GlutaredoxinV1, Main, Exploration, bibRecord, 000448

Induction of mitochondrial reactive oxygen species production by GSH mediated S-glutathionylation of 2-oxoglutarate dehydrogenase.

Identifieur interne : 000448 ( Main/Exploration ); précédent : 000447; suivant : 000449

Induction of mitochondrial reactive oxygen species production by GSH mediated S-glutathionylation of 2-oxoglutarate dehydrogenase.

Auteurs : Ryan J. Mailloux [Canada] ; D. Craig Ayre [Canada] ; Sherri L. Christian [Canada]

Source :

Redox biology [ 2213-2317 ] ; 2016.

RBID : pubmed:26928132

Descripteurs français

English descriptors

KwdEn :
- Animals (MeSH), Glutaredoxins (metabolism), Glutathione (metabolism), Glutathione Disulfide (metabolism), Hydrogen Peroxide (metabolism), Ketoglutarate Dehydrogenase Complex (metabolism), Mice (MeSH), Mitochondria, Liver (metabolism), NAD (metabolism), Oxidation-Reduction (MeSH), Reactive Oxygen Species (metabolism).
MESH :
- chemical , metabolism : Glutaredoxins, Glutathione, Glutathione Disulfide, Hydrogen Peroxide, Ketoglutarate Dehydrogenase Complex, NAD, Reactive Oxygen Species.
- metabolism : Mitochondria, Liver.
- Animals, Mice, Oxidation-Reduction.

Abstract

2-Oxoglutarate dehydrogenase (Ogdh) is an important mitochondria redox sensor that can undergo S-glutathionylation following an increase in H2O2 levels. Although S-glutathionylation is required to protect Ogdh from irreversible oxidation while simultaneously modulating its activity it remains unknown if glutathione can also modulate reactive oxygen species (ROS) production by the complex. We report that reduced (GSH) and oxidized (GSSG) glutathione control O2(∙-)/H2O2 formation by Ogdh through protein S-glutathionylation reactions. GSSG (1mM) induced a modest decrease in Ogdh activity which was associated with a significant decrease in O2(∙-)/H2O2 formation. GSH had the opposite effect, amplifying O2(∙-)/H2O2 formation by Ogdh. Incubation of purified Ogdh in 2.5mM GSH led to significant increase in O2(∙-)/H2O2 formation which also lowered NADH production. Inclusion of enzymatically active glutaredoxin-2 (Grx2) in reaction mixtures reversed the GSH-mediated amplification of O2(∙-)/H2O2 formation. Similarly pre-incubation of permeabilized liver mitochondria from mouse depleted of GSH showed an approximately ~3.5-fold increase in Ogdh-mediated O2(∙-)/H2O2 production that was matched by a significant decrease in NADH formation which could be reversed by Grx2. Taken together, our results demonstrate GSH and GSSG modulate ROS production by Ogdh through S-glutathionylation of different subunits. This is also the first demonstration that GSH can work in the opposite direction in mitochondria-amplifying ROS formation instead of quenching it. We propose that this regulatory mechanism is required to modulate ROS emission from Ogdh in response to variations in glutathione redox buffering capacity.

DOI: 10.1016/j.redox.2016.02.002
PubMed: 26928132
PubMed Central: PMC4776629

Affiliations:

