GlutaredoxinV1, Main, Exploration, bibRecord, 000360

Glutathione oxidation in response to intracellular H2O2: Key but overlapping roles for dehydroascorbate reductases.

Identifieur interne : 000360 ( Main/Exploration ); précédent : 000359; suivant : 000361

Glutathione oxidation in response to intracellular H2O2: Key but overlapping roles for dehydroascorbate reductases.

Auteurs : Marie-Sylviane Rahantaniaina [France] ; Shengchun Li [France] ; Gilles Chatel-Innocenti [France] ; Andrée Tuzet [France] ; Amna Mhamdi [France] ; Hélène Vanacker [France] ; Graham Noctor [France]

Source :

Plant signaling & behavior [ 1559-2324 ] ; 2017.

RBID : pubmed:28782990

Descripteurs français

KwdFr :
- Amitrole (pharmacologie), Arabidopsis (effets des médicaments et des substances chimiques), Arabidopsis (génétique), Arabidopsis (métabolisme), Espace intracellulaire (métabolisme), Glutathion (métabolisme), Oxidoreductases (métabolisme), Oxydants (MeSH), Oxydoréduction (MeSH), Peroxyde d'hydrogène (métabolisme), Peroxyde d'hydrogène (toxicité), Phénotype (MeSH), Régulation de l'expression des gènes végétaux (effets des médicaments et des substances chimiques), Stress oxydatif (effets des médicaments et des substances chimiques).
MESH :
- effets des médicaments et des substances chimiques : Arabidopsis, Régulation de l'expression des gènes végétaux, Stress oxydatif.
- génétique : Arabidopsis.
- métabolisme : Arabidopsis, Espace intracellulaire, Glutathion, Oxidoreductases, Peroxyde d'hydrogène.
- pharmacologie : Amitrole.
- toxicité : Peroxyde d'hydrogène.
- Oxydants, Oxydoréduction, Phénotype.

English descriptors

KwdEn :
- Amitrole (pharmacology), Arabidopsis (drug effects), Arabidopsis (genetics), Arabidopsis (metabolism), Gene Expression Regulation, Plant (drug effects), Glutathione (metabolism), Hydrogen Peroxide (metabolism), Hydrogen Peroxide (toxicity), Intracellular Space (metabolism), Oxidants (MeSH), Oxidation-Reduction (MeSH), Oxidative Stress (drug effects), Oxidoreductases (metabolism), Phenotype (MeSH).
MESH :
- chemical , metabolism : Glutathione, Hydrogen Peroxide, Oxidoreductases.
- chemical , pharmacology : Amitrole.
- drug effects : Arabidopsis, Gene Expression Regulation, Plant, Oxidative Stress.
- genetics : Arabidopsis.
- metabolism : Arabidopsis, Intracellular Space.
- chemical , toxicity : Hydrogen Peroxide.
- chemical : Oxidants, Oxidation-Reduction, Phenotype.

Abstract

Glutathione is a pivotal molecule in oxidative stress, during which it is potentially oxidized by several pathways linked to H₂O₂ detoxification. We have investigated the response and functional importance of 3 potential routes for glutathione oxidation pathways mediated by glutathione S-transferases (GST), glutaredoxin-dependent peroxiredoxins (PRXII), and dehydroascorbate reductases (DHAR) in Arabidopsis during oxidative stress. Loss-of-function gstU8, gstU24, gstF8, prxIIE and prxIIF mutants as well as double gstU8 gstU24, gstU8 gstF8, gstU24 gstF8, prxIIE prxIIF mutants were obtained. No mutant lines showed marked changes in their phenotype and glutathione profiles in comparison to the wild-type plants in either optimal conditions or oxidative stress triggered by catalase inhibition. By contrast, multiple loss of DHAR functions markedly decreased glutathione oxidation triggered by catalase deficiency. To assess whether this effect was mediated directly by loss of DHAR enzyme activity, or more indirectly by upregulation of other enzymes involved in glutathione and ascorbate recycling, we measured expression of glutathione reductase (GR) and expression and activity of monodehydroascorbate reductases (MDHAR). No evidence was obtained that either GRs or MDHARs were upregulated in plants lacking DHAR function. Hence, interplay between different DHARs appears to be necessary to couple ascorbate and glutathione pools and to allow glutathione-related signaling during enhanced H₂O₂ metabolism.

