GlutaredoxinV1, Main, Exploration, bibRecord, 000655

Glutaredoxin 2 (Grx2) gene deletion induces early onset of age-dependent cataracts in mice.

Identifieur interne : 000655 ( Main/Exploration ); précédent : 000654; suivant : 000656

Glutaredoxin 2 (Grx2) gene deletion induces early onset of age-dependent cataracts in mice.

Auteurs : Hongli Wu [États-Unis] ; Yibo Yu [République populaire de Chine] ; Larry David [États-Unis] ; Ye-Shih Ho ; Marjorie F. Lou [États-Unis]

Source :

The Journal of biological chemistry [ 1083-351X ] ; 2014.

RBID : pubmed:25362663

Descripteurs français

KwdFr :
- Adénosine triphosphate (métabolisme), Animaux (MeSH), Capsule du cristallin (anatomopathologie), Capsule du cristallin (métabolisme), Cataracte (génétique), Complexe I de la chaîne respiratoire (métabolisme), Complexe IV de la chaîne respiratoire (métabolisme), Cystine (métabolisme), Délétion de gène (MeSH), Glutarédoxines (génétique), Glutathion (métabolisme), Mâle (MeSH), Protéines de l'oeil (métabolisme), Souris de souche-129 (MeSH), Souris knockout (MeSH).
MESH :
- anatomopathologie : Capsule du cristallin.
- génétique : Cataracte, Glutarédoxines.
- métabolisme : Adénosine triphosphate, Capsule du cristallin, Complexe I de la chaîne respiratoire, Complexe IV de la chaîne respiratoire, Cystine, Glutathion, Protéines de l'oeil.
- Animaux, Délétion de gène, Mâle, Souris de souche-129, Souris knockout.

English descriptors

KwdEn :
- Adenosine Triphosphate (metabolism), Animals (MeSH), Cataract (genetics), Cystine (metabolism), Electron Transport Complex I (metabolism), Electron Transport Complex IV (metabolism), Eye Proteins (metabolism), Gene Deletion (MeSH), Glutaredoxins (genetics), Glutathione (metabolism), Lens Capsule, Crystalline (metabolism), Lens Capsule, Crystalline (pathology), Male (MeSH), Mice, 129 Strain (MeSH), Mice, Knockout (MeSH).
MESH :
- chemical , genetics : Glutaredoxins.
- chemical , metabolism : Adenosine Triphosphate, Cystine, Electron Transport Complex I, Electron Transport Complex IV, Eye Proteins, Glutathione.
- genetics : Cataract.
- metabolism : Lens Capsule, Crystalline.
- pathology : Lens Capsule, Crystalline.
- Animals, Gene Deletion, Male, Mice, 129 Strain, Mice, Knockout.

Abstract

Glutaredoxin 2 (Grx2) is an isozyme of glutaredoxin1 (thioltransferase) present in the mitochondria and nucleus with disulfide reductase and peroxidase activities, and it controls thiol/disulfide balance in cells. In this study, we investigated whether Grx2 gene deletion could induce faster age-related cataract formation and elucidated the biochemical changes effected by Grx2 gene deletion that may contribute to lens opacity. Slit lamp was used to examine the lenses in Grx2 knock-out (KO) mice and age-matched wild-type (WT) mice ages 1 to 16 months. In the Grx2 null mice, the lens nuclear opacity began at 5 months, 3 months sooner than that of the control mice, and the progression of cataracts was also much faster than the age-matched controls. Lenses of KO mice contained lower levels of protein thiols and GSH with a significant accumulation of S-glutathionylated proteins. Actin, αA-crystallin, and βB2-crystallin were identified by Western blot and mass spectroscopy as the major S-glutathionylated proteins in the lenses of 16-month-old Grx2 KO mice. Compared with the WT control, the lens of Grx2 KO mice had only 50% of the activity in complex I and complex IV and less than 10% of the ATP pool. It was concluded that Grx2 gene deletion altered the function of lens structural proteins through S-glutathionylation and also caused severe disturbance in mitochondrial function. These combined alterations affected lens transparency.

DOI: 10.1074/jbc.M114.620047
PubMed: 25362663
PubMed Central: PMC4276876

Affiliations:

