GlutaredoxinV1, Main, Exploration, bibRecord, 001249

Dehydroascorbate reduction.

Identifieur interne : 001249 ( Main/Exploration ); précédent : 001248; suivant : 001250

Dehydroascorbate reduction.

Auteurs : W W Wells [États-Unis] ; D P Xu

Source :

Journal of bioenergetics and biomembranes [ 0145-479X ] ; 1994.

RBID : pubmed:7844111

Descripteurs français

KwdFr :
- Acide déhydroascorbique (analogues et dérivés), Acide déhydroascorbique (métabolisme), Animaux (MeSH), Animaux nouveau-nés (MeSH), Espèces réactives de l'oxygène (MeSH), Glutarédoxines (MeSH), Glutathion (déficit), Isomerases (physiologie), Mammifères (métabolisme), NADH, NADPH oxidoreductases (métabolisme), Oxidoreductases (métabolisme), Oxidoreductases (physiologie), Oxydoréduction (MeSH), Protein Disulfide-Isomerases (MeSH), Protein-disulfide reductase (glutathione) (MeSH), Protéines végétales (métabolisme).
MESH :
- analogues et dérivés : Acide déhydroascorbique.
- déficit : Glutathion.
- métabolisme : Acide déhydroascorbique, Mammifères, NADH, NADPH oxidoreductases, Oxidoreductases, Protéines végétales.
- physiologie : Isomerases, Oxidoreductases.
- Animaux, Animaux nouveau-nés, Espèces réactives de l'oxygène, Glutarédoxines, Oxydoréduction, Protein Disulfide-Isomerases, Protein-disulfide reductase (glutathione).

English descriptors

KwdEn :
- Animals (MeSH), Animals, Newborn (MeSH), Dehydroascorbic Acid (analogs & derivatives), Dehydroascorbic Acid (metabolism), Glutaredoxins (MeSH), Glutathione (deficiency), Isomerases (physiology), Mammals (metabolism), NADH, NADPH Oxidoreductases (metabolism), Oxidation-Reduction (MeSH), Oxidoreductases (metabolism), Oxidoreductases (physiology), Plant Proteins (metabolism), Protein Disulfide Reductase (Glutathione) (MeSH), Protein Disulfide-Isomerases (MeSH), Reactive Oxygen Species (MeSH).
MESH :
- chemical , analogs & derivatives : Dehydroascorbic Acid.
- chemical , deficiency : Glutathione.
- chemical , metabolism : Dehydroascorbic Acid, NADH, NADPH Oxidoreductases, Oxidoreductases, Plant Proteins.
- chemical , physiology : Isomerases, Oxidoreductases.
- metabolism : Mammals.
- Animals, Animals, Newborn, Glutaredoxins, Oxidation-Reduction, Protein Disulfide Reductase (Glutathione), Protein Disulfide-Isomerases, Reactive Oxygen Species.

Abstract

Dehydroascorbic acid is generated in plants and animal cells by oxidation of ascorbic acid. The reaction is believed to occur by the one-electron oxidation of ascorbic acid to semidehydroascorbate radical followed by disproportionation to dehydroascorbic acid and ascorbic acid. Semidehydroascorbic acid may recycle to ascorbic acid catalyzed by membrane-bound NADH-semidehydroscorbate reductase. However, disproportionation of the free radical occurs at a rapid rate, 10(5) M-1 s-1, accounting for measurable cellular levels of dehydroascorbate. Dehydroascorbate reductase, studied earlier and more extensively in plants, is now recognized as the intrinsic activity of thioltransferases (glutaredoxins) and protein disulfide isomerase in animal cells. These enzymes catalyze the glutathione-dependent two-electron regeneration of ascorbic acid. The importance of the latter route of ascorbic acid renewal was seen in studies of GSH-deficient rodents (Meister, A. (1992) Biochem. Pharmacol. 44, 1905-1915). GSH deficiency in newborn animals resulted in decreased tissue ascorbic acid and increased dehydroascorbate-to-ascorbate ratios. Administration of ascorbic acid daily to GSH-deficient animals decreased animal mortality and cell damage from oxygen stress. A cellular role is proposed for dehydroascorbate in the oxidation of nascent protein dithiols to disulfides catalyzed in the endoplasmic reticulum compartment by protein disulfide isomerase.

DOI: 10.1007/BF00762777
PubMed: 7844111

Affiliations:

