GlutaredoxinV1, Main, Exploration, bibRecord, 000316

Redox status in a model of cancer stem cells.

Identifieur interne : 000316 ( Main/Exploration ); précédent : 000315; suivant : 000317

Redox status in a model of cancer stem cells.

Auteurs : Mattia Zaccarin [Italie] ; Valentina Bosello-Travain [Italie] ; Maria Luisa Di Paolo [Italie] ; Marco Falda [Italie] ; Matilde Maiorino [Italie] ; Giovanni Miotto [Italie] ; Stefano Piccolo [Italie] ; Antonella Roveri [Italie] ; Fulvio Ursini [Italie] ; Rina Venerando [Italie] ; Stefano Toppo [Italie]

Source :

Archives of biochemistry and biophysics [ 1096-0384 ] ; 2017.

RBID : pubmed:27638050

Descripteurs français

KwdFr :
- Cellules souches tumorales (cytologie), Espèces réactives de l'oxygène (métabolisme), Glucose 6-phosphate dehydrogenase (métabolisme), Glutarédoxines (métabolisme), Humains (MeSH), Lignée cellulaire tumorale (MeSH), Lignée de cellules transformées (MeSH), Mutation (MeSH), Nucléotides (génétique), Oxydoréduction (MeSH), Oxygène (composition chimique), Protéomique (MeSH), Pyridines (composition chimique), Stress oxydatif (MeSH), Thioredoxin-disulfide reductase (métabolisme), Thiorédoxines (métabolisme), Transduction du signal (MeSH).
MESH :
- composition chimique : Oxygène, Pyridines.
- cytologie : Cellules souches tumorales.
- génétique : Nucléotides.
- métabolisme : Espèces réactives de l'oxygène, Glucose 6-phosphate dehydrogenase, Glutarédoxines, Thioredoxin-disulfide reductase, Thiorédoxines.
- Humains, Lignée cellulaire tumorale, Lignée de cellules transformées, Mutation, Oxydoréduction, Protéomique, Stress oxydatif, Transduction du signal.

English descriptors

KwdEn :
- Cell Line, Transformed (MeSH), Cell Line, Tumor (MeSH), Glucosephosphate Dehydrogenase (metabolism), Glutaredoxins (metabolism), Humans (MeSH), Mutation (MeSH), Neoplastic Stem Cells (cytology), Nucleotides (genetics), Oxidation-Reduction (MeSH), Oxidative Stress (MeSH), Oxygen (chemistry), Proteomics (MeSH), Pyridines (chemistry), Reactive Oxygen Species (metabolism), Signal Transduction (MeSH), Thioredoxin-Disulfide Reductase (metabolism), Thioredoxins (metabolism).
MESH :
- chemical , chemistry : Oxygen, Pyridines.
- chemical , genetics : Nucleotides.
- chemical , metabolism : Glucosephosphate Dehydrogenase, Glutaredoxins, Reactive Oxygen Species, Thioredoxin-Disulfide Reductase, Thioredoxins.
- cytology : Neoplastic Stem Cells.
- Cell Line, Transformed, Cell Line, Tumor, Humans, Mutation, Oxidation-Reduction, Oxidative Stress, Proteomics, Signal Transduction.

Abstract

Reversible oxidation of Cys residues is a crucial element of redox homeostasis and signaling. According to a popular concept in oxidative stress signaling, the oxidation of targets of signals can only take place following an overwhelming of the cellular antioxidant capacity. This concept, however, ignores the activation of feedback mechanisms possibly leading to a paradoxical effect. In a model of cancer stem cells (CSC), stably overexpressing the TAZ oncogene, we observed that the increased formation of oxidants is associated with a globally more reduced state of proteins. Redox proteomics revealed that several proteins, capable of undergoing reversible redox transitions, are indeed more reduced while just few are more oxidized. Among the proteins more oxidized, G6PDH emerges as both more expressed and activated by oxidation. This accounts for the observed more reduced state of the NADPH/NADP⁺ couple. The dynamic redox flux generating this apparently paradoxical effect is rationalized in a computational system biology model highlighting the crucial role of G6PDH activity on the rate of redox transitions eventually leading to the reduction of reversible redox switches.

DOI: 10.1016/j.abb.2016.09.002
PubMed: 27638050

Affiliations:

Italie

Links toward previous steps (curation, corpus...)

