Proteomic approaches to evaluate protein s-nitrosylation in disease
Article first published online: 15 JUN 2013
© 2013 Wiley Periodicals, Inc.
Mass Spectrometry Reviews
Special Issue: Special Issue on Redox Proteomics Part 1
Volume 33, Issue 1, pages 7–20, January/February 2014
How to Cite
López-Sánchez, L. M., López-Pedrera, C. and Rodríguez-Ariza, A. (2014), Proteomic approaches to evaluate protein s-nitrosylation in disease. Mass Spectrom. Rev., 33: 7–20. doi: 10.1002/mas.21373
- Issue published online: 27 NOV 2013
- Article first published online: 15 JUN 2013
- Manuscript Accepted: 29 JAN 2013
- Manuscript Received: 28 NOV 2012
- Consejería de Salud de la Junta de Andalucía. Grant Number: JA0230/09
- Programa de Promoción de la Investigación en Salud del Ministerio de Economía y Competitividad. Grant Number: FIS 10/00428
- nitric oxide;
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.