title: Protein S-glutathionylation: from current basics to targeted modifications.
abstract: The interaction between antioxidant glutathione and the free thiol in susceptible cysteine residues of proteins leads to reversible protein S-glutathionylation. This reaction ensures cellular homeostasis control (as a common redox-dependent post-translational modification associated with signal transduction) and intervenes in oxidative stress-related cardiovascular pathology (as initiated by redox imbalance). The purpose of this review is to evaluate the recent knowledge on protein S-glutathionylation in terms of chemistry, broad cellular intervention, specific quantification, and potential for therapeutic exploitation. The data bases searched were Medline and PubMed, from 2009 to 2014 (term: glutathionylation). Protein S-glutathionylation ensures protection of protein thiols against irreversible over-oxidation, operates as a biological redox switch in both cell survival (influencing kinases and protein phosphatases pathways) and cell death (by potentiation of apoptosis), and cross-talks with phosphorylation and with S-nitrosylation. Collectively, protein S-glutathionylation appears as a valuable biomarker for oxidative stress, with potential for translation into novel therapeutic strategies.
authors.affiliation: Institute of Cellular Biology and Pathology "N. Simionescu" of the Romanian Academy , 8, B.P. Hasdeu Street, Bucharest 050568 , Romania.
authors.forename: Doina
authors.initials: D
authors.lastname: Popov
mesh_terms: D000818:Animals; D005978:Glutathione / Q000378:metabolism*; D006801:Humans; D018384:Oxidative Stress; D011499:Protein Processing, Post-Translational; D011506:Proteins / Q000378:metabolism*; D013438:Sulfhydryl Compounds / Q000737:chemistry*
chemical_list: D011506:Proteins; D013438:Sulfhydryl Compounds; D005978:Glutathione
keywords: Cysteine; glutaredoxin; glutathione; protein tyrosine phosphatases (PTPs); thioredoxin