Detection and identification of protein citrullination in complex biological systems
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UMass Chan Affiliations
Program in Chemical BiologyDepartment of Biochemistry and Molecular Pharmacology
Document Type
Journal ArticlePublication Date
2016-02-01
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Protein citrullination is a post-translational modification of arginine that is catalyzed by the Protein Arginine Deiminase (PAD) family of enzymes. Aberrantly increased citrullination is associated with a host of inflammatory diseases and cancer and PAD inhibitors have shown remarkable efficacy in a range of diseases including rheumatoid arthritis, lupus, atherosclerosis, and ulcerative colitis. In rheumatoid arthritis, citrullinated proteins serve as key antigens for rheumatoid arthritis-associated autoantibodies. These data suggest that citrullinated proteins may serve more generally as biomarkers of specific disease states, however, the identification of citrullinated residues remains challenging due to the small 1Da mass change that occurs upon citrullination. Herein, we highlight the available techniques to identify citrullinated proteins/residues focusing on advanced MS techniques as well as chemical derivatization strategies that are currently being employed to identify citrullinated proteins as well as the specific residues modified within those proteins.Source
Curr Opin Chem Biol. 2016 Feb;30:1-6. doi: 10.1016/j.cbpa.2015.10.014. Epub 2015 Oct 27.Link to article on publisher's siteDOI
10.1016/j.cbpa.2015.10.014Permanent Link to this Item
http://hdl.handle.net/20.500.14038/49984PubMed ID
26517730Related Resources
Link to Article in PubMedae974a485f413a2113503eed53cd6c53
10.1016/j.cbpa.2015.10.014