Endoplasmic reticulum: reduced and oxidized glutathione revisited.
Identifieur interne : 000768 ( Main/Exploration ); précédent : 000767; suivant : 000769Endoplasmic reticulum: reduced and oxidized glutathione revisited.
Auteurs : Julia Birk [Suisse] ; Mariangela Meyer ; Isabel Aller ; Henning G. Hansen ; Alex Odermatt ; Tobias P. Dick ; Andreas J. Meyer ; Christian Appenzeller-HerzogSource :
- Journal of cell science [ 1477-9137 ] ; 2013.
Descripteurs français
- KwdFr :
- Cellules HeLa (MeSH), Disulfure de glutathion (métabolisme), Glutathion (métabolisme), Humains (MeSH), Oxydoréduction (MeSH), Protéines à fluorescence verte (génétique), Protéines à fluorescence verte (métabolisme), Réponse aux protéines mal repliées (génétique), Réponse aux protéines mal repliées (physiologie), Réticulum endoplasmique (métabolisme).
- MESH :
- génétique : Protéines à fluorescence verte, Réponse aux protéines mal repliées.
- métabolisme : Disulfure de glutathion, Glutathion, Protéines à fluorescence verte, Réticulum endoplasmique.
- physiologie : Réponse aux protéines mal repliées.
- Cellules HeLa, Humains, Oxydoréduction.
English descriptors
- KwdEn :
- Endoplasmic Reticulum (metabolism), Glutathione (metabolism), Glutathione Disulfide (metabolism), Green Fluorescent Proteins (genetics), Green Fluorescent Proteins (metabolism), HeLa Cells (MeSH), Humans (MeSH), Oxidation-Reduction (MeSH), Unfolded Protein Response (genetics), Unfolded Protein Response (physiology).
- MESH :
- chemical , genetics : Green Fluorescent Proteins.
- chemical , metabolism : Glutathione, Glutathione Disulfide, Green Fluorescent Proteins.
- genetics : Unfolded Protein Response.
- metabolism : Endoplasmic Reticulum.
- physiology : Unfolded Protein Response.
- HeLa Cells, Humans, Oxidation-Reduction.
Abstract
The reducing power of glutathione, expressed by its reduction potential EGSH, is an accepted measure for redox conditions in a given cell compartment. In the endoplasmic reticulum (ER), EGSH is less reducing than elsewhere in the cell. However, attempts to determine EGSH(ER) have been inconsistent and based on ineligible assumptions. Using a codon-optimized and evidently glutathione-specific glutaredoxin-coupled redox-sensitive green fluorescent protein (roGFP) variant, we determined EGSH(ER) in HeLa cells as -208±4 mV (at pH 7.0). At variance with existing models, this is not oxidizing enough to maintain the known redox state of protein disulfide isomerase family enzymes. Live-cell microscopy confirmed ER hypo-oxidation upon inhibition of ER Ca(2+) import. Conversely, stressing the ER with a glycosylation inhibitor did not lead to more reducing conditions, as reported for yeast. These results, which for the first time establish the oxidative capacity of glutathione in the ER, illustrate a context-dependent interplay between ER stress and EGSH(ER). The reported development of ER-localized EGSH sensors will enable more targeted in vivo redox analyses in ER-related disorders.
DOI: 10.1242/jcs.117218
PubMed: 23424194
Affiliations:
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Hansen</name></author><author><name sortKey="Odermatt, Alex" sort="Odermatt, Alex" uniqKey="Odermatt A" first="Alex" last="Odermatt">Alex Odermatt</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><author><name sortKey="Meyer, Andreas J" sort="Meyer, Andreas J" uniqKey="Meyer A" first="Andreas J" last="Meyer">Andreas J. Meyer</name></author><author><name sortKey="Appenzeller Herzog, Christian" sort="Appenzeller Herzog, Christian" uniqKey="Appenzeller Herzog C" first="Christian" last="Appenzeller-Herzog">Christian Appenzeller-Herzog</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2013">2013</date><idno type="RBID">pubmed:23424194</idno><idno type="pmid">23424194</idno><idno type="doi">10.1242/jcs.117218</idno><idno type="wicri:Area/Main/Corpus">000759</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000759</idno><idno type="wicri:Area/Main/Curation">000759</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000759</idno><idno type="wicri:Area/Main/Exploration">000759</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Endoplasmic reticulum: reduced and oxidized glutathione revisited.</title><author><name sortKey="Birk, Julia" sort="Birk, Julia" uniqKey="Birk J" first="Julia" last="Birk">Julia Birk</name><affiliation wicri:level="1"><nlm:affiliation>Division of Molecular and Systems Toxicology, Department of Pharmaceutical Sciences, University of Basel, 4056 Basel, Switzerland.