GSBS Student Publications

Title

Measurement of protein S-nitrosylation during cell signaling

UMMS Affiliation

Graduate School of Biomedical Sciences; Department of Medicine, Division of Infectious Diseases and Immunology; Department of Cell Biology

Date

4-22-2008

Document Type

Article

Medical Subject Headings

Animals; *Cell Physiological Phenomena; Cells; Humans; Proteins; S-Nitrosothiols; Signal Transduction

Disciplines

Life Sciences | Medicine and Health Sciences

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.

Rights and Permissions

Citation: Methods Enzymol. 2008;440:231-42. Link to article on publisher's site

Related Resources

Link to Article in PubMed

Journal Title

Methods in enzymology

PubMed ID

18423221