GlutaredoxinV1, Main, Exploration, bibRecord, 000762

Glutaredoxin regulates vascular development by reversible glutathionylation of sirtuin 1.

Identifieur interne : 000762 ( Main/Exploration ); précédent : 000761; suivant : 000763

Glutaredoxin regulates vascular development by reversible glutathionylation of sirtuin 1.

Auteurs : Lars Br Utigam [Suède] ; Lasse Dahl Ejby Jensen ; Gereon Poschmann ; Staffan Nyström ; Sarah Bannenberg ; Kristian Dreij ; Klaudia Lepka ; Timour Prozorovski ; Sergio J. Montano ; Orhan Aktas ; Per Uhlén ; Kai Stühler ; Yihai Cao ; Arne Holmgren ; Carsten Berndt

Source :

Proceedings of the National Academy of Sciences of the United States of America [ 1091-6490 ] ; 2013.

RBID : pubmed:24277839

Descripteurs français

English descriptors

KwdEn :
- Animals (MeSH), Blotting, Western (MeSH), Cardiovascular System (embryology), DNA Primers (genetics), Gene Knockdown Techniques (MeSH), Glutaredoxins (genetics), Glutaredoxins (metabolism), Glutathione (metabolism), HeLa Cells (MeSH), Humans (MeSH), Mass Spectrometry (MeSH), Microscopy, Confocal (MeSH), Neovascularization, Physiologic (physiology), Oxidation-Reduction (MeSH), Real-Time Polymerase Chain Reaction (MeSH), Signal Transduction (genetics), Signal Transduction (physiology), Sirtuin 1 (metabolism), Time-Lapse Imaging (MeSH), Zebrafish (MeSH).
MESH :
- chemical , genetics : DNA Primers, Glutaredoxins.
- embryology : Cardiovascular System.
- genetics : Signal Transduction.
- chemical , metabolism : Glutaredoxins, Glutathione, Sirtuin 1.
- physiology : Neovascularization, Physiologic, Signal Transduction.
- Animals, Blotting, Western, Gene Knockdown Techniques, HeLa Cells, Humans, Mass Spectrometry, Microscopy, Confocal, Oxidation-Reduction, Real-Time Polymerase Chain Reaction, Time-Lapse Imaging, Zebrafish.

Abstract

Embryonic development depends on complex and precisely orchestrated signaling pathways including specific reduction/oxidation cascades. Oxidoreductases of the thioredoxin family are key players conveying redox signals through reversible posttranslational modifications of protein thiols. The importance of this protein family during embryogenesis has recently been exemplified for glutaredoxin 2, a vertebrate-specific glutathione-disulfide oxidoreductase with a critical role for embryonic brain development. Here, we discovered an essential function of glutaredoxin 2 during vascular development. Confocal microscopy and time-lapse studies based on two-photon microscopy revealed that morpholino-based knockdown of glutaredoxin 2 in zebrafish, a model organism to study vertebrate embryogenesis, resulted in a delayed and disordered blood vessel network. We were able to show that formation of a functional vascular system requires glutaredoxin 2-dependent reversible S-glutathionylation of the NAD(+)-dependent protein deacetylase sirtuin 1. Using mass spectrometry, we identified a cysteine residue in the conserved catalytic region of sirtuin 1 as target for glutaredoxin 2-specific deglutathionylation. Thereby, glutaredoxin 2-mediated redox regulation controls enzymatic activity of sirtuin 1, a mechanism we found to be conserved between zebrafish and humans. These results link S-glutathionylation to vertebrate development and successful embryonic angiogenesis.

