Redox proteomics applied to the thiol secretome

Ghezzi, Pietro and Philippe, Chan (2017) Redox proteomics applied to the thiol secretome. Antioxidants and Redox Signaling, 26 (7). pp. 299-312. ISSN 1523-0864

[img] PDF - Accepted Version
Download (3MB)

Abstract

Significance: Secreted proteins are important both as signaling molecules and potential biomarkers.

Recent Advances: Protein can undergo different types of oxidation, both in physiological conditions or under oxidative stress. Several redox proteomics techniques have been successfully applied to the identification of glutathionylated proteins, an oxidative post-translational modification consisting in the formation of a mixed disulfide between a protein cysteine and glutathione. Redox proteomics has also been used to study other forms of protein oxidation.

Critical Issues: Because of the highest proportion of free cysteines in the cytosol, redox proteomics of protein thiols has focused, so far, on intracellular proteins. However, plasma proteins, such as transthyretin and albumin, have been described as glutathionylated or cysteinylated. The present review discusses the redox state of protein cysteines in relation to their cellular distribution. We describe the various approaches used to detect secreted glutathionylated proteins, the only thiol modification studied so far in secreted proteins, and the specific problems presented in the study of the secretome.

Future Directions: This review focusses on glutathionylated proteins secreted under inflammatory conditions and that may act as soluble mediators (cytokines). Future studies on the redox secretome (including other forms of oxidation) might identify new soluble mediators and biomarkers of oxidative stress.

Item Type: Article
Schools and Departments: Brighton and Sussex Medical School > Clinical and Experimental Medicine
Subjects: Q Science
R Medicine
R Medicine > R Medicine (General)
Depositing User: Pietro Ghezzi
Date Deposited: 04 May 2016 11:02
Last Modified: 05 Oct 2017 18:25
URI: http://sro.sussex.ac.uk/id/eprint/60752

View download statistics for this item

📧 Request an update