Chemical Proteomic Platform To Identify Citrullinated Proteins
Department of Biochemistry and Molecular Pharmacology
Biochemistry | Enzymes and Coenzymes | Medicinal-Pharmaceutical Chemistry | Therapeutics
Anti-citrullinated protein antibodies (ACPAs) are a hallmark of rheumatoid arthritis (RA) and are routinely used for disease diagnosis. Protein citrullination is also increased in cancer and other autoimmune disorders, suggesting that citrullinated proteins may serve as biomarkers for diseases beyond RA. To identify these citrullinated proteins, we developed biotin-conjugated phenylglyoxal (biotin-PG). Using this probe and our platform technology, we identified > 50 intracellular citrullinated proteins. More than 20 of these are involved in RNA splicing, suggesting, for the first time, that citrullination modulates RNA biology. Overall, this chemical proteomic platform will play a key role in furthering our understanding of protein citrullination in rheumatoid arthritis and potentially a wider spectrum of inflammatory diseases.
DOI of Published Version
ACS Chem Biol. 2015 Sep 23. [Epub ahead of print] Link to article on publisher's site
ACS chemical biology
Lewallen DM, Bicker KL, Subramanian V, Clancy KW, Slade DJ, Martell J, Dreyton CJ, Sokolove J, Weerapana E, Thompson PR. (2015). Chemical Proteomic Platform To Identify Citrullinated Proteins. Thompson Lab Publications. https://doi.org/10.1021/acschembio.5b00438. Retrieved from https://escholarship.umassmed.edu/thompson/103