Key result
Biotin-PG probe identifies ~50 intracellular citrullinated proteins including key RNA splicing factors.
Why the study?
Protein citrullination is increased in rheumatoid arthritis, cancer, and other autoimmune disorders, but identification of citrullinated proteins beyond RA is limited.
Development of a chemical proteomic platform using biotin-PG identified over 50 citrullinated proteins, suggesting a novel role for citrullination in RNA biology.
Biotin-PG probe maps citrullinated proteins beyond RA; leaves open their validation as biomarkers in cancer and autoimmunity.
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.
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Lewallen et al. (2015) studied Rheumatoid arthritis. Biotin-conjugated phenylglyoxal (biotin-PG) chemical proteomic platform was evaluated on Identification of intracellular citrullinated proteins. A chemical proteomic platform using biotin-conjugated phenylglyoxal identified >50 intracellular citrullinated proteins, including >20 involved in RNA splicing.
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