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

to stream Main, to step Corpus: 000584
to stream Main, to step Curation: 000584

Le document en format XML

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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Adenosine Triphosphate (metabolism)</term>
<term>Animals (MeSH)</term>
<term>Cataract (genetics)</term>
<term>Cystine (metabolism)</term>
<term>Electron Transport Complex I (metabolism)</term>
<term>Electron Transport Complex IV (metabolism)</term>
<term>Eye Proteins (metabolism)</term>
<term>Gene Deletion (MeSH)</term>
<term>Glutaredoxins (genetics)</term>
<term>Glutathione (metabolism)</term>
<term>Lens Capsule, Crystalline (metabolism)</term>
<term>Lens Capsule, Crystalline (pathology)</term>
<term>Male (MeSH)</term>
<term>Mice, 129 Strain (MeSH)</term>
<term>Mice, Knockout (MeSH)</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Adénosine triphosphate (métabolisme)</term>
<term>Animaux (MeSH)</term>
<term>Capsule du cristallin (anatomopathologie)</term>
<term>Capsule du cristallin (métabolisme)</term>
<term>Cataracte (génétique)</term>
<term>Complexe I de la chaîne respiratoire (métabolisme)</term>
<term>Complexe IV de la chaîne respiratoire (métabolisme)</term>
<term>Cystine (métabolisme)</term>
<term>Délétion de gène (MeSH)</term>
<term>Glutarédoxines (génétique)</term>
<term>Glutathion (métabolisme)</term>
<term>Mâle (MeSH)</term>
<term>Protéines de l'oeil (métabolisme)</term>
<term>Souris de souche-129 (MeSH)</term>
<term>Souris knockout (MeSH)</term>
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<term>Cystine</term>
<term>Electron Transport Complex I</term>
<term>Electron Transport Complex IV</term>
<term>Eye Proteins</term>
<term>Glutathione</term>
</keywords>
<keywords scheme="MESH" qualifier="anatomopathologie" xml:lang="fr"><term>Capsule du cristallin</term>
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<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Cataract</term>
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<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Cataracte</term>
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<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Lens Capsule, Crystalline</term>
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<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Adénosine triphosphate</term>
<term>Capsule du cristallin</term>
<term>Complexe I de la chaîne respiratoire</term>
<term>Complexe IV de la chaîne respiratoire</term>
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<term>Glutathion</term>
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<term>Délétion de gène</term>
<term>Mâle</term>
<term>Souris de souche-129</term>
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<front><div type="abstract" xml:lang="en">Glutaredoxin 2 (Grx2) is an isozyme of glutaredoxin1 (thioltransferase) present in the mitochondria and nucleus with disulfide reductase and peroxidase activities, and it controls thiol/disulfide balance in cells. In this study, we investigated whether Grx2 gene deletion could induce faster age-related cataract formation and elucidated the biochemical changes effected by Grx2 gene deletion that may contribute to lens opacity. Slit lamp was used to examine the lenses in Grx2 knock-out (KO) mice and age-matched wild-type (WT) mice ages 1 to 16 months. In the Grx2 null mice, the lens nuclear opacity began at 5 months, 3 months sooner than that of the control mice, and the progression of cataracts was also much faster than the age-matched controls. Lenses of KO mice contained lower levels of protein thiols and GSH with a significant accumulation of S-glutathionylated proteins. Actin, αA-crystallin, and βB2-crystallin were identified by Western blot and mass spectroscopy as the major S-glutathionylated proteins in the lenses of 16-month-old Grx2 KO mice. Compared with the WT control, the lens of Grx2 KO mice had only 50% of the activity in complex I and complex IV and less than 10% of the ATP pool. It was concluded that Grx2 gene deletion altered the function of lens structural proteins through S-glutathionylation and also caused severe disturbance in mitochondrial function. These combined alterations affected lens transparency. </div>
</front>
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<Abstract><AbstractText>Glutaredoxin 2 (Grx2) is an isozyme of glutaredoxin1 (thioltransferase) present in the mitochondria and nucleus with disulfide reductase and peroxidase activities, and it controls thiol/disulfide balance in cells. In this study, we investigated whether Grx2 gene deletion could induce faster age-related cataract formation and elucidated the biochemical changes effected by Grx2 gene deletion that may contribute to lens opacity. Slit lamp was used to examine the lenses in Grx2 knock-out (KO) mice and age-matched wild-type (WT) mice ages 1 to 16 months. In the Grx2 null mice, the lens nuclear opacity began at 5 months, 3 months sooner than that of the control mice, and the progression of cataracts was also much faster than the age-matched controls. Lenses of KO mice contained lower levels of protein thiols and GSH with a significant accumulation of S-glutathionylated proteins. Actin, αA-crystallin, and βB2-crystallin were identified by Western blot and mass spectroscopy as the major S-glutathionylated proteins in the lenses of 16-month-old Grx2 KO mice. Compared with the WT control, the lens of Grx2 KO mice had only 50% of the activity in complex I and complex IV and less than 10% of the ATP pool. It was concluded that Grx2 gene deletion altered the function of lens structural proteins through S-glutathionylation and also caused severe disturbance in mitochondrial function. These combined alterations affected lens transparency. </AbstractText>
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Glutaredoxin 2 (Grx2) gene deletion induces early onset of age-dependent cataracts in mice.

Glutaredoxin 2 (Grx2) gene deletion induces early onset of age-dependent cataracts in mice.

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