GlutaredoxinV1, Main, Exploration, bibRecord, 000112

The glutathione system and the related thiol network in Caenorhabditis elegans.

Identifieur interne : 000112 ( Main/Exploration ); précédent : 000111; suivant : 000113

The glutathione system and the related thiol network in Caenorhabditis elegans.

Auteurs : Gavin Douglas Ferguson [Australie] ; Wallace John Bridge [Australie]

Source :

Redox biology [ 2213-2317 ] ; 2019.

RBID : pubmed:30901603

Descripteurs français

KwdFr :
- Animaux (MeSH), Caenorhabditis elegans (métabolisme), Glutarédoxines (métabolisme), Glutathion (métabolisme), Glutathione peroxidase (métabolisme), Oxydoréduction (MeSH), Stress oxydatif (MeSH), Thiols (métabolisme), Transduction du signal (MeSH), Voies et réseaux métaboliques (MeSH).
MESH :
- métabolisme : Caenorhabditis elegans, Glutarédoxines, Glutathion, Glutathione peroxidase, Thiols.
- Animaux, Oxydoréduction, Stress oxydatif, Transduction du signal, Voies et réseaux métaboliques.

English descriptors

KwdEn :
- Animals (MeSH), Caenorhabditis elegans (metabolism), Glutaredoxins (metabolism), Glutathione (metabolism), Glutathione Peroxidase (metabolism), Metabolic Networks and Pathways (MeSH), Oxidation-Reduction (MeSH), Oxidative Stress (MeSH), Signal Transduction (MeSH), Sulfhydryl Compounds (metabolism).
MESH :
- chemical , metabolism : Glutaredoxins, Glutathione, Glutathione Peroxidase, Sulfhydryl Compounds.
- metabolism : Caenorhabditis elegans.
- Animals, Metabolic Networks and Pathways, Oxidation-Reduction, Oxidative Stress, Signal Transduction.

Abstract

Advances in the field of redox biology have contributed to the understanding of the complexity of the thiol-based system in mediating signal transduction. The redox environment is the overall spatiotemporal balance of oxidation-reduction systems within the integrated compartments of the cell, tissues and whole organisms. The ratio of the reduced to disulfide glutathione redox couple (GSH:GSSG) is a key indicator of the redox environment and its associated cellular health. The reaction mechanisms of glutathione-dependent and related thiol-based enzymes play a fundamental role in the function of GSH as a redox regulator. Glutathione homeostasis is maintained by the balance of GSH synthesis (de novo and salvage pathways) and its utilization through its detoxification, thiol signalling, and antioxidant defence functions via GSH-dependent enzymes and free radical scavenging. As such, GSH acts in concert with the entire redox network to maintain reducing conditions in the cell. Caenorhabditis elegans offers a simple model to facilitate further understanding at the multicellular level of the physiological functions of GSH and the GSH-dependent redox network. This review discusses the C. elegans studies that have investigated glutathione and related systems of the redox network including; orthologs to the protein-encoding genes of GSH synthesis; glutathione peroxidases; glutathione-S-transferases; and the glutaredoxin, thioredoxin and peroxiredoxin systems.

DOI: 10.1016/j.redox.2019.101171
PubMed: 30901603
PubMed Central: PMC6429583

Affiliations:

Australie

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

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Le document en format XML

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<term>Glutathione (metabolism)</term>
<term>Glutathione Peroxidase (metabolism)</term>
<term>Metabolic Networks and Pathways (MeSH)</term>
<term>Oxidation-Reduction (MeSH)</term>
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<term>Glutarédoxines (métabolisme)</term>
<term>Glutathion (métabolisme)</term>
<term>Glutathione peroxidase (métabolisme)</term>
<term>Oxydoréduction (MeSH)</term>
<term>Stress oxydatif (MeSH)</term>
<term>Thiols (métabolisme)</term>
<term>Transduction du signal (MeSH)</term>
<term>Voies et réseaux métaboliques (MeSH)</term>
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<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glutaredoxins</term>
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<term>Glutathione Peroxidase</term>
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<term>Signal Transduction</term>
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<term>Oxydoréduction</term>
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<front><div type="abstract" xml:lang="en">Advances in the field of redox biology have contributed to the understanding of the complexity of the thiol-based system in mediating signal transduction. The redox environment is the overall spatiotemporal balance of oxidation-reduction systems within the integrated compartments of the cell, tissues and whole organisms. The ratio of the reduced to disulfide glutathione redox couple (GSH:GSSG) is a key indicator of the redox environment and its associated cellular health. The reaction mechanisms of glutathione-dependent and related thiol-based enzymes play a fundamental role in the function of GSH as a redox regulator. Glutathione homeostasis is maintained by the balance of GSH synthesis (de novo and salvage pathways) and its utilization through its detoxification, thiol signalling, and antioxidant defence functions via GSH-dependent enzymes and free radical scavenging. As such, GSH acts in concert with the entire redox network to maintain reducing conditions in the cell. Caenorhabditis elegans offers a simple model to facilitate further understanding at the multicellular level of the physiological functions of GSH and the GSH-dependent redox network. This review discusses the C. elegans studies that have investigated glutathione and related systems of the redox network including; orthologs to the protein-encoding genes of GSH synthesis; glutathione peroxidases; glutathione-S-transferases; and the glutaredoxin, thioredoxin and peroxiredoxin systems.</div>
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The glutathione system and the related thiol network in Caenorhabditis elegans.

The glutathione system and the related thiol network in Caenorhabditis elegans.

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