S-Glutathionyl quantification in the attomole range using glutaredoxin-3-catalyzed cysteine derivatization and capillary gel electrophoresis with laser-induced fluorescence detection.
Identifieur interne : 000919 ( Main/Exploration ); précédent : 000918; suivant : 000920S-Glutathionyl quantification in the attomole range using glutaredoxin-3-catalyzed cysteine derivatization and capillary gel electrophoresis with laser-induced fluorescence detection.
Auteurs : Cheng Zhang [États-Unis] ; Cynthia Rodriguez ; Magdalena L. Circu ; Tak Yee Aw ; June FengSource :
- Analytical and bioanalytical chemistry [ 1618-2650 ] ; 2011.
Descripteurs français
- KwdFr :
- Animaux (MeSH), Bovins (MeSH), Cellules HT29 (MeSH), Cystéine (composition chimique), Fluorescence (MeSH), Glutarédoxines (métabolisme), Glutathion (métabolisme), Humains (MeSH), Lasers (MeSH), Maladie d'Alzheimer (diagnostic), Maturation post-traductionnelle des protéines (MeSH), Modèles animaux de maladie humaine (MeSH), Oxydoréduction (MeSH), Souris (MeSH), Sérumalbumine bovine (métabolisme), Électrophorèse capillaire (instrumentation), Électrophorèse capillaire (méthodes).
- MESH :
- composition chimique : Cystéine.
- diagnostic : Maladie d'Alzheimer.
- métabolisme : Glutarédoxines, Glutathion, Sérumalbumine bovine.
- méthodes : Électrophorèse capillaire.
- instrumentation : Animaux, Bovins, Cellules HT29, Fluorescence, Humains, Lasers, Maturation post-traductionnelle des protéines, Modèles animaux de maladie humaine, Oxydoréduction, Souris, Électrophorèse capillaire.
English descriptors
- KwdEn :
- Alzheimer Disease (diagnosis), Animals (MeSH), Cattle (MeSH), Cysteine (chemistry), Disease Models, Animal (MeSH), Electrophoresis, Capillary (instrumentation), Electrophoresis, Capillary (methods), Fluorescence (MeSH), Glutaredoxins (metabolism), Glutathione (metabolism), HT29 Cells (MeSH), Humans (MeSH), Lasers (MeSH), Mice (MeSH), Oxidation-Reduction (MeSH), Protein Processing, Post-Translational (MeSH), Serum Albumin, Bovine (metabolism).
- MESH :
- chemical , chemistry : Cysteine.
- diagnosis : Alzheimer Disease.
- instrumentation : Electrophoresis, Capillary.
- chemical , metabolism : Glutaredoxins, Glutathione, Serum Albumin, Bovine.
- methods : Electrophoresis, Capillary.
- Animals, Cattle, Disease Models, Animal, Fluorescence, HT29 Cells, Humans, Lasers, Mice, Oxidation-Reduction, Protein Processing, Post-Translational.
Abstract
S-glutathionylation (Pr-SSG) is a specific post-translational modification of cysteine residues by the addition of glutathione. S-Glutathionylated proteins induced by oxidative or nitrosative stress play an essential role in understanding the pathogenesis of the aging and age-related disorder, such as Alzheimer's disease (AD). The purpose of this research is to develop a novel and ultrasensitive method to accurately and rapidly quantify the Pr-SSG by using capillary gel electrophoresis with laser-induced fluorescence detection (CGE-LIF). The derivatization method is based on the specific reduction of protein-bound S-glutathionylation with glutaredoxin (Grx) and labeling with thiol-reactive fluorescent dye (Dylight 488 maleimide). The experiments were performed by coupling the derivatization method with CGE-LIF to study electrophoretic profiling in in vitro oxidative stress model-S-glutathionylated bovine serum albumin (BSA-SSG), oxidant-induced human colon adenocarcinoma (HT-29) cells, brain tissues, and whole blood samples from an AD transgenic (Tg) mouse model. The results showed almost an eightfold increase in S-glutathionyl abundance when subjecting HT-29 cells in an oxidant environment, resulting in Pr-SSG at 232 ± 10.64 (average ±SD; n=3) nmol/mg. In the AD-Tg mouse model, an initial quantitative measurement demonstrated the extent of protein S-glutathionylation in three brain regions (hippocampus, cerebellum, and cerebrum), ranging from 1 to 10 nmol/mg. Additionally, we described our developed method to potentially serve as a highly desirable diagnostic tool for monitoring S-glutathionylated protein profile in minuscule amount of whole blood. The whole blood samples for S-glutathionyl expression of 5-month-old AD-Tg mice are quantified as 16.3 μmol/L (=7.2 nmol/mg protein). Altogether, this is a fast, easy, and accurate method, reaching the lowest limit of Pr-SSG detection at 1.8 attomole (amol) level, reported to date.
