Intracellular glutathione pools are heterogeneously concentrated.
Identifieur interne : 000748 ( Main/Exploration ); précédent : 000747; suivant : 000749Intracellular glutathione pools are heterogeneously concentrated.
Auteurs : Davide Montero [Suisse] ; Christine Tachibana ; Jakob Rahr Winther ; Christian Appenzeller-HerzogSource :
- Redox biology [ 2213-2317 ] ; 2013.
Descripteurs français
- KwdFr :
- MESH :
- génétique : Glutarédoxines.
- métabolisme : Cytosol, Glutarédoxines, Glutathion, Réticulum endoplasmique.
- Cellules HeLa, Homéostasie, Humains.
English descriptors
- KwdEn :
- MESH :
- chemical , genetics : Glutaredoxins.
- metabolism : Cytosol, Endoplasmic Reticulum, Glutaredoxins, Glutathione.
- HeLa Cells, Homeostasis, Humans.
Abstract
Glutathione is present in millimolar concentrations in the cell, but its relative distribution among cellular compartments remains elusive. We have chosen the endoplasmic reticulum (ER) as an example organelle to study compartment-specific glutathione levels. Using a glutaredoxin sensor (sCGrx1pER), which rapidly and specifically equilibrates with the reduced glutathione (GSH)-glutathione disulfide (GSSG) redox couple with known equilibrium constant, we showed that the [GSH]:[GSSG] ratio in the ER of intact HeLa cells is less than 7:1. Taking into consideration the previously determined value for [GSH](2):[GSSG] in the ER of 83 mM, this translates into a total glutathione concentration in the ER ([GStot]=[GSH]+2[GSSG]) of greater than 15 mM. Since the integrated, intracellular [GStot] was measured as ~7 mM, we conclude the existence of a [GStot] gradient across the ER membrane. A possible homeostatic mechanism by which cytosol-derived glutathione is trapped in the ER is discussed. We propose a high [GStot] as a distinguishing feature of the ER environment compared to the extracellular space.
DOI: 10.1016/j.redox.2013.10.005
PubMed: 24251119
PubMed Central: PMC3830055
Affiliations:
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Jakob" uniqKey="Rahr Winther J" first="Jakob" last="Rahr Winther">Jakob Rahr Winther</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:24251119</idno><idno type="pmid">24251119</idno><idno type="doi">10.1016/j.redox.2013.10.005</idno><idno type="pmc">PMC3830055</idno><idno type="wicri:Area/Main/Corpus">000686</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000686</idno><idno type="wicri:Area/Main/Curation">000686</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000686</idno><idno type="wicri:Area/Main/Exploration">000686</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Intracellular glutathione pools are heterogeneously concentrated.</title><author><name sortKey="Montero, Davide" sort="Montero, Davide" uniqKey="Montero D" first="Davide" last="Montero">Davide Montero</name><affiliation wicri:level="1"><nlm:affiliation>Division of Molecular & Systems Toxicology, Department of Pharmaceutical Sciences, University of Basel, Klingelbergstrasse 50, 4056 Basel, Switzerland.</nlm:affiliation><country xml:lang="fr">Suisse</country><wicri:regionArea>Division of Molecular & Systems Toxicology, Department of Pharmaceutical Sciences, University of Basel, Klingelbergstrasse 50, 4056 Basel</wicri:regionArea><wicri:noRegion>4056 Basel</wicri:noRegion></affiliation></author><author><name sortKey="Tachibana, Christine" sort="Tachibana, Christine" uniqKey="Tachibana C" first="Christine" last="Tachibana">Christine Tachibana</name></author><author><name sortKey="Rahr Winther, Jakob" sort="Rahr Winther, Jakob" uniqKey="Rahr Winther J" first="Jakob" last="Rahr Winther">Jakob Rahr Winther</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">Redox biology</title><idno type="eISSN">2213-2317</idno><imprint><date when="2013" type="published">2013</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Cytosol (metabolism)</term><term>Endoplasmic Reticulum (metabolism)</term><term>Glutaredoxins (genetics)</term><term>Glutaredoxins (metabolism)</term><term>Glutathione (metabolism)</term><term>HeLa Cells (MeSH)</term><term>Homeostasis (MeSH)</term><term>Humans (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Cellules HeLa (MeSH)</term><term>Cytosol (métabolisme)</term><term>Glutarédoxines (génétique)</term><term>Glutarédoxines (métabolisme)</term><term>Glutathion 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type="abstract" xml:lang="en">Glutathione is present in millimolar concentrations in the cell, but its relative distribution among cellular compartments remains elusive. We have chosen the endoplasmic reticulum (ER) as an example organelle to study compartment-specific glutathione levels. Using a glutaredoxin sensor (sCGrx1pER), which rapidly and specifically equilibrates with the reduced glutathione (GSH)-glutathione disulfide (GSSG) redox couple with known equilibrium constant, we showed that the [GSH]:[GSSG] ratio in the ER of intact HeLa cells is less than 7:1. Taking into consideration the previously determined value for [GSH](2):[GSSG] in the ER of 83 mM, this translates into a total glutathione concentration in the ER ([GStot]=[GSH]+2[GSSG]) of greater than 15 mM. Since the integrated, intracellular [GStot] was measured as ~7 mM, we conclude the existence of a [GStot] gradient across the ER membrane. A possible homeostatic mechanism by which cytosol-derived glutathione is trapped in the ER is discussed. We propose a high [GStot] as a distinguishing feature of the ER environment compared to the extracellular space. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">24251119</PMID><DateCompleted><Year>2015</Year><Month>05</Month><Day>13</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Electronic-eCollection"><Journal><ISSN IssnType="Electronic">2213-2317</ISSN><JournalIssue CitedMedium="Internet"><Volume>1</Volume><PubDate><Year>2013</Year></PubDate></JournalIssue><Title>Redox biology</Title><ISOAbbreviation>Redox Biol</ISOAbbreviation></Journal><ArticleTitle>Intracellular glutathione pools are heterogeneously concentrated.