Seeing citrulline: development of a phenylglyoxal-based probe to visualize protein citrullination.
AuthorsBicker, Kevin L.
Chumanevich, Alexander A.
Hofseth, Lorne J.
Thompson, Paul R
UMass Chan AffiliationsDepartment of Biochemistry and Molecular Pharmacology
Document TypeJournal Article
Enzymes and Coenzymes
MetadataShow full item record
AbstractProtein arginine deiminases (PADs) catalyze the hydrolysis of peptidyl arginine to form peptidyl citrulline. Abnormally high PAD activity is observed in a host of human diseases, but the exact role of protein citrullination in these diseases and the identities of specific citrullinated disease biomarkers remain unknown, largely because of the lack of readily available chemical probes to detect protein citrullination. For this reason, we developed a citrulline-specific chemical probe, rhodamine-phenylglyoxal (Rh-PG), which we show can be used to investigate protein citrullination. This methodology is superior to existing techniques because it possesses higher throughput and excellent sensitivity. Additionally, we demonstrate that this probe can be used to determine the kinetic parameters for a number of protein substrates, monitor drug efficacy, and identify disease biomarkers in an animal model of ulcerative colitis that displays aberrantly increased PAD activity.
SourceJ Am Chem Soc. 2012 Oct 17;134(41):17015-8. doi: 10.1021/ja308871v. Epub 2012 Oct 3. Link to article on publisher's site
Permanent Link to this Itemhttp://hdl.handle.net/20.500.14038/50022
At the time of publication, Paul Thompson was not yet affiliated with UMass Medical School.
Related ResourcesLink to Article in PubMed