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Le document en format XML

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<term>Cell Line, Tumor (MeSH)</term>
<term>Glucosephosphate Dehydrogenase (metabolism)</term>
<term>Glutaredoxins (metabolism)</term>
<term>Humans (MeSH)</term>
<term>Mutation (MeSH)</term>
<term>Neoplastic Stem Cells (cytology)</term>
<term>Nucleotides (genetics)</term>
<term>Oxidation-Reduction (MeSH)</term>
<term>Oxidative Stress (MeSH)</term>
<term>Oxygen (chemistry)</term>
<term>Proteomics (MeSH)</term>
<term>Pyridines (chemistry)</term>
<term>Reactive Oxygen Species (metabolism)</term>
<term>Signal Transduction (MeSH)</term>
<term>Thioredoxin-Disulfide Reductase (metabolism)</term>
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<term>Glutarédoxines (métabolisme)</term>
<term>Humains (MeSH)</term>
<term>Lignée cellulaire tumorale (MeSH)</term>
<term>Lignée de cellules transformées (MeSH)</term>
<term>Mutation (MeSH)</term>
<term>Nucléotides (génétique)</term>
<term>Oxydoréduction (MeSH)</term>
<term>Oxygène (composition chimique)</term>
<term>Protéomique (MeSH)</term>
<term>Pyridines (composition chimique)</term>
<term>Stress oxydatif (MeSH)</term>
<term>Thioredoxin-disulfide reductase (métabolisme)</term>
<term>Thiorédoxines (métabolisme)</term>
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<term>Reactive Oxygen Species</term>
<term>Thioredoxin-Disulfide Reductase</term>
<term>Thioredoxins</term>
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<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Nucléotides</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Espèces réactives de l'oxygène</term>
<term>Glucose 6-phosphate dehydrogenase</term>
<term>Glutarédoxines</term>
<term>Thioredoxin-disulfide reductase</term>
<term>Thiorédoxines</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Cell Line, Transformed</term>
<term>Cell Line, Tumor</term>
<term>Humans</term>
<term>Mutation</term>
<term>Oxidation-Reduction</term>
<term>Oxidative Stress</term>
<term>Proteomics</term>
<term>Signal Transduction</term>
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<term>Lignée cellulaire tumorale</term>
<term>Lignée de cellules transformées</term>
<term>Mutation</term>
<term>Oxydoréduction</term>
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<front><div type="abstract" xml:lang="en">Reversible oxidation of Cys residues is a crucial element of redox homeostasis and signaling. According to a popular concept in oxidative stress signaling, the oxidation of targets of signals can only take place following an overwhelming of the cellular antioxidant capacity. This concept, however, ignores the activation of feedback mechanisms possibly leading to a paradoxical effect. In a model of cancer stem cells (CSC), stably overexpressing the TAZ oncogene, we observed that the increased formation of oxidants is associated with a globally more reduced state of proteins. Redox proteomics revealed that several proteins, capable of undergoing reversible redox transitions, are indeed more reduced while just few are more oxidized. Among the proteins more oxidized, G6PDH emerges as both more expressed and activated by oxidation. This accounts for the observed more reduced state of the NADPH/NADP<sup>+</sup>
 couple. The dynamic redox flux generating this apparently paradoxical effect is rationalized in a computational system biology model highlighting the crucial role of G6PDH activity on the rate of redox transitions eventually leading to the reduction of reversible redox switches.</div>
</front>
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<Abstract><AbstractText>Reversible oxidation of Cys residues is a crucial element of redox homeostasis and signaling. According to a popular concept in oxidative stress signaling, the oxidation of targets of signals can only take place following an overwhelming of the cellular antioxidant capacity. This concept, however, ignores the activation of feedback mechanisms possibly leading to a paradoxical effect. In a model of cancer stem cells (CSC), stably overexpressing the TAZ oncogene, we observed that the increased formation of oxidants is associated with a globally more reduced state of proteins. Redox proteomics revealed that several proteins, capable of undergoing reversible redox transitions, are indeed more reduced while just few are more oxidized. Among the proteins more oxidized, G6PDH emerges as both more expressed and activated by oxidation. This accounts for the observed more reduced state of the NADPH/NADP<sup>+</sup>
