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

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Abstract

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.

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Abbreviations

ANOVA:

One-way analysis of variance

AUC:

Area under receiver operating characteristic curve

MALDI–FTICR MS:

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

MS:

Mass spectrometry

PAC:

Pancreatic adenocarcinoma

PT:

Pancreatitis

ROC:

Receiver operating characteristic

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Acknowledgments

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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Correspondence to Zhili Li.

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Chen, G., Li, H., Qiu, L. et al. Change of fucosylated IgG2 Fc-glycoforms in pancreatitis and pancreatic adenocarcinoma: a promising disease-classification model. Anal Bioanal Chem 406, 267–273 (2014). https://doi.org/10.1007/s00216-013-7439-3

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  • DOI: https://doi.org/10.1007/s00216-013-7439-3

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