Multiple glutathione disulfide removal pathways mediate cytosolic redox homeostasis.
Identifieur interne : 000734 ( Main/Exploration ); précédent : 000733; suivant : 000735Multiple glutathione disulfide removal pathways mediate cytosolic redox homeostasis.
Auteurs : Bruce Morgan [Allemagne] ; Daria Ezeri A ; Theresa N E. Amoako ; Jan Riemer ; Matthias Seedorf ; Tobias P. DickSource :
- Nature chemical biology [ 1552-4469 ] ; 2013.
Descripteurs français
- KwdFr :
- Cytosol (métabolisme), Disulfure de glutathion (composition chimique), Facteurs temps (MeSH), Glutarédoxines (métabolisme), Glutathion (métabolisme), Glutathione transferase (métabolisme), Homéostasie (MeSH), Humains (MeSH), Modèles biologiques (MeSH), Modèles chimiques (MeSH), Oxydoréduction (MeSH), Protéines de Saccharomyces cerevisiae (métabolisme), Thiorédoxines (métabolisme), Transporteurs ABC (métabolisme), Vacuoles (métabolisme).
- MESH :
- composition chimique : Disulfure de glutathion.
- métabolisme : Cytosol, Glutarédoxines, Glutathion, Glutathione transferase, Protéines de Saccharomyces cerevisiae, Thiorédoxines, Transporteurs ABC, Vacuoles.
- Facteurs temps, Homéostasie, Humains, Modèles biologiques, Modèles chimiques, Oxydoréduction.
English descriptors
- KwdEn :
- ATP-Binding Cassette Transporters (metabolism), Cytosol (metabolism), Glutaredoxins (metabolism), Glutathione (metabolism), Glutathione Disulfide (chemistry), Glutathione Transferase (metabolism), Homeostasis (MeSH), Humans (MeSH), Models, Biological (MeSH), Models, Chemical (MeSH), Oxidation-Reduction (MeSH), Saccharomyces cerevisiae Proteins (metabolism), Thioredoxins (metabolism), Time Factors (MeSH), Vacuoles (metabolism).
- MESH :
- chemical , chemistry : Glutathione Disulfide.
- chemical , metabolism : ATP-Binding Cassette Transporters, Glutaredoxins, Glutathione, Glutathione Transferase, Saccharomyces cerevisiae Proteins, Thioredoxins.
- metabolism : Cytosol, Vacuoles.
- Homeostasis, Humans, Models, Biological, Models, Chemical, Oxidation-Reduction, Time Factors.
Abstract
Glutathione is central to cellular redox chemistry. The majority of glutathione redox research has been based on the chemical analysis of whole-cell extracts, which unavoidably destroy subcellular compartment-specific information. Compartment-specific real-time measurements based on genetically encoded fluorescent probes now suggest that the cytosolic glutathione redox potential is about 100 mV more reducing than previously thought. Using these probes in yeast, we show that even during severe oxidative stress, the cytosolic glutathione disulfide (GSSG) concentration is much more tightly regulated than expected and provides a mechanistic explanation for the discrepancy with conventional measurements. GSSG that is not immediately reduced in the cytosol is rapidly transported into the vacuole by the ABC-C transporter Ycf1. The amount of whole-cell GSSG is entirely dependent on Ycf1 and uninformative about the cytosolic glutathione pool. Applying these insights, we identify Trx2 and Grx2 as efficient backup systems to glutathione reductase for cytosolic GSSG reduction.
DOI: 10.1038/nchembio.1142
PubMed: 23242256
Affiliations:
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Amoako</name></author><author><name sortKey="Riemer, Jan" sort="Riemer, Jan" uniqKey="Riemer J" first="Jan" last="Riemer">Jan Riemer</name></author><author><name sortKey="Seedorf, Matthias" sort="Seedorf, Matthias" uniqKey="Seedorf M" first="Matthias" last="Seedorf">Matthias Seedorf</name></author><author><name sortKey="Dick, Tobias P" sort="Dick, Tobias P" uniqKey="Dick T" first="Tobias P" last="Dick">Tobias P. Dick</name></author></analytic><series><title level="j">Nature chemical biology</title><idno type="eISSN">1552-4469</idno><imprint><date when="2013" type="published">2013</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>ATP-Binding Cassette Transporters (metabolism)</term><term>Cytosol (metabolism)</term><term>Glutaredoxins (metabolism)</term><term>Glutathione (metabolism)</term><term>Glutathione Disulfide (chemistry)</term><term>Glutathione Transferase (metabolism)</term><term>Homeostasis (MeSH)</term><term>Humans (MeSH)</term><term>Models, Biological (MeSH)</term><term>Models, Chemical (MeSH)</term><term>Oxidation-Reduction (MeSH)</term><term>Saccharomyces cerevisiae Proteins (metabolism)</term><term>Thioredoxins (metabolism)</term><term>Time Factors (MeSH)</term><term>Vacuoles (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Cytosol (métabolisme)</term><term>Disulfure de glutathion (composition chimique)</term><term>Facteurs temps (MeSH)</term><term>Glutarédoxines (métabolisme)</term><term>Glutathion (métabolisme)</term><term>Glutathione transferase (métabolisme)</term><term>Homéostasie (MeSH)</term><term>Humains (MeSH)</term><term>Modèles biologiques (MeSH)</term><term>Modèles chimiques (MeSH)</term><term>Oxydoréduction (MeSH)</term><term>Protéines de Saccharomyces cerevisiae (métabolisme)</term><term>Thiorédoxines (métabolisme)</term><term>Transporteurs ABC (métabolisme)</term><term>Vacuoles (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Glutathione Disulfide</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>ATP-Binding Cassette Transporters</term><term>Glutaredoxins</term><term>Glutathione</term><term>Glutathione Transferase</term><term>Saccharomyces cerevisiae Proteins</term><term>Thioredoxins</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Disulfure de glutathion</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Cytosol</term><term>Vacuoles</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cytosol</term><term>Glutarédoxines</term><term>Glutathion</term><term>Glutathione transferase</term><term>Protéines de Saccharomyces