 couple. The dynamic redox flux generating this apparently paradoxical effect is rationalized in a computational system biology model highlighting the crucial role of G6PDH activity on the rate of redox transitions eventually leading to the reduction of reversible redox switches.</AbstractText>
<CopyrightInformation>Copyright © 2016 Elsevier Inc. All rights reserved.</CopyrightInformation>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Zaccarin</LastName>
<ForeName>Mattia</ForeName>
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<ForeName>Valentina</ForeName>
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<AffiliationInfo><Affiliation>Department of Molecular Medicine, University of Padova, Viale G.Colombo 3, 35121 Padova, Italy.</Affiliation>
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<Author ValidYN="Y"><LastName>Di Paolo</LastName>
<ForeName>Maria Luisa</ForeName>
<Initials>ML</Initials>
<AffiliationInfo><Affiliation>Department of Molecular Medicine, University of Padova, Viale G.Colombo 3, 35121 Padova, Italy.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Falda</LastName>
<ForeName>Marco</ForeName>
<Initials>M</Initials>
<AffiliationInfo><Affiliation>Department of Molecular Medicine, University of Padova, Viale G.Colombo 3, 35121 Padova, Italy.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Maiorino</LastName>
<ForeName>Matilde</ForeName>
<Initials>M</Initials>
<AffiliationInfo><Affiliation>Department of Molecular Medicine, University of Padova, Viale G.Colombo 3, 35121 Padova, Italy.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Miotto</LastName>
<ForeName>Giovanni</ForeName>
<Initials>G</Initials>
<AffiliationInfo><Affiliation>Department of Molecular Medicine, University of Padova, Viale G.Colombo 3, 35121 Padova, Italy.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Piccolo</LastName>
<ForeName>Stefano</ForeName>
<Initials>S</Initials>
<AffiliationInfo><Affiliation>Department of Molecular Medicine, University of Padova, Viale G.Colombo 3, 35121 Padova, Italy.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Roveri</LastName>
<ForeName>Antonella</ForeName>
<Initials>A</Initials>
<AffiliationInfo><Affiliation>Department of Molecular Medicine, University of Padova, Viale G.Colombo 3, 35121 Padova, Italy.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Ursini</LastName>
<ForeName>Fulvio</ForeName>
<Initials>F</Initials>
<AffiliationInfo><Affiliation>Department of Molecular Medicine, University of Padova, Viale G.Colombo 3, 35121 Padova, Italy.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Venerando</LastName>
<ForeName>Rina</ForeName>
<Initials>R</Initials>
<AffiliationInfo><Affiliation>Department of Molecular Medicine, University of Padova, Viale G.Colombo 3, 35121 Padova, Italy.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Toppo</LastName>
<ForeName>Stefano</ForeName>
<Initials>S</Initials>
<AffiliationInfo><Affiliation>Department of Molecular Medicine, University of Padova, Viale G.Colombo 3, 35121 Padova, Italy. Electronic address: stefano.toppo@unipd.it.</Affiliation>
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</Author>
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<Language>eng</Language>
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<ArticleDate DateType="Electronic"><Year>2016</Year>
<Month>09</Month>
<Day>13</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo><Country>United States</Country>
<MedlineTA>Arch Biochem Biophys</MedlineTA>
<NlmUniqueID>0372430</NlmUniqueID>
<ISSNLinking>0003-9861</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D009711">Nucleotides</NameOfSubstance>
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<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D011725">Pyridines</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D017382">Reactive Oxygen Species</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>52500-60-4</RegistryNumber>
<NameOfSubstance UI="D013879">Thioredoxins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 1.1.1.49</RegistryNumber>
<NameOfSubstance UI="D005954">Glucosephosphate Dehydrogenase</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 1.8.1.9</RegistryNumber>
<NameOfSubstance UI="D013880">Thioredoxin-Disulfide Reductase</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>NH9L3PP67S</RegistryNumber>
<NameOfSubstance UI="C023666">pyridine</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>S88TT14065</RegistryNumber>
<NameOfSubstance UI="D010100">Oxygen</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