DOI: 10.1080/15592324.2017.1356531
PubMed: 28782990
PubMed Central: PMC5616140

Affiliations:

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

to stream Main, to step Corpus: 000315
to stream Main, to step Curation: 000315

Le document en format XML

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<term>Arabidopsis (metabolism)</term>
<term>Gene Expression Regulation, Plant (drug effects)</term>
<term>Glutathione (metabolism)</term>
<term>Hydrogen Peroxide (metabolism)</term>
<term>Hydrogen Peroxide (toxicity)</term>
<term>Intracellular Space (metabolism)</term>
<term>Oxidants (MeSH)</term>
<term>Oxidation-Reduction (MeSH)</term>
<term>Oxidative Stress (drug effects)</term>
<term>Oxidoreductases (metabolism)</term>
<term>Phenotype (MeSH)</term>
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<term>Arabidopsis (effets des médicaments et des substances chimiques)</term>
<term>Arabidopsis (génétique)</term>
<term>Arabidopsis (métabolisme)</term>
<term>Espace intracellulaire (métabolisme)</term>
<term>Glutathion (métabolisme)</term>
<term>Oxidoreductases (métabolisme)</term>
<term>Oxydants (MeSH)</term>
<term>Oxydoréduction (MeSH)</term>
<term>Peroxyde d'hydrogène (métabolisme)</term>
<term>Peroxyde d'hydrogène (toxicité)</term>
<term>Phénotype (MeSH)</term>
<term>Régulation de l'expression des gènes végétaux (effets des médicaments et des substances chimiques)</term>
<term>Stress oxydatif (effets des médicaments et des substances chimiques)</term>
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<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glutathione</term>
<term>Hydrogen Peroxide</term>
<term>Oxidoreductases</term>
</keywords>
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<term>Gene Expression Regulation, Plant</term>
<term>Oxidative Stress</term>
</keywords>
<keywords scheme="MESH" qualifier="effets des médicaments et des substances chimiques" xml:lang="fr"><term>Arabidopsis</term>
<term>Régulation de l'expression des gènes végétaux</term>
<term>Stress oxydatif</term>
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<term>Intracellular Space</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Arabidopsis</term>
<term>Espace intracellulaire</term>
<term>Glutathion</term>
<term>Oxidoreductases</term>
<term>Peroxyde d'hydrogène</term>
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<term>Oxidation-Reduction</term>
<term>Phenotype</term>
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<front><div type="abstract" xml:lang="en">Glutathione is a pivotal molecule in oxidative stress, during which it is potentially oxidized by several pathways linked to H<sub>2</sub>
O<sub>2</sub>
 detoxification. We have investigated the response and functional importance of 3 potential routes for glutathione oxidation pathways mediated by glutathione S-transferases (GST), glutaredoxin-dependent peroxiredoxins (PRXII), and dehydroascorbate reductases (DHAR) in Arabidopsis during oxidative stress. Loss-of-function gstU8, gstU24, gstF8, prxIIE and prxIIF mutants as well as double gstU8 gstU24, gstU8 gstF8, gstU24 gstF8, prxIIE prxIIF mutants were obtained. No mutant lines showed marked changes in their phenotype and glutathione profiles in comparison to the wild-type plants in either optimal conditions or oxidative stress triggered by catalase inhibition. By contrast, multiple loss of DHAR functions markedly decreased glutathione oxidation triggered by catalase deficiency. To assess whether this effect was mediated directly by loss of DHAR enzyme activity, or more indirectly by upregulation of other enzymes involved in glutathione and ascorbate recycling, we measured expression of glutathione reductase (GR) and expression and activity of monodehydroascorbate reductases (MDHAR). No evidence was obtained that either GRs or MDHARs were upregulated in plants lacking DHAR function. Hence, interplay between different DHARs appears to be necessary to couple ascorbate and glutathione pools and to allow glutathione-related signaling during enhanced H<sub>2</sub>
O<sub>2</sub>
 metabolism.</div>
</front>
