Measurement of protein S-nitrosylation during cell signaling

Methods in Enzymology
Joan B Mannick, Christopher M Schonhoff

Abstract

S-Nitrosylation, the modification of a cysteine thiol by a nitric oxide (NO) group, has emerged as an important posttranslational modification of signaling proteins. An impediment to studying the regulation of cell signaling by S-nitrosylation has been the technical challenge of detecting endogenously S-nitrosylated proteins. Detection of S-nitrosylated proteins is difficult because the S-NO bond is labile and therefore can be lost or gained artifactually during sample preparation. Nevertheless, several methods have been developed to measure endogenous protein S-nitrosylation, including the biotin switch assay and the chemical reduction/chemiluminescence assay. This chapter describes these two methods and provides examples of how they have been used successfully to elucidate the role of protein S-nitrosylation in cell physiology and pathophysiology.

Citations

Jun 30, 2009·Antioxidants & Redox Signaling·Vittorio CalabreseD Allan Butterfield
Feb 27, 2013·Chemical Reviews·Yaoyang ZhangJohn R Yates
Jan 23, 2009·Proteomics·Laura M López-SánchezAntonio Rodríguez-Ariza
Dec 27, 2017·Free Radical Biology & Medicine·Markus DagnellElias S J Arnér
May 15, 2009·Free Radical Biology & Medicine·Clare L HawkinsMichael J Davies
Mar 15, 2011·Biochimica Et Biophysica Acta·Claude A Piantadosi

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