cerevisiae</term><term>Thiorédoxines</term><term>Transporteurs ABC</term><term>Vacuoles</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Homeostasis</term><term>Humans</term><term>Models, Biological</term><term>Models, Chemical</term><term>Oxidation-Reduction</term><term>Time Factors</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Facteurs temps</term><term>Homéostasie</term><term>Humains</term><term>Modèles biologiques</term><term>Modèles chimiques</term><term>Oxydoréduction</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Glutathione is central to cellular redox chemistry. The majority of glutathione redox research has been based on the chemical analysis of whole-cell extracts, which unavoidably destroy subcellular compartment-specific information. Compartment-specific real-time measurements based on genetically encoded fluorescent probes now suggest that the cytosolic glutathione redox potential is about 100 mV more reducing than previously thought. Using these probes in yeast, we show that even during severe oxidative stress, the cytosolic glutathione disulfide (GSSG) concentration is much more tightly regulated than expected and provides a mechanistic explanation for the discrepancy with conventional measurements. GSSG that is not immediately reduced in the cytosol is rapidly transported into the vacuole by the ABC-C transporter Ycf1. The amount of whole-cell GSSG is entirely dependent on Ycf1 and uninformative about the cytosolic glutathione pool. Applying these insights, we identify Trx2 and Grx2 as efficient backup systems to glutathione reductase for cytosolic GSSG reduction.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">23242256</PMID><DateCompleted><Year>2013</Year><Month>03</Month><Day>19</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1552-4469</ISSN><JournalIssue CitedMedium="Internet"><Volume>9</Volume><Issue>2</Issue><PubDate><Year>2013</Year><Month>Feb</Month></PubDate></JournalIssue><Title>Nature chemical biology</Title><ISOAbbreviation>Nat Chem Biol</ISOAbbreviation></Journal><ArticleTitle>Multiple glutathione disulfide removal pathways mediate cytosolic redox homeostasis.</ArticleTitle><Pagination><MedlinePgn>119-25</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1038/nchembio.1142</ELocationID><Abstract><AbstractText>Glutathione is central to cellular redox chemistry. The majority of glutathione redox research has been based on the chemical analysis of whole-cell extracts, which unavoidably destroy subcellular compartment-specific information. Compartment-specific real-time measurements based on genetically encoded fluorescent probes now suggest that the cytosolic glutathione redox potential is about 100 mV more reducing than previously thought. Using these probes in yeast, we show that even during severe oxidative stress, the cytosolic glutathione disulfide (GSSG) concentration is much more tightly regulated than expected and provides a mechanistic explanation for the discrepancy with conventional measurements. GSSG that is not immediately reduced in the cytosol is rapidly transported into the vacuole by the ABC-C transporter Ycf1. The amount of whole-cell GSSG is entirely dependent on Ycf1 and uninformative about the cytosolic glutathione pool. Applying these insights, we identify Trx2 and Grx2 as efficient backup systems to glutathione reductase for cytosolic GSSG reduction.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Morgan</LastName><ForeName>Bruce</ForeName><Initials>B</Initials><AffiliationInfo><Affiliation>Division of Redox Regulation, German Cancer Research Center, DKFZ-ZMBH Alliance, Heidelberg, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ezeriņa</LastName><ForeName>Daria</ForeName><Initials>D</Initials></Author><Author ValidYN="Y"><LastName>Amoako</LastName><ForeName>Theresa N E</ForeName><Initials>TN</Initials></Author><Author ValidYN="Y"><LastName>Riemer</LastName><ForeName>Jan</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Seedorf</LastName><ForeName>Matthias</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Dick</LastName><ForeName>Tobias P</ForeName><Initials>TP</Initials></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>2012</Year><Month>12</Month><Day>16</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Nat Chem Biol</MedlineTA><NlmUniqueID>101231976</NlmUniqueID><ISSNLinking>1552-4450</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D018528">ATP-Binding Cassette Transporters</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C527885">Grx2 protein, S 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Amoako</name><name sortKey="Dick, Tobias P" sort="Dick, Tobias P" uniqKey="Dick T" first="Tobias P" last="Dick">Tobias P. Dick</name><name sortKey="Ezeri A, Daria" sort="Ezeri A, Daria" uniqKey="Ezeri A D" first="Daria" last="Ezeri A">Daria Ezeri A</name><name sortKey="Riemer, Jan" sort="Riemer, Jan" uniqKey="Riemer J" first="Jan" last="Riemer">Jan Riemer</name><name sortKey="Seedorf, Matthias" sort="Seedorf, Matthias" uniqKey="Seedorf M" first="Matthias" last="Seedorf">Matthias Seedorf</name></noCountry><country name="Allemagne"><region name="Bade-Wurtemberg"><name sortKey="Morgan, Bruce" sort="Morgan, Bruce" uniqKey="Morgan B" first="Bruce" last="Morgan">Bruce Morgan</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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|wiki= Bois
|area= GlutaredoxinV1
|flux= Main
|étape= Exploration
|type= RBID
|clé= pubmed:23242256
|texte= Multiple glutathione disulfide removal pathways mediate cytosolic redox homeostasis.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:23242256" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \
| NlmPubMed2Wicri -a GlutaredoxinV1
| This area was generated with Dilib version V0.6.37. |  |