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Le document en format XML

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<term>Animals, Newborn (MeSH)</term>
<term>Dehydroascorbic Acid (analogs & derivatives)</term>
<term>Dehydroascorbic Acid (metabolism)</term>
<term>Glutaredoxins (MeSH)</term>
<term>Glutathione (deficiency)</term>
<term>Isomerases (physiology)</term>
<term>Mammals (metabolism)</term>
<term>NADH, NADPH Oxidoreductases (metabolism)</term>
<term>Oxidation-Reduction (MeSH)</term>
<term>Oxidoreductases (metabolism)</term>
<term>Oxidoreductases (physiology)</term>
<term>Plant Proteins (metabolism)</term>
<term>Protein Disulfide Reductase (Glutathione) (MeSH)</term>
<term>Protein Disulfide-Isomerases (MeSH)</term>
<term>Reactive Oxygen Species (MeSH)</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Acide déhydroascorbique (analogues et dérivés)</term>
<term>Acide déhydroascorbique (métabolisme)</term>
<term>Animaux (MeSH)</term>
<term>Animaux nouveau-nés (MeSH)</term>
<term>Espèces réactives de l'oxygène (MeSH)</term>
<term>Glutarédoxines (MeSH)</term>
<term>Glutathion (déficit)</term>
<term>Isomerases (physiologie)</term>
<term>Mammifères (métabolisme)</term>
<term>NADH, NADPH oxidoreductases (métabolisme)</term>
<term>Oxidoreductases (métabolisme)</term>
<term>Oxidoreductases (physiologie)</term>
<term>Oxydoréduction (MeSH)</term>
<term>Protein Disulfide-Isomerases (MeSH)</term>
<term>Protein-disulfide reductase (glutathione) (MeSH)</term>
<term>Protéines végétales (métabolisme)</term>
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<keywords scheme="MESH" type="chemical" qualifier="analogs & derivatives" xml:lang="en"><term>Dehydroascorbic Acid</term>
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<keywords scheme="MESH" type="chemical" qualifier="deficiency" xml:lang="en"><term>Glutathione</term>
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<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Dehydroascorbic Acid</term>
<term>NADH, NADPH Oxidoreductases</term>
<term>Oxidoreductases</term>
<term>Plant Proteins</term>
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<keywords scheme="MESH" type="chemical" qualifier="physiology" xml:lang="en"><term>Isomerases</term>
<term>Oxidoreductases</term>
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<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Acide déhydroascorbique</term>
<term>Mammifères</term>
<term>NADH, NADPH oxidoreductases</term>
<term>Oxidoreductases</term>
<term>Protéines végétales</term>
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<term>Oxidoreductases</term>
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<term>Animals, Newborn</term>
<term>Glutaredoxins</term>
<term>Oxidation-Reduction</term>
<term>Protein Disulfide Reductase (Glutathione)</term>
<term>Protein Disulfide-Isomerases</term>
<term>Reactive Oxygen Species</term>
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<term>Animaux nouveau-nés</term>
<term>Espèces réactives de l'oxygène</term>
<term>Glutarédoxines</term>
<term>Oxydoréduction</term>
<term>Protein Disulfide-Isomerases</term>
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<front><div type="abstract" xml:lang="en">Dehydroascorbic acid is generated in plants and animal cells by oxidation of ascorbic acid. The reaction is believed to occur by the one-electron oxidation of ascorbic acid to semidehydroascorbate radical followed by disproportionation to dehydroascorbic acid and ascorbic acid. Semidehydroascorbic acid may recycle to ascorbic acid catalyzed by membrane-bound NADH-semidehydroscorbate reductase. However, disproportionation of the free radical occurs at a rapid rate, 10(5) M-1 s-1, accounting for measurable cellular levels of dehydroascorbate. Dehydroascorbate reductase, studied earlier and more extensively in plants, is now recognized as the intrinsic activity of thioltransferases (glutaredoxins) and protein disulfide isomerase in animal cells. These enzymes catalyze the glutathione-dependent two-electron regeneration of ascorbic acid. The importance of the latter route of ascorbic acid renewal was seen in studies of GSH-deficient rodents (Meister, A. (1992) Biochem. Pharmacol. 44, 1905-1915). GSH deficiency in newborn animals resulted in decreased tissue ascorbic acid and increased dehydroascorbate-to-ascorbate ratios. Administration of ascorbic acid daily to GSH-deficient animals decreased animal mortality and cell damage from oxygen stress. A cellular role is proposed for dehydroascorbate in the oxidation of nascent protein dithiols to disulfides catalyzed in the endoplasmic reticulum compartment by protein disulfide isomerase.</div>
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<Abstract><AbstractText>Dehydroascorbic acid is generated in plants and animal cells by oxidation of ascorbic acid. The reaction is believed to occur by the one-electron oxidation of ascorbic acid to semidehydroascorbate radical followed by disproportionation to dehydroascorbic acid and ascorbic acid. Semidehydroascorbic acid may recycle to ascorbic acid catalyzed by membrane-bound NADH-semidehydroscorbate reductase. However, disproportionation of the free radical occurs at a rapid rate, 10(5) M-1 s-1, accounting for measurable cellular levels of dehydroascorbate. Dehydroascorbate reductase, studied earlier and more extensively in plants, is now recognized as the intrinsic activity of thioltransferases (glutaredoxins) and protein disulfide isomerase in animal cells. These enzymes catalyze the glutathione-dependent two-electron regeneration of ascorbic acid. The importance of the latter route of ascorbic acid renewal was seen in studies of GSH-deficient rodents (Meister, A. (1992) Biochem. Pharmacol. 44, 1905-1915). GSH deficiency in newborn animals resulted in decreased tissue ascorbic acid and increased dehydroascorbate-to-ascorbate ratios. Administration of ascorbic acid daily to GSH-deficient animals decreased animal mortality and cell damage from oxygen stress. A cellular role is proposed for dehydroascorbate in the oxidation of nascent protein dithiols to disulfides catalyzed in the endoplasmic reticulum compartment by protein disulfide isomerase.</AbstractText>
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	Serveur d'exploration sur la glutarédoxine
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Serveur d'exploration sur la glutarédoxine

Dehydroascorbate reduction.

Dehydroascorbate reduction.

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