DOI: 10.1073/pnas.1313753110
PubMed: 24277839
PubMed Central: PMC3864331

Affiliations:

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

to stream Main, to step Corpus: 000684
to stream Main, to step Curation: 000684

Le document en format XML

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<term>Blotting, Western (MeSH)</term>
<term>Cardiovascular System (embryology)</term>
<term>DNA Primers (genetics)</term>
<term>Gene Knockdown Techniques (MeSH)</term>
<term>Glutaredoxins (genetics)</term>
<term>Glutaredoxins (metabolism)</term>
<term>Glutathione (metabolism)</term>
<term>HeLa Cells (MeSH)</term>
<term>Humans (MeSH)</term>
<term>Mass Spectrometry (MeSH)</term>
<term>Microscopy, Confocal (MeSH)</term>
<term>Neovascularization, Physiologic (physiology)</term>
<term>Oxidation-Reduction (MeSH)</term>
<term>Real-Time Polymerase Chain Reaction (MeSH)</term>
<term>Signal Transduction (genetics)</term>
<term>Signal Transduction (physiology)</term>
<term>Sirtuin 1 (metabolism)</term>
<term>Time-Lapse Imaging (MeSH)</term>
<term>Zebrafish (MeSH)</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Amorces ADN (génétique)</term>
<term>Animaux (MeSH)</term>
<term>Cellules HeLa (MeSH)</term>
<term>Danio zébré (MeSH)</term>
<term>Glutarédoxines (génétique)</term>
<term>Glutarédoxines (métabolisme)</term>
<term>Glutathion (métabolisme)</term>
<term>Humains (MeSH)</term>
<term>Imagerie accélérée (MeSH)</term>
<term>Microscopie confocale (MeSH)</term>
<term>Néovascularisation physiologique (physiologie)</term>
<term>Oxydoréduction (MeSH)</term>
<term>Réaction de polymérisation en chaine en temps réel (MeSH)</term>
<term>Sirtuine-1 (métabolisme)</term>
<term>Spectrométrie de masse (MeSH)</term>
<term>Système cardiovasculaire (embryologie)</term>
<term>Technique de Western (MeSH)</term>
<term>Techniques de knock-down de gènes (MeSH)</term>
<term>Transduction du signal (génétique)</term>
<term>Transduction du signal (physiologie)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>DNA Primers</term>
<term>Glutaredoxins</term>
</keywords>
<keywords scheme="MESH" qualifier="embryologie" xml:lang="fr"><term>Système cardiovasculaire</term>
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</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Signal Transduction</term>
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<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Amorces ADN</term>
<term>Glutarédoxines</term>
<term>Transduction du signal</term>
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<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glutaredoxins</term>
<term>Glutathione</term>
<term>Sirtuin 1</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glutarédoxines</term>
<term>Glutathion</term>
<term>Sirtuine-1</term>
</keywords>
<keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Néovascularisation physiologique</term>
<term>Transduction du signal</term>
</keywords>
<keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Neovascularization, Physiologic</term>
<term>Signal Transduction</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Animals</term>
<term>Blotting, Western</term>
<term>Gene Knockdown Techniques</term>
<term>HeLa Cells</term>
<term>Humans</term>
<term>Mass Spectrometry</term>
<term>Microscopy, Confocal</term>
<term>Oxidation-Reduction</term>
<term>Real-Time Polymerase Chain Reaction</term>
<term>Time-Lapse Imaging</term>
<term>Zebrafish</term>
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<term>Cellules HeLa</term>
<term>Danio zébré</term>
<term>Humains</term>
<term>Imagerie accélérée</term>
<term>Microscopie confocale</term>
<term>Oxydoréduction</term>
<term>Réaction de polymérisation en chaine en temps réel</term>
<term>Spectrométrie de masse</term>
<term>Technique de Western</term>
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<front><div type="abstract" xml:lang="en">Embryonic development depends on complex and precisely orchestrated signaling pathways including specific reduction/oxidation cascades. Oxidoreductases of the thioredoxin family are key players conveying redox signals through reversible posttranslational modifications of protein thiols. The importance of this protein family during embryogenesis has recently been exemplified for glutaredoxin 2, a vertebrate-specific glutathione-disulfide oxidoreductase with a critical role for embryonic brain development. Here, we discovered an essential function of glutaredoxin 2 during vascular development. Confocal microscopy and time-lapse studies based on two-photon microscopy revealed that morpholino-based knockdown of