Title

Chemical Proteomic Platform To Identify Citrullinated Proteins

UMMS Affiliation

Department of Biochemistry and Molecular Pharmacology

Publication Date

9-23-2015

Document Type

Article

Disciplines

Biochemistry | Enzymes and Coenzymes | Medicinal-Pharmaceutical Chemistry | Therapeutics

Abstract

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

10.1021/acschembio.5b00438

Source

ACS Chem Biol. 2015 Sep 23. [Epub ahead of print] Link to article on publisher's site

Journal/Book/Conference Title

ACS chemical biology

Related Resources

Link to Article in PubMed

PubMed ID

26360112