GlutaredoxinV1, Main, Exploration, bibRecord, 000698

Thioredoxin 1 is inactivated due to oxidation induced by peroxiredoxin under oxidative stress and reactivated by the glutaredoxin system.

Identifieur interne : 000698 ( Main/Exploration ); précédent : 000697; suivant : 000699

Thioredoxin 1 is inactivated due to oxidation induced by peroxiredoxin under oxidative stress and reactivated by the glutaredoxin system.

Auteurs : Yatao Du [Suède] ; Huihui Zhang ; Xu Zhang ; Jun Lu ; Arne Holmgren

Source :

The Journal of biological chemistry [ 1083-351X ] ; 2013.

RBID : pubmed:24062305

Descripteurs français

KwdFr :
- Cellules HeLa (MeSH), Glutarédoxines (génétique), Glutarédoxines (métabolisme), Glutathion (génétique), Glutathion (métabolisme), Glutathione reductase (génétique), Glutathione reductase (métabolisme), Humains (MeSH), NADP (génétique), NADP (métabolisme), Oxydants (pharmacologie), Oxydoréduction (effets des médicaments et des substances chimiques), Peroxirédoxines (génétique), Peroxirédoxines (métabolisme), Peroxyde d'hydrogène (pharmacologie), Stress oxydatif (effets des médicaments et des substances chimiques), Stress oxydatif (physiologie), Thiorédoxines (génétique), Thiorédoxines (métabolisme), Transduction du signal (effets des médicaments et des substances chimiques), Transduction du signal (physiologie).
MESH :
- effets des médicaments et des substances chimiques : Oxydoréduction, Stress oxydatif, Transduction du signal.
- génétique : Glutarédoxines, Glutathion, Glutathione reductase, NADP, Peroxirédoxines, Thiorédoxines.
- métabolisme : Glutarédoxines, Glutathion, Glutathione reductase, NADP, Peroxirédoxines, Thiorédoxines.
- pharmacologie : Oxydants, Peroxyde d'hydrogène.
- physiologie : Stress oxydatif, Transduction du signal.
- Cellules HeLa, Humains.

English descriptors

KwdEn :
- Glutaredoxins (genetics), Glutaredoxins (metabolism), Glutathione (genetics), Glutathione (metabolism), Glutathione Reductase (genetics), Glutathione Reductase (metabolism), HeLa Cells (MeSH), Humans (MeSH), Hydrogen Peroxide (pharmacology), NADP (genetics), NADP (metabolism), Oxidants (pharmacology), Oxidation-Reduction (drug effects), Oxidative Stress (drug effects), Oxidative Stress (physiology), Peroxiredoxins (genetics), Peroxiredoxins (metabolism), Signal Transduction (drug effects), Signal Transduction (physiology), Thioredoxins (genetics), Thioredoxins (metabolism).
MESH :
- chemical , genetics : Glutaredoxins, Glutathione, Glutathione Reductase, NADP, Peroxiredoxins, Thioredoxins.
- chemical , metabolism : Glutaredoxins, Glutathione, Glutathione Reductase, NADP, Peroxiredoxins, Thioredoxins.
- chemical , pharmacology : Hydrogen Peroxide, Oxidants.
- drug effects : Oxidation-Reduction, Oxidative Stress, Signal Transduction.
- physiology : Oxidative Stress, Signal Transduction.
- HeLa Cells, Humans.

Abstract

The mammalian cytosolic thioredoxin system, comprising thioredoxin (Trx), Trx reductase, and NADPH, is the major protein-disulfide reductase of the cell and has numerous functions. Besides the active site thiols, human Trx1 contains three non-active site cysteine residues at positions 62, 69, and 73. A two-disulfide form of Trx1, containing an active site disulfide between Cys-32 and Cys-35 and a non-active site disulfide between Cys-62 and Cys-69, is inactive either as a disulfide reductase or as a substrate for Trx reductase. This could possibly provide a structural switch affecting Trx1 function during oxidative stress and redox signaling. We found that two-disulfide Trx1 was generated in A549 cells under oxidative stress. In vitro data showed that two-disulfide Trx1 was generated from oxidation of Trx1 catalyzed by peroxiredoxin 1 in the presence of H2O2. The redox Western blot data indicated that the glutaredoxin system protected Trx1 in HeLa cells from oxidation caused by ebselen, a superfast oxidant for Trx1. Our results also showed that physiological concentrations of glutathione, NADPH, and glutathione reductase reduced the non-active site disulfide in vitro. This reaction was stimulated by glutaredoxin 1 via the so-called monothiol mechanism. In conclusion, reversible oxidation of the non-active site disulfide of Trx1 is suggested to play an important role in redox regulation and cell signaling via temporal inhibition of its protein-disulfide reductase activity for the transmission of oxidative signals under oxidative stress.

