Identification by Redox Proteomics of Glutathionylated Proteins in Oxidatively Stressed Human T Lymphocytes

Formation of mixed disulfides between glutathione and the cysteines of some proteins (glutathionylation) has been suggested as a mechanism through which protein functions can be regulated by the redox status. The aim of this study was to identify the proteins of T cell blasts that undergo glutathion...

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Veröffentlicht in:Proceedings of the National Academy of Sciences - PNAS 2002-03, Vol.99 (6), p.3505-3510
Hauptverfasser: Fratelli, Maddalena, Demol, Hans, Puype, Magda, Casagrande, Simona, Eberini, Ivano, Salmona, Mario, Bonetto, Valentina, Mengozzi, Manuela, Duffieux, Francis, Miclet, Emeric, Bachi, Angela, Vandekerckhove, Joel, Gianazza, Elisabetta, Ghezzi, Pietro
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container_issue 6
container_start_page 3505
container_title Proceedings of the National Academy of Sciences - PNAS
container_volume 99
creator Fratelli, Maddalena
Demol, Hans
Puype, Magda
Casagrande, Simona
Eberini, Ivano
Salmona, Mario
Bonetto, Valentina
Mengozzi, Manuela
Duffieux, Francis
Miclet, Emeric
Bachi, Angela
Vandekerckhove, Joel
Gianazza, Elisabetta
Ghezzi, Pietro
description Formation of mixed disulfides between glutathione and the cysteines of some proteins (glutathionylation) has been suggested as a mechanism through which protein functions can be regulated by the redox status. The aim of this study was to identify the proteins of T cell blasts that undergo glutathionylation under oxidative stress. To this purpose, we radiolabeled cellular glutathione with35S, exposed T cells to oxidants (diamide or hydrogen peroxide), and performed nonreducing, two-dimensional electrophoresis followed by detection of labeled proteins by phosphorimaging and their identification by mass spectrometry techniques. We detected several proteins previously not recognized to be glutathionylated, including cytoskeletal proteins (vimentin, myosin, tropomyosin, cofilin, profilin, and the already known actin), enzymes (enolase, aldolase, 6-phosphogluconolactonase, adenylate kinase, ubiquitin-conjugating enzyme, phosphoglycerate kinase, triosephosphate isomerase, and pyrophosphatase), redox enzymes (peroxiredoxin 1, protein disulfide isomerase, and cytochrome c oxidase), cyclophilin, stress proteins (HSP70 and HSP60), nucleophosmin, transgelin, galectin, and fatty acid binding protein. Based on the presence of several protein isoforms in control cells, we suggest that enolase and cyclophilin are heavily glutathionylated under basal conditions. We studied the effect of glutathionylation on some of the enzymes identified in the present study and found that some of them (enolase and 6-phosphogluconolactonase) are inhibited by glutathionylation, whereas the enzymatic activity of cyclophilin (peptidylprolyl isomerase) is not. These findings suggest that protein glutathionylation might be a common mechanism for the global regulation of protein functions.
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The aim of this study was to identify the proteins of T cell blasts that undergo glutathionylation under oxidative stress. To this purpose, we radiolabeled cellular glutathione with35S, exposed T cells to oxidants (diamide or hydrogen peroxide), and performed nonreducing, two-dimensional electrophoresis followed by detection of labeled proteins by phosphorimaging and their identification by mass spectrometry techniques. We detected several proteins previously not recognized to be glutathionylated, including cytoskeletal proteins (vimentin, myosin, tropomyosin, cofilin, profilin, and the already known actin), enzymes (enolase, aldolase, 6-phosphogluconolactonase, adenylate kinase, ubiquitin-conjugating enzyme, phosphoglycerate kinase, triosephosphate isomerase, and pyrophosphatase), redox enzymes (peroxiredoxin 1, protein disulfide isomerase, and cytochrome c oxidase), cyclophilin, stress proteins (HSP70 and HSP60), nucleophosmin, transgelin, galectin, and fatty acid binding protein. Based on the presence of several protein isoforms in control cells, we suggest that enolase and cyclophilin are heavily glutathionylated under basal conditions. We studied the effect of glutathionylation on some of the enzymes identified in the present study and found that some of them (enolase and 6-phosphogluconolactonase) are inhibited by glutathionylation, whereas the enzymatic activity of cyclophilin (peptidylprolyl isomerase) is not. 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Based on the presence of several protein isoforms in control cells, we suggest that enolase and cyclophilin are heavily glutathionylated under basal conditions. We studied the effect of glutathionylation on some of the enzymes identified in the present study and found that some of them (enolase and 6-phosphogluconolactonase) are inhibited by glutathionylation, whereas the enzymatic activity of cyclophilin (peptidylprolyl isomerase) is not. 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subjects Biochemistry
Biological Sciences
Biology
Blasts
Cells, Cultured
Chemistry
Diamide - pharmacology
Disulfides
Disulfides - metabolism
Electrophoresis
Electrophoresis, Gel, Two-Dimensional
Enzymes
Galectins
glutathione
Glutathione - metabolism
glutathionylation
Humans
Hydrogen Peroxide - pharmacology
Mass Spectrometry
Molecular Weight
Oxidants - pharmacology
Oxidation
Oxidation-Reduction - drug effects
Oxidative stress
Oxidative Stress - drug effects
Physiological regulation
Protein isoforms
Proteins
Proteome - chemistry
Proteome - drug effects
Proteome - metabolism
proteomics
Rosaniline Dyes
Staining and Labeling
T lymphocytes
T-Lymphocytes - chemistry
T-Lymphocytes - drug effects
T-Lymphocytes - enzymology
T-Lymphocytes - metabolism
title Identification by Redox Proteomics of Glutathionylated Proteins in Oxidatively Stressed Human T Lymphocytes
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