Proteomic approaches to evaluate protein s-nitrosylation in disease

Authors

  • Laura M. López-Sánchez,

    1. Research Unit, Instituto Maimónides de Investigación Biomédica de Córdoba (IMIBIC), Hospital Reina Sofía, Universidad de Córdoba, Spain
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  • Chary López-Pedrera,

    1. Research Unit, Instituto Maimónides de Investigación Biomédica de Córdoba (IMIBIC), Hospital Reina Sofía, Universidad de Córdoba, Spain
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  • Antonio Rodríguez-Ariza

    Corresponding author
    1. Research Unit, Instituto Maimónides de Investigación Biomédica de Córdoba (IMIBIC), Hospital Reina Sofía, Universidad de Córdoba, Spain
    • Correspondence to: Antonio Rodríguez-Ariza, IMIBIC, Unidad de Investigación, Hospital Universitario Reina Sofía, Avda Menéndez Pidal s/n, 14004 Córdoba, Spain. E-mail: antonio.rodriguez.exts@juntadeandalucia.es

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Abstract

Many of nitric oxide (NO) actions are mediated through the coupling of a nitroso moiety to a reactive cysteine leading to the formation of a S-nitrosothiol (SNO), a process known as S-nitrosylation or S-nitrosation. In many cases this reversible post-translational modification is accompanied by altered protein function and aberrant S-nitrosylation of proteins, caused by altered production of NO and/or impaired SNO homeostasis, has been repeatedly reported in a variety of pathophysiological settings. A growing number of studies are directed to the identification and characterization of those proteins that undergo S-nitrosylation and the analysis of S-nitrosoproteomes under pathological conditions is beginning to be reported. The study of these S-nitrosoproteomes has been fueled by advances in proteomic technologies that are providing researchers with improved tools for exploring this post-translational modification. Here we review novel refinements and improvements to these methods, and some recent studies of the S-nitrosoproteome in disease. © 2013 Wiley Periodicals, Inc. Mass Spec Rev 33: 7–20, 2014.

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