biology and disease.</AbstractText><CopyrightInformation>Copyright © 2013 Wiley Periodicals, Inc.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Janssen-Heininger</LastName><ForeName>Yvonne M W</ForeName><Initials>YM</Initials><AffiliationInfo><Affiliation>Department of Pathology, University of Vermont College of Medicine, Burlington, Vermont 05405, USA. yvonne.janssen@uvm.edu</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Nolin</LastName><ForeName>James D</ForeName><Initials>JD</Initials></Author><Author ValidYN="Y"><LastName>Hoffman</LastName><ForeName>Sidra M</ForeName><Initials>SM</Initials></Author><Author ValidYN="Y"><LastName>van der Velden</LastName><ForeName>Jos L</ForeName><Initials>JL</Initials></Author><Author ValidYN="Y"><LastName>Tully</LastName><ForeName>Jane E</ForeName><Initials>JE</Initials></Author><Author ValidYN="Y"><LastName>Lahue</LastName><ForeName>Karolyn G</ForeName><Initials>KG</Initials></Author><Author ValidYN="Y"><LastName>Abdalla</LastName><ForeName>Sarah T</ForeName><Initials>ST</Initials></Author><Author ValidYN="Y"><LastName>Chapman</LastName><ForeName>David G</ForeName><Initials>DG</Initials></Author><Author ValidYN="Y"><LastName>Reynaert</LastName><ForeName>Niki L</ForeName><Initials>NL</Initials></Author><Author ValidYN="Y"><LastName>van der Vliet</LastName><ForeName>Albert</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Anathy</LastName><ForeName>Vikas</ForeName><Initials>V</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>R01 HL060014</GrantID><Acronym>HL</Acronym><Agency>NHLBI NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01 HL085464</GrantID><Acronym>HL</Acronym><Agency>NHLBI NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01 HL85646</GrantID><Acronym>HL</Acronym><Agency>NHLBI NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01 HL079331</GrantID><Acronym>HL</Acronym><Agency>NHLBI NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01 HL085646</GrantID><Acronym>HL</Acronym><Agency>NHLBI NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01 ES021476</GrantID><Acronym>ES</Acronym><Agency>NIEHS 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><PublicationType 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MajorTopicYN="N">Biotin</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005978" MajorTopicYN="N">Glutathione</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013438" MajorTopicYN="N">Sulfhydryl Compounds</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">BIOTIN SWITCH</Keyword><Keyword 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Abdalla</name><name sortKey="Anathy, Vikas" sort="Anathy, Vikas" uniqKey="Anathy V" first="Vikas" last="Anathy">Vikas Anathy</name><name sortKey="Chapman, David G" sort="Chapman, David G" uniqKey="Chapman D" first="David G" last="Chapman">David G. Chapman</name><name sortKey="Hoffman, Sidra M" sort="Hoffman, Sidra M" uniqKey="Hoffman S" first="Sidra M" last="Hoffman">Sidra M. Hoffman</name><name sortKey="Lahue, Karolyn G" sort="Lahue, Karolyn G" uniqKey="Lahue K" first="Karolyn G" last="Lahue">Karolyn G. Lahue</name><name sortKey="Nolin, James D" sort="Nolin, James D" uniqKey="Nolin J" first="James D" last="Nolin">James D. Nolin</name><name sortKey="Reynaert, Niki L" sort="Reynaert, Niki L" uniqKey="Reynaert N" first="Niki L" last="Reynaert">Niki L. Reynaert</name><name sortKey="Tully, Jane E" sort="Tully, Jane E" uniqKey="Tully J" first="Jane E" last="Tully">Jane E. Tully</name><name sortKey="Van Der Velden, Jos L" sort="Van Der Velden, Jos L" uniqKey="Van Der Velden J" first="Jos L" last="Van Der Velden">Jos L. Van Der Velden</name><name sortKey="Van Der Vliet, Albert" sort="Van Der Vliet, Albert" uniqKey="Van Der Vliet A" first="Albert" last="Van Der Vliet">Albert Van Der Vliet</name></noCountry><country name="États-Unis"><noRegion><name sortKey="Janssen Heininger, Yvonne M W" sort="Janssen Heininger, Yvonne M W" uniqKey="Janssen Heininger Y" first="Yvonne M W" last="Janssen-Heininger">Yvonne M W. Janssen-Heininger</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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