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Protein glutathionylation in health and disease

Biochimica Et Biophysica Acta - General Subjects, 2013
It is now recognized that protein cysteines exist not only as free thiols or intramolecular disulfides, that help maintain the 3D structure of proteins, but can also undergo different types of oxidation, one of which is glutathionylation, or the formation of mixed disulfides with glutathione (GSH).We will discuss how proteins can undergo ...
Pietro Ghezzi
exaly   +4 more sources

Role of Glutathionylation in Infection and Inflammation [PDF]

Nutrients, 2019
Glutathionylation, that is, the formation of mixed disulfides between protein cysteines and glutathione (GSH) cysteines, is a reversible post-translational modification catalyzed by different cellular oxidoreductases, by which the redox state of the cell modulates protein function. So far, most studies on the identification of glutathionylated proteins
Sara Baldelli, Paola Checconi, Anna Teresa Palamara   +2 more
exaly   +8 more sources

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Emerging chemistry and biology in protein glutathionylation

Current Opinion in Chemical Biology, 2022
Protein S-glutathionylation serves a regulatory role in proteins and modulates distinct biological processes implicated in health and diseases. Despite challenges in analyzing the dynamic and reversible nature of S-glutathionylation, recent chemical and biological methods have significantly advanced the field of S-glutathionylation, culminating in ...
Young-Hoon Ahn, Dhanushika S K Kukulage, Nadee N J Matarage Don   +2 more
exaly   +3 more sources

Chemistry and biology of enzymes in protein glutathionylation

Current Opinion in Chemical Biology, 2023
Protein 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, Madhu C Shivamadhu
exaly   +3 more sources

Redox Regulation by Protein S-Glutathionylation: From Molecular Mechanisms to Implications in Health and Disease

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
exaly   +2 more sources

Glutathionylation regulates IκB

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
Jeen-Woo Park, In Sup Kil
exaly   +2 more sources

Overview of Protein Glutathionylation

Current Protocols in Toxicology, 2006
AbstractMany 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, Michael P, Murphy   +1 more
openaire   +2 more sources

Measurement of Protein Glutathionylation

Current Protocols in Toxicology, 2006
AbstractProteins 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, Michael P, Murphy   +1 more
openaire   +2 more sources

Glutathionylation of Mitochondrial Proteins

Antioxidants & Redox Signaling, 2005
Many 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, Nikola J, Costa, Christina C, Dahm, Samantha M, Beer, Stephanie E, Brown, Aleksandra, Filipovska, Michael P, Murphy   +6 more
openaire   +2 more sources

Redox regulation of cyclophilin A by glutathionylation

PROTEOMICS, 2006
AbstractUsing redox proteomics techniques to characterize the thiol status of proteins in human T lymphocytes, we identified cyclophilin A (CypA) as a specifically oxidized protein early after mitogen activation. CypA is an abundantly expressed cytosolic protein, target of the immunosuppressive drug cyclosporin A (CsA), for which a variety of functions
Ghezzi, Pietro, Casagrande, Simona, Massignan, Tania, Basso, Manuela, Bellacchio, Emanuele, Mollica, Luca, Biasini, Emiliano, Tonelli, Rossella, Eberini, Ivano, Gianazza, Elisabetta, Dai, Wei Wei, Fratelli, Maddalena, Salmona, Mario, Sherry, Barbara, Bonetto, Valentina   +14 more
openaire   +2 more sources