DOI: 10.1007/s00216-011-5311-x
PubMed: 21842197
PubMed Central: PMC4221632
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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<term>Electrophoresis, Capillary (instrumentation)</term>
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<term>Lasers (MeSH)</term>
<term>Mice (MeSH)</term>
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<term>Protein Processing, Post-Translational (MeSH)</term>
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<term>Fluorescence (MeSH)</term>
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<term>Glutathion (métabolisme)</term>
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<term>Lasers (MeSH)</term>
<term>Maladie d'Alzheimer (diagnostic)</term>
<term>Maturation post-traductionnelle des protéines (MeSH)</term>
<term>Modèles animaux de maladie humaine (MeSH)</term>
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<front><div type="abstract" xml:lang="en">S-glutathionylation (Pr-SSG) is a specific post-translational modification of cysteine residues by the addition of glutathione. S-Glutathionylated proteins induced by oxidative or nitrosative stress play an essential role in understanding the pathogenesis of the aging and age-related disorder, such as Alzheimer's disease (AD). The purpose of this research is to develop a novel and ultrasensitive method to accurately and rapidly quantify the Pr-SSG by using capillary gel electrophoresis with laser-induced fluorescence detection (CGE-LIF). The derivatization method is based on the specific reduction of protein-bound S-glutathionylation with glutaredoxin (Grx) and labeling with thiol-reactive fluorescent dye (Dylight 488 maleimide). The experiments were performed by coupling the derivatization method with CGE-LIF to study electrophoretic profiling in in vitro oxidative stress model-S-glutathionylated bovine serum albumin (BSA-SSG), oxidant-induced human colon adenocarcinoma (HT-29) cells, brain tissues, and whole blood samples from an AD transgenic (Tg) mouse model. The results showed almost an eightfold increase in S-glutathionyl abundance when subjecting HT-29 cells in an oxidant environment, resulting in Pr-SSG at 232 ± 10.64 (average ±SD; n=3) nmol/mg. In the AD-Tg mouse model, an initial quantitative measurement demonstrated the extent of protein S-glutathionylation in three brain regions (hippocampus, cerebellum, and cerebrum), ranging from 1 to 10 nmol/mg. Additionally, we described our developed method to potentially serve as a highly desirable diagnostic tool for monitoring S-glutathionylated protein profile in minuscule amount of whole blood. The whole blood samples for S-glutathionyl expression of 5-month-old AD-Tg mice are quantified as 16.3 μmol/L (=7.2 nmol/mg protein). Altogether, this is a fast, easy, and accurate method, reaching the lowest limit of Pr-SSG detection at 1.8 attomole (amol) level, reported to date.</div>
</front>
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<Abstract><AbstractText>S-glutathionylation (Pr-SSG) is a specific post-translational modification of cysteine residues by the addition of glutathione. S-Glutathionylated proteins induced by oxidative or nitrosative stress play an essential role in understanding the pathogenesis of the aging and age-related disorder, such as Alzheimer's disease (AD). The purpose of this research is to develop a novel and ultrasensitive method to accurately and rapidly quantify the Pr-SSG by using capillary gel electrophoresis with laser-induced fluorescence detection (CGE-LIF). The derivatization method is based on the specific reduction of protein-bound S-glutathionylation with glutaredoxin (Grx) and labeling with thiol-reactive fluorescent dye (Dylight 488 maleimide). The experiments were performed by coupling the derivatization method with CGE-LIF to study electrophoretic profiling in in vitro oxidative stress model-S-glutathionylated bovine serum albumin (BSA-SSG), oxidant-induced human colon adenocarcinoma (HT-29) cells, brain tissues, and whole blood samples from an AD transgenic (Tg) mouse model. The results showed almost an eightfold increase in S-glutathionyl abundance when subjecting HT-29 cells in an oxidant environment, resulting in Pr-SSG at 232 ± 10.64 (average ±SD; n=3) nmol/mg. In the AD-Tg mouse model, an initial quantitative measurement demonstrated the extent of protein S-glutathionylation in three brain regions (hippocampus, cerebellum, and cerebrum), ranging from 1 to 10 nmol/mg. Additionally, we described our developed method to potentially serve as a highly desirable diagnostic tool for monitoring S-glutathionylated protein profile in minuscule amount of whole blood. The whole blood samples for S-glutathionyl expression of 5-month-old AD-Tg mice are quantified as 16.3 μmol/L (=7.2 nmol/mg protein). Altogether, this is a fast, easy, and accurate method, reaching the lowest limit of Pr-SSG detection at 1.8 attomole (amol) level, reported to date.</AbstractText>
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