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<DateCompleted><Year>2018</Year>
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<Title>Plant signaling & behavior</Title>
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<ArticleTitle>Glutathione oxidation in response to intracellular H<sub>2</sub>
O<sub>2</sub>
: Key but overlapping roles for dehydroascorbate reductases.</ArticleTitle>
<Pagination><MedlinePgn>e1356531</MedlinePgn>
</Pagination>
<ELocationID EIdType="doi" ValidYN="Y">10.1080/15592324.2017.1356531</ELocationID>
<Abstract><AbstractText>Glutathione is a pivotal molecule in oxidative stress, during which it is potentially oxidized by several pathways linked to H<sub>2</sub>
O<sub>2</sub>
 detoxification. We have investigated the response and functional importance of 3 potential routes for glutathione oxidation pathways mediated by glutathione S-transferases (GST), glutaredoxin-dependent peroxiredoxins (PRXII), and dehydroascorbate reductases (DHAR) in Arabidopsis during oxidative stress. Loss-of-function gstU8, gstU24, gstF8, prxIIE and prxIIF mutants as well as double gstU8 gstU24, gstU8 gstF8, gstU24 gstF8, prxIIE prxIIF mutants were obtained. No mutant lines showed marked changes in their phenotype and glutathione profiles in comparison to the wild-type plants in either optimal conditions or oxidative stress triggered by catalase inhibition. By contrast, multiple loss of DHAR functions markedly decreased glutathione oxidation triggered by catalase deficiency. To assess whether this effect was mediated directly by loss of DHAR enzyme activity, or more indirectly by upregulation of other enzymes involved in glutathione and ascorbate recycling, we measured expression of glutathione reductase (GR) and expression and activity of monodehydroascorbate reductases (MDHAR). No evidence was obtained that either GRs or MDHARs were upregulated in plants lacking DHAR function. Hence, interplay between different DHARs appears to be necessary to couple ascorbate and glutathione pools and to allow glutathione-related signaling during enhanced H<sub>2</sub>
O<sub>2</sub>
 metabolism.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Rahantaniaina</LastName>
<ForeName>Marie-Sylviane</ForeName>
<Initials>MS</Initials>
<AffiliationInfo><Affiliation>a Institute of Plant Sciences Paris-Saclay (IPS2), UMR 9213/UMR1403 , Université Paris-Sud, CNRS, INRA, Université d'Evry, Université Paris-Diderot, Sorbonne Paris-Cité , Bâtiment 630, Orsay , France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Li</LastName>
<ForeName>Shengchun</ForeName>
<Initials>S</Initials>
<AffiliationInfo><Affiliation>a Institute of Plant Sciences Paris-Saclay (IPS2), UMR 9213/UMR1403 , Université Paris-Sud, CNRS, INRA, Université d'Evry, Université Paris-Diderot, Sorbonne Paris-Cité , Bâtiment 630, Orsay , France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Chatel-Innocenti</LastName>
<ForeName>Gilles</ForeName>
<Initials>G</Initials>
<AffiliationInfo><Affiliation>a Institute of Plant Sciences Paris-Saclay (IPS2), UMR 9213/UMR1403 , Université Paris-Sud, CNRS, INRA, Université d'Evry, Université Paris-Diderot, Sorbonne Paris-Cité , Bâtiment 630, Orsay , France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Tuzet</LastName>
<ForeName>Andrée</ForeName>
<Initials>A</Initials>
<AffiliationInfo><Affiliation>b Unité Mixte de Recherche ECOSYS / Pôle BIOCLIMATOLOGIE, INRA - AgroParisTech , Route de la Ferme, Thiverval-Grignon , France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Mhamdi</LastName>
<ForeName>Amna</ForeName>
<Initials>A</Initials>
<AffiliationInfo><Affiliation>a Institute of Plant Sciences Paris-Saclay (IPS2), UMR 9213/UMR1403 , Université Paris-Sud, CNRS, INRA, Université d'Evry, Université Paris-Diderot, Sorbonne Paris-Cité , Bâtiment 630, Orsay , France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Vanacker</LastName>
<ForeName>Hélène</ForeName>
<Initials>H</Initials>
<AffiliationInfo><Affiliation>a Institute of Plant Sciences Paris-Saclay (IPS2), UMR 9213/UMR1403 , Université Paris-Sud, CNRS, INRA, Université d'Evry, Université Paris-Diderot, Sorbonne Paris-Cité , Bâtiment 630, Orsay , France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Noctor</LastName>
