Analytical and Bioanalytical Chemistry

, Volume 406, Issue 1, pp 267–273 | Cite as

Change of fucosylated IgG2 Fc-glycoforms in pancreatitis and pancreatic adenocarcinoma: a promising disease-classification model

  • Guoqiang Chen
  • Hexiang Li
  • Ling Qiu
  • Xuzhen Qin
  • Hui Liu
  • Zhili Li
Research Paper


The fixed constant (Fc) region of IgG is subject to changes in glycosylation state in response to diseases. On the basis of sera from 75 healthy controls, 75 pancreatitis (PT) patients, and 75 pancreatic adenocarcinoma (PAC) patients, we analyzed six fucosylated glycoforms of IgG2 (G0F, G1F, G2F, G0FN, G1FN, and G2FN), by matrix-assisted laser desorption/ionization–Fourier-transform ion cyclotron resonance mass spectrometry (MALDI–FTICR MS), to evaluate their use as biomarkers for pancreatic diseases. Compared with healthy controls, significant increases in agalactosylated glycoforms and decreases in galactosylated glycoforms were observed for PT and PAC patients. Logistic regression analysis suggested that truncation of the sugar chain was prone to occur in PT and, especially, PAC patients. After participants were stratified by sex and age, receiver operating characteristic curve analysis revealed good overall sensitivity and specificity for discrimination of PAC and PT patients from healthy controls. A combination of G0F and galactosylation also had acceptable power for differentiating PAC patients from PT patients.


IgG2 N-glycosylation Pancreatitis Pancreatic adenocarcinoma Diagnosis MALDI–FTICR MS 



One-way analysis of variance


Area under receiver operating characteristic curve


Matrix-assisted laser desorption/ionization–Fourier-transform ion cyclotron resonance mass spectrometry


Mass spectrometry


Pancreatic adenocarcinoma




Receiver operating characteristic



This study was supported by grant no. 21075137 from the National Natural Science Foundation of China and by the Research Fund for the Doctoral Program of Higher Education (grant no. 20121106110023) (to Z. Li).


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Copyright information

© Springer-Verlag Berlin Heidelberg 2013

Authors and Affiliations

  • Guoqiang Chen
    • 1
  • Hexiang Li
    • 2
  • Ling Qiu
    • 3
  • Xuzhen Qin
    • 3
  • Hui Liu
    • 1
  • Zhili Li
    • 1
  1. 1.Department of Biophysics and Structural Biology, Institute of Basic Medical SciencesChinese Academy of Medical Sciences and Peking Union Medical CollegeBeijingChina
  2. 2.Caoxian Gongfei HospitalShandongChina
  3. 3.Department of Clinical Laboratory, Peking Union Medical College HospitalChinese Academy of Medical Sciences and Peking Union Medical CollegeBeijingChina

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