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Chemistry and biology of enzymes in protein glutathionylation
Current Opinion in Chemical Biology, 2023Protein S-glutathionylation is emerging as a central oxidation that regulates redox signaling and biological processes linked to diseases. In recent years, the field of protein S-glutathionylation has expanded by developing biochemical tools for the identification and functional analyses of S-glutathionylation, investigating knockout mouse models, and ...
Young-Hoon Ahn
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Glutathionylation regulates IκB
Biochemical and Biophysical Research Communications, 2008Although 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 +2 more
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International Journal of Molecular Sciences, 2020 S-glutathionylation, the post-translational modification forming mixed disulfides between protein reactive thiols and glutathione, regulates redox-based signaling events in the cell and serves as a protective mechanism against oxidative damage.
Yuh-Cherng Chai
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Overview of Protein Glutathionylation
Current Protocols in Toxicology, 2006AbstractMany proteins contain free thiols that can be modified by the reversible formation of mixed disulfides with glutathione. Protein glutathionylation is of significance for defense against oxidative damage and in redox signaling. Here we outline the mechanisms and possible significance of protein glutathionylation.
Aleksandra, Filipovska +1 more
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Measurement of Protein Glutathionylation
Current Protocols in Toxicology, 2006AbstractProteins contain free, exposed thiols that can be glutathionylated in the native state as a result of thiol‐disulfide exchange reactions with glutathione disulfide, catalyzed by glutaredoxin. A number of other reactions can also lead to protein glutathionylation. The modification of proteins by glutathionylation is important in oxidative damage
Aleksandra, Filipovska +1 more
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Glutathionylation of Mitochondrial Proteins
Antioxidants & Redox Signaling, 2005Many proteins contain free thiols that can be modified by the reversible formation of mixed disulfides with low-molecular-weight thiols through a process called S-thiolation. As the majority of these modifications result from the interaction of protein thiols with the endogenous glutathione pool, protein glutathionylation is the predominant alteration.
Thomas R, Hurd +6 more
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Methods to Detect Protein Glutathionylation
Current Protocols in Toxicology, 2013AbstractGlutathionylation 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 +2 more
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Clickable Glutathione‐Based Identification of Cysteine Glutathionylation
Current Protocols, 2023AbstractClickable 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 +2 more
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Protein glutathionylation and oxidative stress
Journal of Chromatography B, 2007Liquid 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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Oxidant-induced glutathionylation at protein disulfide bonds
Free Radical Biology and Medicine, 2020Disulfide bonds are a key determinant of protein structure and function, and highly conserved across proteomes. They are particularly abundant in extracellular proteins, including those with critical structural, ligand binding or receptor function.
Luke Carroll +7 more
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