Proteomic approaches to evaluate protein S-nitrosylation in disease
- PMID: 23775552
- DOI: 10.1002/mas.21373
Proteomic approaches to evaluate protein S-nitrosylation in disease
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.
Keywords: S-nitrosation; S-nitrosothiol; S-nitrosylation; cysteine; nitric oxide; proteomics.
© 2013 Wiley Periodicals, Inc.
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