Protein glutathionylation in health and disease

Ghezzi, Pietro (2013) Protein glutathionylation in health and disease. BBA - Biochimica et Biophysica Acta, 1830 (5). pp. 3165-3172. ISSN 0006-3002

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Abstract

BACKGROUND

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). SCOPE OF THE REVIEW: We will discuss how proteins can undergo glutathionylation and how this can affect the protein characteristics/function. Glutathionylation is reversible and de-glutathionylation can be catalysed by protein thiol-disulfide oxidoreductases. Genetic modification of the expression of these enzymes, particularly glutaredoxin, using overexpression, knockout mice or siRNA, is becoming an important tool to study the role of protein glutathionylation. While in the past this post-translational modification was mainly known in the context of oxidative stress, measurement of glutathionylated proteins in patients is pointing out a potential importance if this modification in pathogenesis and could identify new biomarkers. We also wanted to point out the main findings in the role of glutathionylation in diseases and drug action.

MAJOR CONCLUSIONS

We identify two major open problems in the field, namely the complexity of the mechanisms responsible for glutathionylation and de-glutathionylation, as well as what makes a protein susceptible to glutathionylation.

GENERAL SIGNIFICANCE

This review underlines the peculiarities of this post-translational modification and their biological role. This article is part of a Special Issue entitled Cellular functions of glutathione.

Item Type: Article
Additional Information: Impact Factor: 3.883
Keywords: Glutathionylation; Cysteinylation; Glutaredoxin; Thioredoxin; Sulfiredoxin; Inflammation
Schools and Departments: Brighton and Sussex Medical School > Clinical and Laboratory Investigation
Subjects: R Medicine
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Depositing User: Patricia Butler
Date Deposited: 30 Apr 2013 06:50
Last Modified: 30 Apr 2013 06:50
URI: http://sro.sussex.ac.uk/id/eprint/44540
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