glutaredoxin 2 in zebrafish, a model organism to study vertebrate embryogenesis, resulted in a delayed and disordered blood vessel network. We were able to show that formation of a functional vascular system requires glutaredoxin 2-dependent reversible S-glutathionylation of the NAD(+)-dependent protein deacetylase sirtuin 1. Using mass spectrometry, we identified a cysteine residue in the conserved catalytic region of sirtuin 1 as target for glutaredoxin 2-specific deglutathionylation. Thereby, glutaredoxin 2-mediated redox regulation controls enzymatic activity of sirtuin 1, a mechanism we found to be conserved between zebrafish and humans. These results link S-glutathionylation to vertebrate development and successful embryonic angiogenesis. </div>
</front>
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<DateCompleted><Year>2014</Year>
<Month>02</Month>
<Day>21</Day>
</DateCompleted>
<DateRevised><Year>2018</Year>
<Month>11</Month>
<Day>13</Day>
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<Title>Proceedings of the National Academy of Sciences of the United States of America</Title>
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<ArticleTitle>Glutaredoxin regulates vascular development by reversible glutathionylation of sirtuin 1.</ArticleTitle>
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<Abstract><AbstractText>Embryonic development depends on complex and precisely orchestrated signaling pathways including specific reduction/oxidation cascades. Oxidoreductases of the thioredoxin family are key players conveying redox signals through reversible posttranslational modifications of protein thiols. The importance of this protein family during embryogenesis has recently been exemplified for glutaredoxin 2, a vertebrate-specific glutathione-disulfide oxidoreductase with a critical role for embryonic brain development. Here, we discovered an essential function of glutaredoxin 2 during vascular development. Confocal microscopy and time-lapse studies based on two-photon microscopy revealed that morpholino-based knockdown of glutaredoxin 2 in zebrafish, a model organism to study vertebrate embryogenesis, resulted in a delayed and disordered blood vessel network. We were able to show that formation of a functional vascular system requires glutaredoxin 2-dependent reversible S-glutathionylation of the NAD(+)-dependent protein deacetylase sirtuin 1. Using mass spectrometry, we identified a cysteine residue in the conserved catalytic region of sirtuin 1 as target for glutaredoxin 2-specific deglutathionylation. Thereby, glutaredoxin 2-mediated redox regulation controls enzymatic activity of sirtuin 1, a mechanism we found to be conserved between zebrafish and humans. These results link S-glutathionylation to vertebrate development and successful embryonic angiogenesis. </AbstractText>
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<ForeName>Gereon</ForeName>
<Initials>G</Initials>
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<ForeName>Staffan</ForeName>
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<ForeName>Sarah</ForeName>
<Initials>S</Initials>
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<ForeName>Kristian</ForeName>
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<ForeName>Timour</ForeName>
<Initials>T</Initials>
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<Author ValidYN="Y"><LastName>Montano</LastName>
<ForeName>Sergio J</ForeName>
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<Author ValidYN="Y"><LastName>Aktas</LastName>
<ForeName>Orhan</ForeName>
<Initials>O</Initials>
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<Author ValidYN="Y"><LastName>Uhlén</LastName>
<ForeName>Per</ForeName>
<Initials>P</Initials>
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<Author ValidYN="Y"><LastName>Stühler</LastName>
<ForeName>Kai</ForeName>
<Initials>K</Initials>
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<Author ValidYN="Y"><LastName>Cao</LastName>
<ForeName>Yihai</ForeName>
<Initials>Y</Initials>
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<Author ValidYN="Y"><LastName>Holmgren</LastName>
<ForeName>Arne</ForeName>
<Initials>A</Initials>
</Author>
<Author ValidYN="Y"><LastName>Berndt</LastName>
<ForeName>Carsten</ForeName>
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Serveur d'exploration sur la glutarédoxine

Glutaredoxin regulates vascular development by reversible glutathionylation of sirtuin 1.

Glutaredoxin regulates vascular development by reversible glutathionylation of sirtuin 1.

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