<MeshHeadingList><MeshHeading><DescriptorName UI="D002461" MajorTopicYN="N">Cell Line, Transformed</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D045744" MajorTopicYN="N">Cell Line, Tumor</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D005954" MajorTopicYN="N">Glucosephosphate Dehydrogenase</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="D006801" MajorTopicYN="N">Humans</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D009154" MajorTopicYN="N">Mutation</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D014411" MajorTopicYN="N">Neoplastic Stem Cells</DescriptorName>
<QualifierName UI="Q000166" MajorTopicYN="Y">cytology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D009711" MajorTopicYN="N">Nucleotides</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D010084" MajorTopicYN="Y">Oxidation-Reduction</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D018384" MajorTopicYN="N">Oxidative Stress</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D010100" MajorTopicYN="N">Oxygen</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D040901" MajorTopicYN="N">Proteomics</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D011725" MajorTopicYN="N">Pyridines</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D017382" MajorTopicYN="N">Reactive Oxygen Species</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D015398" MajorTopicYN="N">Signal Transduction</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D013880" MajorTopicYN="N">Thioredoxin-Disulfide Reductase</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D013879" MajorTopicYN="N">Thioredoxins</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
</MeshHeadingList>
<KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Cancer stem cells</Keyword>
<Keyword MajorTopicYN="N">Protein thiols</Keyword>
<Keyword MajorTopicYN="N">Redox proteomics</Keyword>
<Keyword MajorTopicYN="N">Redox state</Keyword>
</KeywordList>
</MedlineCitation>
<PubmedData><History><PubMedPubDate PubStatus="received"><Year>2016</Year>
<Month>08</Month>
<Day>05</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="revised"><Year>2016</Year>
<Month>09</Month>
<Day>09</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="accepted"><Year>2016</Year>
<Month>09</Month>
<Day>12</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="pubmed"><Year>2016</Year>
<Month>9</Month>
<Day>18</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="medline"><Year>2017</Year>
<Month>5</Month>
<Day>16</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="entrez"><Year>2016</Year>
<Month>9</Month>
<Day>18</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
</History>
<PublicationStatus>ppublish</PublicationStatus>
<ArticleIdList><ArticleId IdType="pubmed">27638050</ArticleId>
<ArticleId IdType="pii">S0003-9861(16)30319-8</ArticleId>
<ArticleId IdType="doi">10.1016/j.abb.2016.09.002</ArticleId>
</ArticleIdList>
</PubmedData>
</pubmed>
<affiliations><list><country><li>Italie</li>
</country>
</list>
<tree><country name="Italie"><noRegion><name sortKey="Zaccarin, Mattia" sort="Zaccarin, Mattia" uniqKey="Zaccarin M" first="Mattia" last="Zaccarin">Mattia Zaccarin</name>
</noRegion>
<name sortKey="Bosello Travain, Valentina" sort="Bosello Travain, Valentina" uniqKey="Bosello Travain V" first="Valentina" last="Bosello-Travain">Valentina Bosello-Travain</name>
<name sortKey="Di Paolo, Maria Luisa" sort="Di Paolo, Maria Luisa" uniqKey="Di Paolo M" first="Maria Luisa" last="Di Paolo">Maria Luisa Di Paolo</name>
<name sortKey="Falda, Marco" sort="Falda, Marco" uniqKey="Falda M" first="Marco" last="Falda">Marco Falda</name>
<name sortKey="Maiorino, Matilde" sort="Maiorino, Matilde" uniqKey="Maiorino M" first="Matilde" last="Maiorino">Matilde Maiorino</name>
<name sortKey="Miotto, Giovanni" sort="Miotto, Giovanni" uniqKey="Miotto G" first="Giovanni" last="Miotto">Giovanni Miotto</name>
<name sortKey="Piccolo, Stefano" sort="Piccolo, Stefano" uniqKey="Piccolo S" first="Stefano" last="Piccolo">Stefano Piccolo</name>
<name sortKey="Roveri, Antonella" sort="Roveri, Antonella" uniqKey="Roveri A" first="Antonella" last="Roveri">Antonella Roveri</name>
<name sortKey="Toppo, Stefano" sort="Toppo, Stefano" uniqKey="Toppo S" first="Stefano" last="Toppo">Stefano Toppo</name>
<name sortKey="Ursini, Fulvio" sort="Ursini, Fulvio" uniqKey="Ursini F" first="Fulvio" last="Ursini">Fulvio Ursini</name>
<name sortKey="Venerando, Rina" sort="Venerando, Rina" uniqKey="Venerando R" first="Rina" last="Venerando">Rina Venerando</name>
</country>
</tree>
</affiliations>
</record>

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	Serveur d'exploration sur la glutarédoxine
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Redox status in a model of cancer stem cells.

Redox status in a model of cancer stem cells.

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