</nlm:affiliation><country xml:lang="fr">Suisse</country><wicri:regionArea>Division of Molecular and Systems Toxicology, Department of Pharmaceutical Sciences, University of Basel, 4056 Basel</wicri:regionArea><wicri:noRegion>4056 Basel</wicri:noRegion></affiliation></author><author><name sortKey="Meyer, Mariangela" sort="Meyer, Mariangela" uniqKey="Meyer M" first="Mariangela" last="Meyer">Mariangela Meyer</name></author><author><name sortKey="Aller, Isabel" sort="Aller, Isabel" uniqKey="Aller I" first="Isabel" last="Aller">Isabel Aller</name></author><author><name sortKey="Hansen, Henning G" sort="Hansen, Henning G" uniqKey="Hansen H" first="Henning G" last="Hansen">Henning G. Hansen</name></author><author><name sortKey="Odermatt, Alex" sort="Odermatt, Alex" uniqKey="Odermatt A" first="Alex" last="Odermatt">Alex Odermatt</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><author><name sortKey="Meyer, Andreas J" sort="Meyer, Andreas J" uniqKey="Meyer A" first="Andreas J" last="Meyer">Andreas J. Meyer</name></author><author><name sortKey="Appenzeller Herzog, Christian" sort="Appenzeller Herzog, Christian" uniqKey="Appenzeller Herzog C" first="Christian" last="Appenzeller-Herzog">Christian Appenzeller-Herzog</name></author></analytic><series><title level="j">Journal of cell science</title><idno type="eISSN">1477-9137</idno><imprint><date when="2013" type="published">2013</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Endoplasmic Reticulum (metabolism)</term><term>Glutathione (metabolism)</term><term>Glutathione Disulfide (metabolism)</term><term>Green Fluorescent Proteins (genetics)</term><term>Green Fluorescent Proteins (metabolism)</term><term>HeLa Cells (MeSH)</term><term>Humans (MeSH)</term><term>Oxidation-Reduction (MeSH)</term><term>Unfolded Protein Response (genetics)</term><term>Unfolded Protein Response (physiology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Cellules HeLa (MeSH)</term><term>Disulfure de glutathion (métabolisme)</term><term>Glutathion (métabolisme)</term><term>Humains (MeSH)</term><term>Oxydoréduction (MeSH)</term><term>Protéines à fluorescence verte (génétique)</term><term>Protéines à fluorescence verte (métabolisme)</term><term>Réponse aux protéines mal repliées (génétique)</term><term>Réponse aux protéines mal repliées (physiologie)</term><term>Réticulum endoplasmique (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Green Fluorescent Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glutathione</term><term>Glutathione Disulfide</term><term>Green Fluorescent Proteins</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Unfolded Protein Response</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Protéines à fluorescence verte</term><term>Réponse aux protéines mal repliées</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Endoplasmic Reticulum</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Disulfure de glutathion</term><term>Glutathion</term><term>Protéines à fluorescence verte</term><term>Réticulum endoplasmique</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Réponse aux protéines mal repliées</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Unfolded Protein Response</term></keywords><keywords scheme="MESH" xml:lang="en"><term>HeLa Cells</term><term>Humans</term><term>Oxidation-Reduction</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cellules HeLa</term><term>Humains</term><term>Oxydoréduction</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The reducing power of glutathione, expressed by its reduction potential EGSH, is an accepted measure for redox conditions in a given cell compartment. In the endoplasmic reticulum (ER), EGSH is less reducing than elsewhere in the cell. However, attempts to determine EGSH(ER) have been inconsistent and based on ineligible assumptions. Using a codon-optimized and evidently glutathione-specific glutaredoxin-coupled redox-sensitive green fluorescent protein (roGFP) variant, we determined EGSH(ER) in HeLa cells as -208±4 mV (at pH 7.0). At variance with existing models, this is not oxidizing enough to maintain the known redox state of protein disulfide isomerase family enzymes. Live-cell microscopy confirmed ER hypo-oxidation upon inhibition of ER Ca(2+) import. Conversely, stressing the ER with a glycosylation inhibitor did not lead to more reducing conditions, as reported for yeast. These results, which for the first time establish the oxidative capacity of glutathione in the ER, illustrate a context-dependent interplay between ER stress and EGSH(ER). The reported development of ER-localized EGSH sensors will enable more targeted in vivo redox analyses in ER-related disorders.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">23424194</PMID><DateCompleted><Year>2013</Year><Month>10</Month><Day>29</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1477-9137</ISSN><JournalIssue CitedMedium="Internet"><Volume>126</Volume><Issue>Pt 7</Issue><PubDate><Year>2013</Year><Month>Apr</Month><Day>01</Day></PubDate></JournalIssue><Title>Journal of cell science</Title><ISOAbbreviation>J Cell Sci</ISOAbbreviation></Journal><ArticleTitle>Endoplasmic reticulum: reduced and oxidized glutathione revisited.