Canada

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

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Le document en format XML

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<term>Glutaredoxins (metabolism)</term>
<term>Glutathione (metabolism)</term>
<term>Glutathione Disulfide (metabolism)</term>
<term>Hydrogen Peroxide (metabolism)</term>
<term>Ketoglutarate Dehydrogenase Complex (metabolism)</term>
<term>Mice (MeSH)</term>
<term>Mitochondria, Liver (metabolism)</term>
<term>NAD (metabolism)</term>
<term>Oxidation-Reduction (MeSH)</term>
<term>Reactive Oxygen Species (metabolism)</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term>
<term>Disulfure de glutathion (métabolisme)</term>
<term>Espèces réactives de l'oxygène (métabolisme)</term>
<term>Glutarédoxines (métabolisme)</term>
<term>Glutathion (métabolisme)</term>
<term>Ketoglutarate dehydrogenase complex (métabolisme)</term>
<term>Mitochondries du foie (métabolisme)</term>
<term>NAD (métabolisme)</term>
<term>Oxydoréduction (MeSH)</term>
<term>Peroxyde d'hydrogène (métabolisme)</term>
<term>Souris (MeSH)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glutaredoxins</term>
<term>Glutathione</term>
<term>Glutathione Disulfide</term>
<term>Hydrogen Peroxide</term>
<term>Ketoglutarate Dehydrogenase Complex</term>
<term>NAD</term>
<term>Reactive Oxygen Species</term>
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<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Mitochondria, Liver</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Disulfure de glutathion</term>
<term>Espèces réactives de l'oxygène</term>
<term>Glutarédoxines</term>
<term>Glutathion</term>
<term>Ketoglutarate dehydrogenase complex</term>
<term>Mitochondries du foie</term>
<term>NAD</term>
<term>Peroxyde d'hydrogène</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Animals</term>
<term>Mice</term>
<term>Oxidation-Reduction</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Animaux</term>
<term>Oxydoréduction</term>
<term>Souris</term>
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<front><div type="abstract" xml:lang="en">2-Oxoglutarate dehydrogenase (Ogdh) is an important mitochondria redox sensor that can undergo S-glutathionylation following an increase in H2O2 levels. Although S-glutathionylation is required to protect Ogdh from irreversible oxidation while simultaneously modulating its activity it remains unknown if glutathione can also modulate reactive oxygen species (ROS) production by the complex. We report that reduced (GSH) and oxidized (GSSG) glutathione control O2(∙-)/H2O2 formation by Ogdh through protein S-glutathionylation reactions. GSSG (1mM) induced a modest decrease in Ogdh activity which was associated with a significant decrease in O2(∙-)/H2O2 formation. GSH had the opposite effect, amplifying O2(∙-)/H2O2 formation by Ogdh. Incubation of purified Ogdh in 2.5mM GSH led to significant increase in O2(∙-)/H2O2 formation which also lowered NADH production. Inclusion of enzymatically active glutaredoxin-2 (Grx2) in reaction mixtures reversed the GSH-mediated amplification of O2(∙-)/H2O2 formation. Similarly pre-incubation of permeabilized liver mitochondria from mouse depleted of GSH showed an approximately ~3.5-fold increase in Ogdh-mediated O2(∙-)/H2O2 production that was matched by a significant decrease in NADH formation which could be reversed by Grx2. Taken together, our results demonstrate GSH and GSSG modulate ROS production by Ogdh through S-glutathionylation of different subunits. This is also the first demonstration that GSH can work in the opposite direction in mitochondria-amplifying ROS formation instead of quenching it. We propose that this regulatory mechanism is required to modulate ROS emission from Ogdh in response to variations in glutathione redox buffering capacity.</div>
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<Abstract><AbstractText>2-Oxoglutarate dehydrogenase (Ogdh) is an important mitochondria redox sensor that can undergo S-glutathionylation following an increase in H2O2 levels. Although S-glutathionylation is required to protect Ogdh from irreversible oxidation while simultaneously modulating its activity it remains unknown if glutathione can also modulate reactive oxygen species (ROS) production by the complex. We report that reduced (GSH) and oxidized (GSSG) glutathione control O2(∙-)/H2O2 formation by Ogdh through protein S-glutathionylation reactions. GSSG (1mM) induced a modest decrease in Ogdh activity which was associated with a significant decrease in O2(∙-)/H2O2 formation. GSH had the opposite effect, amplifying O2(∙-)/H2O2 formation by Ogdh. Incubation of purified Ogdh in 2.5mM GSH led to significant increase in O2(∙-)/H2O2 formation which also lowered NADH production. Inclusion of enzymatically active glutaredoxin-2 (Grx2) in reaction mixtures reversed the GSH-mediated amplification of O2(∙-)/H2O2 formation. Similarly pre-incubation of permeabilized liver mitochondria from mouse depleted of GSH showed an approximately ~3.5-fold increase in Ogdh-mediated O2(∙-)/H2O2 production that was matched by a significant decrease in NADH formation which could be reversed by Grx2. Taken together, our results demonstrate GSH and GSSG modulate ROS production by Ogdh through S-glutathionylation of different subunits. This is also the first demonstration that GSH can work in the opposite direction in mitochondria-amplifying ROS formation instead of quenching it. We propose that this regulatory mechanism is required to modulate ROS emission from Ogdh in response to variations in glutathione redox buffering capacity.</AbstractText>
<CopyrightInformation>Copyright © 2016 The Authors. Published by Elsevier B.V. All rights reserved.</CopyrightInformation>
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<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
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Induction of mitochondrial reactive oxygen species production by GSH mediated S-glutathionylation of 2-oxoglutarate dehydrogenase.

Induction of mitochondrial reactive oxygen species production by GSH mediated S-glutathionylation of 2-oxoglutarate dehydrogenase.

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