title: Redox Proteomics Applied to the Thiol Secretome.
abstract: 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.
  
  
  
  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.
  
  
  
  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. Antioxid. Redox Signal. 26, 299-312.
authors.affiliation: 1 Brighton & Sussex Medical School , Brighton, United Kingdom .
authors.forename: Pietro
authors.initials: P
authors.lastname: Ghezzi
authors.affiliation: 2 PISSARO Proteomic Platform, Institute for Research and Innovation in Biomedicine, University of Rouen , Rouen, France .
authors.forename: Philippe
authors.initials: P
authors.lastname: Chan
mesh_terms: D000818:Animals; D015415:Biomarkers; D003545:Cysteine / Q000378:metabolism; D004220:Disulfides / Q000378:metabolism; D006801:Humans; D010084:Oxidation-Reduction; D018384:Oxidative Stress; D046988:Proteasome Endopeptidase Complex; D011499:Protein Processing, Post-Translational; D021381:Protein Transport; D011506:Proteins / Q000378:metabolism*; D020543:Proteome; D040901:Proteomics / Q000379:methods; D013438:Sulfhydryl Compounds / Q000378:metabolism*
chemical_list: D015415:Biomarkers; D004220:Disulfides; D011506:Proteins; D020543:Proteome; D013438:Sulfhydryl Compounds; D046988:Proteasome Endopeptidase Complex; D003545:Cysteine
keywords: biomarkers; glutathione; oxidative stress; protein oxidation; proteomics; secretome