GlutaredoxinV1, Main, Exploration, bibRecord, 000495

Thiol-based antioxidants elicit mitochondrial oxidation via respiratory complex III.

Identifieur interne : 000495 ( Main/Exploration ); précédent : 000494; suivant : 000496

Thiol-based antioxidants elicit mitochondrial oxidation via respiratory complex III.

Auteurs : Vladimir L. Kolossov ; Jessica N. Beaudoin ; Nagendraprabhu Ponnuraj ; Stephen J. Diliberto ; William P. Hanafin ; Paul J A. Kenis ; H Rex Gaskins

Source :

American journal of physiology. Cell physiology [ 1522-1563 ] ; 2015.

RBID : pubmed:25994788

Descripteurs français

KwdFr :
- Animaux (MeSH), Antioxydants (pharmacologie), Cellules CHO (MeSH), Cellules HCT116 (MeSH), Cellules HEK293 (MeSH), Complexe III de la chaîne respiratoire (antagonistes et inhibiteurs), Complexe III de la chaîne respiratoire (métabolisme), Cricetulus (MeSH), Espèces réactives de l'oxygène (métabolisme), Facteurs temps (MeSH), Glutarédoxines (génétique), Glutarédoxines (métabolisme), Glutathion (métabolisme), Humains (MeSH), Mitochondries (effets des médicaments et des substances chimiques), Mitochondries (métabolisme), Oxydoréduction (MeSH), Potentiel de membrane mitochondriale (effets des médicaments et des substances chimiques), Stress oxydatif (effets des médicaments et des substances chimiques), Suidae (MeSH), Techniques de biocapteur (MeSH), Thiols (pharmacologie), Transfection (MeSH).
MESH :
- antagonistes et inhibiteurs : Complexe III de la chaîne respiratoire.
- effets des médicaments et des substances chimiques : Mitochondries, Potentiel de membrane mitochondriale, Stress oxydatif.
- génétique : Glutarédoxines.
- métabolisme : Complexe III de la chaîne respiratoire, Espèces réactives de l'oxygène, Glutarédoxines, Glutathion, Mitochondries.
- pharmacologie : Antioxydants, Thiols.
- Animaux, Cellules CHO, Cellules HCT116, Cellules HEK293, Cricetulus, Facteurs temps, Humains, Oxydoréduction, Suidae, Techniques de biocapteur, Transfection.

English descriptors

KwdEn :
- Animals (MeSH), Antioxidants (pharmacology), Biosensing Techniques (MeSH), CHO Cells (MeSH), Cricetulus (MeSH), Electron Transport Complex III (antagonists & inhibitors), Electron Transport Complex III (metabolism), Glutaredoxins (genetics), Glutaredoxins (metabolism), Glutathione (metabolism), HCT116 Cells (MeSH), HEK293 Cells (MeSH), Humans (MeSH), Membrane Potential, Mitochondrial (drug effects), Mitochondria (drug effects), Mitochondria (metabolism), Oxidation-Reduction (MeSH), Oxidative Stress (drug effects), Reactive Oxygen Species (metabolism), Sulfhydryl Compounds (pharmacology), Swine (MeSH), Time Factors (MeSH), Transfection (MeSH).
MESH :
- chemical , antagonists & inhibitors : Electron Transport Complex III.
- chemical , genetics : Glutaredoxins.
- chemical , metabolism : Electron Transport Complex III, Glutaredoxins, Glutathione, Reactive Oxygen Species.
- chemical , pharmacology : Antioxidants, Sulfhydryl Compounds.
- drug effects : Membrane Potential, Mitochondrial, Mitochondria, Oxidative Stress.
- metabolism : Mitochondria.
- Animals, Biosensing Techniques, CHO Cells, Cricetulus, HCT116 Cells, HEK293 Cells, Humans, Oxidation-Reduction, Swine, Time Factors, Transfection.

