Proteomic approaches to evaluate protein s‐nitrosylation in disease. Issue 1 (15th June 2013)

• Record Type: Journal Article
• Authors: López‐Sánchez, Laura M.; López‐Pedrera, Chary; Rodríguez‐Ariza, Antonio; Allan Butterfield, D.; Dalle‐Donne, Isabella
• Is Part Of: Mass spectrometry reviews. Volume 33:Issue 1(2014:Jan./Feb.)
• Page Start: 7
• Page End: 20
• Publication Date: 2013-06-15
• Subjects: Mass spectrometry -- Periodicals; 543
• DOI: 10.1002/mas.21373
• Languages: English
• ISSNs: 0277-7037

Abstract

<abstract abstract-type="main" xml:lang="en"> <title>Abstract</title> <sec id="mas21373-sec-0001" sec-type="section"> <p>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 <italic>S</italic>‐nitrosothiol (SNO), a process known as <italic>S</italic>‐nitrosylation or <italic>S</italic>‐nitrosation. In many cases this reversible post‐translational modification is accompanied by altered protein function and aberrant <italic>S</italic>‐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 <italic>S</italic>‐nitrosylation and the analysis of <italic>S</italic>‐nitrosoproteomes under pathological conditions is beginning to be reported. The study of these <italic>S</italic>‐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 <italic>S</italic>‐nitrosoproteome in disease. Copyright © 2013 Wiley Periodicals, Inc. Rapid Commun. Mass Spectrom. 33: 7–20, 2014.</p> </sec> </abstract>