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Methods for Analysis of Protein Glutathionylation and their Application to Photosynthetic Organisms

Molecular Plant, 2009
Protein S-glutathionylation, the reversible formation of a mixed-disulfide between glutathione and protein thiols, is involved in protection of protein cysteines from irreversible oxidation, but also in protein redox regulation.
Mirko Zaffagnini, Stéphane D Lemaire, Mariette Bedhomme   +2 more
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Methods to Detect Protein Glutathionylation

Current Protocols in Toxicology, 2013
AbstractGlutathionylation is a posttranslational modification that results in the formation of a mixed disulfide between glutathione and the thiol group of a protein cysteine residue. Glutathionylation of proteins occurs via both nonenzymatic mechanisms involving thiol/disulfide exchange and enzyme‐mediated reactions.
Robyn L, Poerschke, Kristofer S, Fritz, Christopher C, Franklin   +2 more
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Clickable Glutathione‐Based Identification of Cysteine Glutathionylation

Current Protocols, 2023
AbstractClickable glutathione is a glutathione‐derived chemical probe designed to identify and analyze protein S‐glutathionylation, a major cysteine oxidation in redox signaling. An engineered glutathione synthetase mutant (GS M4) is used to synthesize clickable glutathione in cells or in vitro, which affords utility via click chemistry to detect ...
Nadee N J, Matarage Don, Dhanushika S K, Kukulage, Young-Hoon, Ahn   +2 more
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The emerging roles of protein glutathionylation in chloroplasts

Plant Science, 2012
Reactive oxygen species play important roles in redox signaling mainly through a set of reversible post-translational modifications of cysteine thiol residues in proteins, including glutathionylation and dithiol/disulfide exchange. Protein glutathionylation has been extensively studied in mammals but emerging evidence suggests that it can play ...
ZAFFAGNINI, MIRKO, Bedhomme M., Lemaire S. D., TROST, PAOLO BERNARDO   +3 more
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Protein glutathionylation and oxidative stress

Journal of Chromatography B, 2007
Liquid chromatography/electrospray ionization-mass spectrometry (LC/ESI-MS) demonstrated that glutathionyl hemoglobin (Hb) levels are increased in patients with diabetes, hyperlipidemia, uremia and Friedreich's ataxia. Glutathionylation of Hb is enhanced by oxidative stress.
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Measurement of Mixed Disulfides Including Glutathionylated Proteins

2010
Mixed disulfides between protein cysteines and low-molecular-weight thiol cysteine or glutathione lead to the formation of cysteinylated proteins or glutathionylated proteins. These types of posttranslational modification are of great importance in the so-called redox regulation, by which changes in the redox state of the cell regulate a number of ...
PRIORA R., COPPO L., SALZANO S., CHERUBINI DI SIMPLICIO P., GHEZZI P.   +4 more
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Thioredoxins, glutaredoxins, and glutathionylation: new crosstalks to explore

Photosynthesis Research, 2006
Oxidants are widely considered as toxic molecules that cells have to scavenge and detoxify efficiently and continuously. However, emerging evidence suggests that these oxidants can play an important role in redox signaling, mainly through a set of reversible post-translational modifications of thiol residues on proteins.
Michelet L, ZAFFAGNINI, MIRKO, Massot V, Keryer E, Vanacker H, Miginiac Maslow M, Issakidis Bourguet E, Lemaire S.D.   +7 more
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Glutathionylation regulates IkappaB.

Biochemical and biophysical research communications, 2008
Although there has been considerable interest in the regulation of NFkappaB activation by glutathionylation, the possibility of IkappaB as a target for glutathionylation has not been investigated. We now report that Cys(189) of IkappaB alpha is a target for S-glutathionylation. This modification is reversed by thiols such as dithiothreitol and GSH. The
In Sup, Kil, Sung Youl, Kim, Jeen-Woo, Park   +2 more
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Thioltransferase is a specific glutathionyl mixed-disulfide oxidoreductase

Biochemistry, 1993
To study the substrate specificity and mechanism of thioltransferase (TTase) catalysis, we have used 14C- and 35S-radiolabeled mixed disulfides of cysteine and glutathione (GSH) with various cysteine-containing proteins. These protein mixed disulfide substrates were incubated with glutathione, glutathione disulfide (GSSG) reductase, and NADPH in the ...
S A, Gravina, J J, Mieyal
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First Proteomic Study of S-Glutathionylation in Cyanobacteria

Journal of Proteome Research, 2014
Glutathionylation, the reversible post-translational formation of a mixed disulfide between a cysteine residue and glutathione (GSH), is a crucial mechanism for signal transduction and regulation of protein function. Until now this reversible redox modification was studied mainly in eukaryotic cells.
Chardonnet, Solenne, Sakr, Samer, Cassier-Chauvat, Corinne, Le Maréchal, Pierre, Chauvat, Franck, Lemaire, Stéphane D, Decottignies, Paulette   +6 more
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