title: Protein Cysteinyl-S-Nitrosylation: Analysis and Quantification.
abstract: The thiol moiety of cysteine residues can undergo a number of biologic modifications including oxidation, sulfenylation, nitrosylation, persulfidation, metalation, and other modifications. These modifications can control biological function, including gain as well as loss of function. Herein, we focus attention on the proteomic analysis of S-nitrosylation in health and disease. We describe a novel quantitative approach that combines accurate, sensitive fluorescence modification of cysteinyl-S-nitrosylation that leaves electrophoretic mobility unaffected (SNOFlo), and introduce unique concepts for measuring changes in S-nitrosylation status relative to protein abundance. We present several studies where suitability of this approach for investigating endogenous S-nitrosylation is addressed.
authors.affiliation: Sealy Center of Molecular Medicine, University of Texas Medical Branch, Galveston, TX, United States; Institute for Translational Sciences, University of Texas Medical Branch, Galveston, TX, United States; Institute for Human Infections and Immunity, University of Texas Medical Branch, Galveston, TX, United States.
authors.forename: J E
authors.initials: JE
authors.lastname: Wiktorowicz
authors.affiliation: Sealy Center of Molecular Medicine, University of Texas Medical Branch, Galveston, TX, United States.
authors.forename: S J
authors.initials: SJ
authors.lastname: Stafford
authors.affiliation: University of Texas Medical Branch, Galveston, TX, United States; Institute for Translational Sciences, University of Texas Medical Branch, Galveston, TX, United States; Institute for Human Infections and Immunity, University of Texas Medical Branch, Galveston, TX, United States. Electronic address: nigarg@utmb.edu.
authors.forename: N J
authors.initials: NJ
authors.lastname: Garg
mesh_terms: D000818:Animals; D003545:Cysteine / Q000031:analogs & derivatives* / Q000032:analysis / Q000378:metabolism; D006801:Humans; D011499:Protein Processing, Post-Translational; D020543:Proteome / Q000032:analysis* / Q000378:metabolism; D026403:S-Nitrosothiols / Q000032:analysis* / Q000378:metabolism; D013050:Spectrometry, Fluorescence
chemical_list: D020543:Proteome; D026403:S-Nitrosothiols; C021315:S-nitrosocysteine; D003545:Cysteine
keywords: BODIPY Fl-maleimide; Cysteinyl-S-nitrosylation; Proteome