GlutaredoxinV1, Main, Exploration, bibRecord, 000843

Mitochondrial thiols in the regulation of cell death pathways.

Identifieur interne : 000843 ( Main/Exploration ); précédent : 000842; suivant : 000844

Mitochondrial thiols in the regulation of cell death pathways.

Auteurs : Fei Yin [États-Unis] ; Harsh Sancheti ; Enrique Cadenas

Source :

Antioxidants & redox signaling [ 1557-7716 ] ; 2012.

RBID : pubmed:22530585

Descripteurs français

KwdFr :
- Animaux (MeSH), Glutathione peroxidase (métabolisme), Humains (MeSH), Methionine Sulfoxide Reductases (métabolisme), Mitochondries (métabolisme), Mort cellulaire (génétique), Mort cellulaire (physiologie), Oxydoréduction (MeSH), Peroxirédoxines (métabolisme), Stress oxydatif (génétique), Stress oxydatif (physiologie), Thiols (métabolisme), Transduction du signal (génétique), Transduction du signal (physiologie).
MESH :
- génétique : Mort cellulaire, Stress oxydatif, Transduction du signal.
- métabolisme : Glutathione peroxidase, Methionine Sulfoxide Reductases, Mitochondries, Peroxirédoxines, Thiols.
- physiologie : Mort cellulaire, Stress oxydatif, Transduction du signal.
- Animaux, Humains, Oxydoréduction.

English descriptors

KwdEn :
- Animals (MeSH), Cell Death (genetics), Cell Death (physiology), Glutathione Peroxidase (metabolism), Humans (MeSH), Methionine Sulfoxide Reductases (metabolism), Mitochondria (metabolism), Oxidation-Reduction (MeSH), Oxidative Stress (genetics), Oxidative Stress (physiology), Peroxiredoxins (metabolism), Signal Transduction (genetics), Signal Transduction (physiology), Sulfhydryl Compounds (metabolism).
MESH :
- chemical , metabolism : Glutathione Peroxidase, Methionine Sulfoxide Reductases, Peroxiredoxins, Sulfhydryl Compounds.
- genetics : Cell Death, Oxidative Stress, Signal Transduction.
- metabolism : Mitochondria.
- physiology : Cell Death, Oxidative Stress, Signal Transduction.
- Animals, Humans, Oxidation-Reduction.

Abstract

SIGNIFICANCE

Regulation of mitochondrial H(2)O(2) homeostasis and its involvement in the regulation of redox-sensitive signaling and transcriptional pathways is the consequence of the concerted activities of the mitochondrial energy- and redox systems.

RECENT ADVANCES

The energy component of this mitochondrial energy-redox axis entails the formation of reducing equivalents and their flow through the respiratory chain with the consequent electron leak to generate [Formula: see text] and H(2)O(2). The mitochondrial redox component entails the thiol-based antioxidant system, largely accounted for by glutathione- and thioredoxin-based systems that support the activities of glutathione peroxidases, peroxiredoxins, and methionine sulfoxide reductase. The ultimate reductant for these systems is NADPH: mitochondrial sources of NADPH are the nicotinamide nucleotide transhydrogenase, isocitrate dehydrogenase-2, and malic enzyme. NADPH also supports the glutaredoxin activity that regulates the extent of S-glutathionylation of mitochondrial proteins in response to altered redox status.

CRITICAL ISSUES

The integrated network of these mitochondrial thiols constitute a regulatory device involved in the maintenance of steady-state levels of H(2)O(2), mitochondrial and cellular redox and metabolic homeostasis, as well as the modulation of cytosolic redox-sensitive signaling; disturbances of this regulatory device affects transcription, growth, and ultimately influences cell survival/death.

FUTURE DIRECTIONS

The modulation of key mitochondrial thiol proteins, which participate in redox signaling, maintenance of the bioenergetic machinery, oxidative stress responses, and cell death programming, provides a pivotal direction in developing new therapies towards the prevention and treatment of several diseases.

DOI: 10.1089/ars.2012.4639
PubMed: 22530585
PubMed Central: PMC3474184

Affiliations:

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

to stream Main, to step Corpus: 000846
to stream Main, to step Curation: 000846

Le document en format XML

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<front><div type="abstract" xml:lang="en"><p><b>SIGNIFICANCE</b>
</p>
<p>Regulation of mitochondrial H(2)O(2) homeostasis and its involvement in the regulation of redox-sensitive signaling and transcriptional pathways is the consequence of the concerted activities of the mitochondrial energy- and redox systems.</p>
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<div type="abstract" xml:lang="en"><p><b>RECENT ADVANCES</b>
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<p>The energy component of this mitochondrial energy-redox axis entails the formation of reducing equivalents and their flow through the respiratory chain with the consequent electron leak to generate [Formula: see text] and H(2)O(2). The mitochondrial redox component entails the thiol-based antioxidant system, largely accounted for by glutathione- and thioredoxin-based systems that support the activities of glutathione peroxidases, peroxiredoxins, and methionine sulfoxide reductase. The ultimate reductant for these systems is NADPH: mitochondrial sources of NADPH are the nicotinamide nucleotide transhydrogenase, isocitrate dehydrogenase-2, and malic enzyme. NADPH also supports the glutaredoxin activity that regulates the extent of S-glutathionylation of mitochondrial proteins in response to altered redox status.</p>
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<div type="abstract" xml:lang="en"><p><b>CRITICAL ISSUES</b>
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<p>The integrated network of these mitochondrial thiols constitute a regulatory device involved in the maintenance of steady-state levels of H(2)O(2), mitochondrial and cellular redox and metabolic homeostasis, as well as the modulation of cytosolic redox-sensitive signaling; disturbances of this regulatory device affects transcription, growth, and ultimately influences cell survival/death.</p>
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<div type="abstract" xml:lang="en"><p><b>FUTURE DIRECTIONS</b>
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<p>The modulation of key mitochondrial thiol proteins, which participate in redox signaling, maintenance of the bioenergetic machinery, oxidative stress responses, and cell death programming, provides a pivotal direction in developing new therapies towards the prevention and treatment of several diseases.</p>
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Mitochondrial thiols in the regulation of cell death pathways.

Mitochondrial thiols in the regulation of cell death pathways.

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