</ArticleTitle><Pagination><MedlinePgn>1604-17</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1242/jcs.117218</ELocationID><Abstract><AbstractText>The reducing power of glutathione, expressed by its reduction potential EGSH, is an accepted measure for redox conditions in a given cell compartment. In the endoplasmic reticulum (ER), EGSH is less reducing than elsewhere in the cell. However, attempts to determine EGSH(ER) have been inconsistent and based on ineligible assumptions. Using a codon-optimized and evidently glutathione-specific glutaredoxin-coupled redox-sensitive green fluorescent protein (roGFP) variant, we determined EGSH(ER) in HeLa cells as -208±4 mV (at pH 7.0). At variance with existing models, this is not oxidizing enough to maintain the known redox state of protein disulfide isomerase family enzymes. Live-cell microscopy confirmed ER hypo-oxidation upon inhibition of ER Ca(2+) import. Conversely, stressing the ER with a glycosylation inhibitor did not lead to more reducing conditions, as reported for yeast. These results, which for the first time establish the oxidative capacity of glutathione in the ER, illustrate a context-dependent interplay between ER stress and EGSH(ER). The reported development of ER-localized EGSH sensors will enable more targeted in vivo redox analyses in ER-related disorders.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Birk</LastName><ForeName>Julia</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Division of Molecular and Systems Toxicology, Department of Pharmaceutical Sciences, University of Basel, 4056 Basel, Switzerland.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Meyer</LastName><ForeName>Mariangela</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Aller</LastName><ForeName>Isabel</ForeName><Initials>I</Initials></Author><Author ValidYN="Y"><LastName>Hansen</LastName><ForeName>Henning G</ForeName><Initials>HG</Initials></Author><Author ValidYN="Y"><LastName>Odermatt</LastName><ForeName>Alex</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Dick</LastName><ForeName>Tobias P</ForeName><Initials>TP</Initials></Author><Author ValidYN="Y"><LastName>Meyer</LastName><ForeName>Andreas J</ForeName><Initials>AJ</Initials></Author><Author ValidYN="Y"><LastName>Appenzeller-Herzog</LastName><ForeName>Christian</ForeName><Initials>C</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>2013</Year><Month>02</Month><Day>19</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>J Cell Sci</MedlineTA><NlmUniqueID>0052457</NlmUniqueID><ISSNLinking>0021-9533</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>147336-22-9</RegistryNumber><NameOfSubstance UI="D049452">Green Fluorescent Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>GAN16C9B8O</RegistryNumber><NameOfSubstance UI="D005978">Glutathione</NameOfSubstance></Chemical><Chemical><RegistryNumber>ULW86O013H</RegistryNumber><NameOfSubstance UI="D019803">Glutathione Disulfide</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D004721" MajorTopicYN="N">Endoplasmic Reticulum</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005978" MajorTopicYN="N">Glutathione</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D019803" MajorTopicYN="N">Glutathione Disulfide</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D049452" MajorTopicYN="N">Green Fluorescent Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006367" MajorTopicYN="N">HeLa Cells</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D056811" MajorTopicYN="N">Unfolded Protein Response</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Endoplasmic reticulum</Keyword><Keyword MajorTopicYN="N">Glutathione</Keyword><Keyword MajorTopicYN="N">Green fluorescent protein</Keyword><Keyword MajorTopicYN="N">Reduction potential</Keyword><Keyword MajorTopicYN="N">Unfolded protein response</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2013</Year><Month>2</Month><Day>21</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2013</Year><Month>2</Month><Day>21</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2013</Year><Month>10</Month><Day>30</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">23424194</ArticleId><ArticleId IdType="pii">jcs.117218</ArticleId><ArticleId IdType="doi">10.1242/jcs.117218</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Suisse</li></country></list><tree><noCountry><name sortKey="Aller, Isabel" sort="Aller, Isabel" uniqKey="Aller I" first="Isabel" last="Aller">Isabel Aller</name><name sortKey="Appenzeller Herzog, Christian" sort="Appenzeller Herzog, Christian" uniqKey="Appenzeller Herzog C" first="Christian" last="Appenzeller-Herzog">Christian Appenzeller-Herzog</name><name sortKey="Dick, Tobias P" sort="Dick, Tobias P" uniqKey="Dick T" first="Tobias P" last="Dick">Tobias P. Dick</name><name sortKey="Hansen, Henning G" sort="Hansen, Henning G" uniqKey="Hansen H" first="Henning G" last="Hansen">Henning G. Hansen</name><name sortKey="Meyer, Andreas J" sort="Meyer, Andreas J" uniqKey="Meyer A" first="Andreas J" last="Meyer">Andreas J. Meyer</name><name sortKey="Meyer, Mariangela" sort="Meyer, Mariangela" uniqKey="Meyer M" first="Mariangela" last="Meyer">Mariangela Meyer</name><name sortKey="Odermatt, Alex" sort="Odermatt, Alex" uniqKey="Odermatt A" first="Alex" last="Odermatt">Alex Odermatt</name></noCountry><country name="Suisse"><noRegion><name sortKey="Birk, Julia" sort="Birk, Julia" uniqKey="Birk J" first="Julia" last="Birk">Julia Birk</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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