Neutral loss of isocyanic acid in peptide CID spectra: A novel diagnostic marker for mass spectrometric identification of protein citrullination |
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Authors: | Gang Hao Danchen Wang Jane Gu Qiuying Shen Steven S Gross Yanming Wang |
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Institution: | (1) Environmental Molecular Sciences Laboratory, MSIN K8-98, Pacific Northwest National Laboratory, P.O. Box 999, Richland, WA 99352, USA;(2) Present address: Department of Chemistry, Chungnam National University, Daejeon, 305-764, South Korea;(3) Biophysics Research Division, Department of Biological Chemistry, University of Michigan, Ann Arbor, MI 48109, USA; |
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Abstract: | Protein citrullination is emerging as an important signaling mechanism that modulates a variety of biological processes. This
protein modification constitutes only a 1 Da mass shift, and can be readily confused with other common protein modifications
that yield an identical mass shift. In an attempt to develop a robust methodology for detection of protein citrullination
sites, we analyzed synthetic citrulline-containing peptides by electrospray ionization tandem mass spectrometry. Collision-induced
dissociation (CID) spectra revealed abundant neutral loss of 43 Da from citrullinated peptide precursor ions, which was reconciled
by elimination of the HNCO moiety (isocyanic acid) from the citrulline ureido group. The elimination occurs readily in multiple
charge states of precursor ions and also in b and y ions. HNCO loss in CID spectra provides a novel diagnostic marker for
citrullination, and its utility was demonstrated by the discovery of Arg197 as the specific site of citrullination on nucleophosmin
upon peptidylarginine deiminase 4 treatment. |
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