DOI: 10.1074/jbc.M113.495150
PubMed: 24062305
PubMed Central: PMC3820862

Affiliations:

Suède

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

to stream Main, to step Corpus: 000702
to stream Main, to step Curation: 000702

Le document en format XML

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<term>Glutathione (metabolism)</term>
<term>Glutathione Reductase (genetics)</term>
<term>Glutathione Reductase (metabolism)</term>
<term>HeLa Cells (MeSH)</term>
<term>Humans (MeSH)</term>
<term>Hydrogen Peroxide (pharmacology)</term>
<term>NADP (genetics)</term>
<term>NADP (metabolism)</term>
<term>Oxidants (pharmacology)</term>
<term>Oxidation-Reduction (drug effects)</term>
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<term>Oxidative Stress (physiology)</term>
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<term>Peroxiredoxins (metabolism)</term>
<term>Signal Transduction (drug effects)</term>
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<term>Thioredoxins (metabolism)</term>
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<term>Glutathion (génétique)</term>
<term>Glutathion (métabolisme)</term>
<term>Glutathione reductase (génétique)</term>
<term>Glutathione reductase (métabolisme)</term>
<term>Humains (MeSH)</term>
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<term>Oxydants (pharmacologie)</term>
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<term>Stress oxydatif (physiologie)</term>
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<term>Thiorédoxines (métabolisme)</term>
<term>Transduction du signal (effets des médicaments et des substances chimiques)</term>
<term>Transduction du signal (physiologie)</term>
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<term>Glutathione</term>
<term>Glutathione Reductase</term>
<term>NADP</term>
<term>Peroxiredoxins</term>
<term>Thioredoxins</term>
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<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glutaredoxins</term>
<term>Glutathione</term>
<term>Glutathione Reductase</term>
<term>NADP</term>
<term>Peroxiredoxins</term>
<term>Thioredoxins</term>
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<keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Hydrogen Peroxide</term>
<term>Oxidants</term>
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<keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Oxidation-Reduction</term>
<term>Oxidative Stress</term>
<term>Signal Transduction</term>
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<keywords scheme="MESH" qualifier="effets des médicaments et des substances chimiques" xml:lang="fr"><term>Oxydoréduction</term>
<term>Stress oxydatif</term>
<term>Transduction du signal</term>
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<term>Glutathion</term>
<term>Glutathione reductase</term>
<term>NADP</term>
<term>Peroxirédoxines</term>
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<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glutarédoxines</term>
<term>Glutathion</term>
<term>Glutathione reductase</term>
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<term>Peroxirédoxines</term>
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<term>Peroxyde d'hydrogène</term>
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<term>Humans</term>
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<front><div type="abstract" xml:lang="en">The mammalian cytosolic thioredoxin system, comprising thioredoxin (Trx), Trx reductase, and NADPH, is the major protein-disulfide reductase of the cell and has numerous functions. Besides the active site thiols, human Trx1 contains three non-active site cysteine residues at positions 62, 69, and 73. A two-disulfide form of Trx1, containing an active site disulfide between Cys-32 and Cys-35 and a non-active site disulfide between Cys-62 and Cys-69, is inactive either as a disulfide reductase or as a substrate for Trx reductase. This could possibly provide a structural switch affecting Trx1 function during oxidative stress and redox signaling. We found that two-disulfide Trx1 was generated in A549 cells under oxidative stress. In vitro data showed that two-disulfide Trx1 was generated from oxidation of Trx1 catalyzed by peroxiredoxin 1 in the presence of H2O2. The redox Western blot data indicated that the glutaredoxin system protected Trx1 in HeLa cells from oxidation caused by ebselen, a superfast oxidant for Trx1. Our results also showed that physiological concentrations of glutathione, NADPH, and glutathione reductase reduced the non-active site disulfide in vitro. This reaction was stimulated by glutaredoxin 1 via the so-called monothiol mechanism. In conclusion, reversible oxidation of the non-active site disulfide of Trx1 is suggested to play an important role in redox regulation and cell signaling via temporal inhibition of its protein-disulfide reductase activity for the transmission of oxidative signals under oxidative stress. </div>
</front>
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<Abstract><AbstractText>The mammalian cytosolic thioredoxin system, comprising thioredoxin (Trx), Trx reductase, and NADPH, is the major protein-disulfide reductase of the cell and has numerous functions. Besides the active site thiols, human Trx1 contains three non-active site cysteine residues at positions 62, 69, and 73. A two-disulfide form of Trx1, containing an active site disulfide between Cys-32 and Cys-35 and a non-active site disulfide between Cys-62 and Cys-69, is inactive either as a disulfide reductase or as a substrate for Trx reductase. This could possibly provide a structural switch affecting Trx1 function during oxidative stress and redox signaling. We found that two-disulfide Trx1 was generated in A549 cells under oxidative stress. In vitro data showed that two-disulfide Trx1 was generated from oxidation of Trx1 catalyzed by peroxiredoxin 1 in the presence of H2O2. The redox Western blot data indicated that the glutaredoxin system protected Trx1 in HeLa cells from oxidation caused by ebselen, a superfast oxidant for Trx1. Our results also showed that physiological concentrations of glutathione, NADPH, and glutathione reductase reduced the non-active site disulfide in vitro. This reaction was stimulated by glutaredoxin 1 via the so-called monothiol mechanism. In conclusion, reversible oxidation of the non-active site disulfide of Trx1 is suggested to play an important role in redox regulation and cell signaling via temporal inhibition of its protein-disulfide reductase activity for the transmission of oxidative signals under oxidative stress. </AbstractText>
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Thioredoxin 1 is inactivated due to oxidation induced by peroxiredoxin under oxidative stress and reactivated by the glutaredoxin system.

Thioredoxin 1 is inactivated due to oxidation induced by peroxiredoxin under oxidative stress and reactivated by the glutaredoxin system.

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