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
Publication Date
2008-04-22
Document Type
Article
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.
DOI of Published Version
10.1016/S0076-6879(07)00814-2
Source
Methods Enzymol. 2008;440:231-42. Link to article on publisher's site
Journal/Book/Conference Title
Methods in enzymology
Related Resources
PubMed ID
18423221
Repository Citation
Mannick JB, Schonhoff CM. (2008). Measurement of protein S-nitrosylation during cell signaling. GSBS Student Publications. https://doi.org/10.1016/S0076-6879(07)00814-2. Retrieved from https://escholarship.umassmed.edu/gsbs_sp/1486