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ACS Chem Biol. 2015 Nov 20;10(11):2520-8. doi: 10.1021/acschembio.5b00438. Epub 2015 Sep 23.

Chemical Proteomic Platform To Identify Citrullinated Proteins.

Author information

1
Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School , Worcester, Massachusetts 01605, United States.
2
Department of Chemistry, Boston College , Chestnut Hill, Massachusetts 02467, United States.
3
Division of Immunology and Rheumatology, Department of Medicine, Stanford University School of Medicine , Stanford, California 94305, United States.

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.

PMID:
26360112
PMCID:
PMC4729336
DOI:
10.1021/acschembio.5b00438
[Indexed for MEDLINE]
Free PMC Article

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