<ForeName>Graham</ForeName>
<Initials>G</Initials>
<AffiliationInfo><Affiliation>a Institute of Plant Sciences Paris-Saclay (IPS2), UMR 9213/UMR1403 , Université Paris-Sud, CNRS, INRA, Université d'Evry, Université Paris-Diderot, Sorbonne Paris-Cité , Bâtiment 630, Orsay , France.</Affiliation>
</AffiliationInfo>
</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>2017</Year>
<Month>08</Month>
<Day>07</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo><Country>United States</Country>
<MedlineTA>Plant Signal Behav</MedlineTA>
<NlmUniqueID>101291431</NlmUniqueID>
<ISSNLinking>1559-2316</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D016877">Oxidants</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>BBX060AN9V</RegistryNumber>
<NameOfSubstance UI="D006861">Hydrogen Peroxide</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 1.-</RegistryNumber>
<NameOfSubstance UI="D010088">Oxidoreductases</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 1.8.5.1</RegistryNumber>
<NameOfSubstance UI="C020666">glutathione dehydrogenase (ascorbate)</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>GAN16C9B8O</RegistryNumber>
<NameOfSubstance UI="D005978">Glutathione</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>ZF80H5GXUF</RegistryNumber>
<NameOfSubstance UI="D000640">Amitrole</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
<MeshHeadingList><MeshHeading><DescriptorName UI="D000640" MajorTopicYN="N">Amitrole</DescriptorName>
<QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D017360" MajorTopicYN="N">Arabidopsis</DescriptorName>
<QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D018506" MajorTopicYN="N">Gene Expression Regulation, Plant</DescriptorName>
<QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D005978" MajorTopicYN="N">Glutathione</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D006861" MajorTopicYN="N">Hydrogen Peroxide</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
<QualifierName UI="Q000633" MajorTopicYN="Y">toxicity</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D042541" MajorTopicYN="N">Intracellular Space</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D016877" MajorTopicYN="N">Oxidants</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D018384" MajorTopicYN="N">Oxidative Stress</DescriptorName>
<QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D010088" MajorTopicYN="N">Oxidoreductases</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D010641" MajorTopicYN="N">Phenotype</DescriptorName>
</MeshHeading>
</MeshHeadingList>
<KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">Antioxidant</Keyword>
<Keyword MajorTopicYN="Y">ascorbate</Keyword>
<Keyword MajorTopicYN="Y">glutathione</Keyword>
<Keyword MajorTopicYN="Y">glutathione S-transferase</Keyword>
<Keyword MajorTopicYN="Y">hydrogen peroxide</Keyword>
<Keyword MajorTopicYN="Y">oxidative stress</Keyword>
<Keyword MajorTopicYN="Y">peroxiredoxin</Keyword>
</KeywordList>
</MedlineCitation>
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<Month>8</Month>
<Day>8</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="medline"><Year>2018</Year>
<Month>5</Month>
<Day>31</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="entrez"><Year>2017</Year>
<Month>8</Month>
<Day>8</Day>
<Hour>6</Hour>
<Minute>0</Minute>
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<PublicationStatus>ppublish</PublicationStatus>
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<tree><country name="France"><region name="Île-de-France"><name sortKey="Rahantaniaina, Marie Sylviane" sort="Rahantaniaina, Marie Sylviane" uniqKey="Rahantaniaina M" first="Marie-Sylviane" last="Rahantaniaina">Marie-Sylviane Rahantaniaina</name>
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Glutathione oxidation in response to intracellular H2O2: Key but overlapping roles for dehydroascorbate reductases.

Glutathione oxidation in response to intracellular H2O2: Key but overlapping roles for dehydroascorbate reductases.

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