</ArticleTitle><Pagination><MedlinePgn>508-13</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.redox.2013.10.005</ELocationID><Abstract><AbstractText>Glutathione is present in millimolar concentrations in the cell, but its relative distribution among cellular compartments remains elusive. We have chosen the endoplasmic reticulum (ER) as an example organelle to study compartment-specific glutathione levels. Using a glutaredoxin sensor (sCGrx1pER), which rapidly and specifically equilibrates with the reduced glutathione (GSH)-glutathione disulfide (GSSG) redox couple with known equilibrium constant, we showed that the [GSH]:[GSSG] ratio in the ER of intact HeLa cells is less than 7:1. Taking into consideration the previously determined value for [GSH](2):[GSSG] in the ER of 83 mM, this translates into a total glutathione concentration in the ER ([GStot]=[GSH]+2[GSSG]) of greater than 15 mM. Since the integrated, intracellular [GStot] was measured as ~7 mM, we conclude the existence of a [GStot] gradient across the ER membrane. A possible homeostatic mechanism by which cytosol-derived glutathione is trapped in the ER is discussed. We propose a high [GStot] as a distinguishing feature of the ER environment compared to the extracellular space. </AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Montero</LastName><ForeName>Davide</ForeName><Initials>D</Initials><AffiliationInfo><Affiliation>Division of Molecular & Systems Toxicology, Department of Pharmaceutical Sciences, University of Basel, Klingelbergstrasse 50, 4056 Basel, Switzerland.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Tachibana</LastName><ForeName>Christine</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Rahr Winther</LastName><ForeName>Jakob</ForeName><Initials>J</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>10</Month><Day>28</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Redox Biol</MedlineTA><NlmUniqueID>101605639</NlmUniqueID><ISSNLinking>2213-2317</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>GAN16C9B8O</RegistryNumber><NameOfSubstance UI="D005978">Glutathione</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D003600" MajorTopicYN="N">Cytosol</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004721" MajorTopicYN="N">Endoplasmic Reticulum</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><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="D006367" MajorTopicYN="N">HeLa Cells</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006706" MajorTopicYN="N">Homeostasis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">DTT, Dithiothreitol</Keyword><Keyword MajorTopicYN="N">EGSH, Half cell reduction potential of glutathione</Keyword><Keyword MajorTopicYN="N">ER, Endoplasmic reticulum</Keyword><Keyword MajorTopicYN="N">Endoplasmic reticulum</Keyword><Keyword MajorTopicYN="N">GSH, Reduced glutathione</Keyword><Keyword MajorTopicYN="N">GSSG, Glutathione disulfide</Keyword><Keyword MajorTopicYN="N">Glutaredoxin</Keyword><Keyword MajorTopicYN="N">Glutathione</Keyword><Keyword MajorTopicYN="N">NEM, N-ethylmaleimide</Keyword><Keyword MajorTopicYN="N">OxD, Percentage of oxidation</Keyword><Keyword MajorTopicYN="N">PDI, Protein disulfide isomerase</Keyword><Keyword MajorTopicYN="N">PERK, Double stranded RNA-activated protein kinase (PKR)-like ER kinase</Keyword><Keyword MajorTopicYN="N">RGS, [GSH]:[GSSG]</Keyword><Keyword MajorTopicYN="N">Redox Homeostasis</Keyword><Keyword MajorTopicYN="N">Redox compartmentalization</Keyword><Keyword MajorTopicYN="N">Redox, Reduction–oxidation</Keyword><Keyword MajorTopicYN="N">Reduction potential</Keyword><Keyword MajorTopicYN="N">TMM(PEG)12, Maleimide-activated polyethylene glycol</Keyword><Keyword MajorTopicYN="N">UPR, Unfolded protein response</Keyword><Keyword MajorTopicYN="N">XBP1, X-box binding protein 1</Keyword><Keyword MajorTopicYN="N">[GStot], Total glutathione concentration</Keyword><Keyword MajorTopicYN="N">sCGrx1p, C30S mutant of yeast glutaredoxin 1</Keyword></KeywordList><GeneralNote Owner="NLM">Original DateCompleted: 20131119</GeneralNote></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2013</Year><Month>09</Month><Day>16</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2013</Year><Month>10</Month><Day>21</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2013</Year><Month>10</Month><Day>22</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2013</Year><Month>11</Month><Day>20</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2013</Year><Month>11</Month><Day>20</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate 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Jul;17(7):3095-107</Citation><ArticleIdList><ArticleId IdType="pubmed">16672378</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed><affiliations><list><country><li>Suisse</li></country></list><tree><noCountry><name sortKey="Appenzeller Herzog, Christian" sort="Appenzeller Herzog, Christian" uniqKey="Appenzeller Herzog C" first="Christian" last="Appenzeller-Herzog">Christian Appenzeller-Herzog</name><name sortKey="Rahr Winther, Jakob" sort="Rahr Winther, Jakob" uniqKey="Rahr Winther J" first="Jakob" last="Rahr Winther">Jakob Rahr Winther</name><name sortKey="Tachibana, Christine" sort="Tachibana, Christine" uniqKey="Tachibana C" first="Christine" last="Tachibana">Christine Tachibana</name></noCountry><country name="Suisse"><noRegion><name sortKey="Montero, Davide" sort="Montero, Davide" uniqKey="Montero D" first="Davide" last="Montero">Davide Montero</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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