Abstract

Excessive oxidation is widely accepted as a precursor to deleterious cellular function. On the other hand, an awareness of the role of reductive stress as a similar pathological insult is emerging. Here we report early dynamic changes in compartmentalized glutathione (GSH) redox potentials in living cells in response to exogenously supplied thiol-based antioxidants. Noninvasive monitoring of intracellular thiol-disulfide exchange via a genetically encoded biosensor targeted to cytosol and mitochondria revealed unexpectedly rapid oxidation of the mitochondrial matrix in response to GSH ethyl ester or N-acetyl-l-cysteine. Oxidation of the probe occurred within seconds in a concentration-dependent manner and was attenuated with the membrane-permeable ROS scavenger tiron. In contrast, the cytosolic sensor did not respond to similar treatments. Surprisingly, the immediate mitochondrial oxidation was not abrogated by depolarization of mitochondrial membrane potential or inhibition of mitochondrial GSH uptake. After detection of elevated levels of mitochondrial ROS, we systematically inhibited multisubunit protein complexes of the mitochondrial respiratory chain and determined that respiratory complex III is a downstream target of thiol-based compounds. Disabling complex III with myxothiazol completely blocked matrix oxidation induced with GSH ethyl ester or N-acetyl-l-cysteine. Our findings provide new evidence of a functional link between exogenous thiol-containing antioxidants and mitochondrial respiration.

DOI: 10.1152/ajpcell.00006.2015
PubMed: 25994788
PubMed Central: PMC4504939

Affiliations:

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

to stream Main, to step Corpus: 000527
to stream Main, to step Curation: 000527

Le document en format XML

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<term>CHO Cells (MeSH)</term>
<term>Cricetulus (MeSH)</term>
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<term>Electron Transport Complex III (metabolism)</term>
<term>Glutaredoxins (genetics)</term>
<term>Glutaredoxins (metabolism)</term>
<term>Glutathione (metabolism)</term>
<term>HCT116 Cells (MeSH)</term>
<term>HEK293 Cells (MeSH)</term>
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<term>Mitochondria (drug effects)</term>
<term>Mitochondria (metabolism)</term>
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<term>Oxidative Stress (drug effects)</term>
<term>Reactive Oxygen Species (metabolism)</term>
<term>Sulfhydryl Compounds (pharmacology)</term>
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<term>Cellules HEK293 (MeSH)</term>
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<term>Complexe III de la chaîne respiratoire (métabolisme)</term>
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<term>Thiols (pharmacologie)</term>
<term>Transfection (MeSH)</term>
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<term>Cellules CHO</term>
<term>Cellules HCT116</term>
<term>Cellules HEK293</term>
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<term>Facteurs temps</term>
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<front><div type="abstract" xml:lang="en">Excessive oxidation is widely accepted as a precursor to deleterious cellular function. On the other hand, an awareness of the role of reductive stress as a similar pathological insult is emerging. Here we report early dynamic changes in compartmentalized glutathione (GSH) redox potentials in living cells in response to exogenously supplied thiol-based antioxidants. Noninvasive monitoring of intracellular thiol-disulfide exchange via a genetically encoded biosensor targeted to cytosol and mitochondria revealed unexpectedly rapid oxidation of the mitochondrial matrix in response to GSH ethyl ester or N-acetyl-l-cysteine. Oxidation of the probe occurred within seconds in a concentration-dependent manner and was attenuated with the membrane-permeable ROS scavenger tiron. In contrast, the cytosolic sensor did not respond to similar treatments. Surprisingly, the immediate mitochondrial oxidation was not abrogated by depolarization of mitochondrial membrane potential or inhibition of mitochondrial GSH uptake. After detection of elevated levels of mitochondrial ROS, we systematically inhibited multisubunit protein complexes of the mitochondrial respiratory chain and determined that respiratory complex III is a downstream target of thiol-based compounds. Disabling complex III with myxothiazol completely blocked matrix oxidation induced with GSH ethyl ester or N-acetyl-l-cysteine. Our findings provide new evidence of a functional link between exogenous thiol-containing antioxidants and mitochondrial respiration.</div>
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<name sortKey="Gaskins, H Rex" sort="Gaskins, H Rex" uniqKey="Gaskins H" first="H Rex" last="Gaskins">H Rex Gaskins</name>
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Thiol-based antioxidants elicit mitochondrial oxidation via respiratory complex III.

Thiol-based antioxidants elicit mitochondrial oxidation via respiratory complex III.

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