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BioMed Research International
Volume 2013 (2013), Article ID 834790, 9 pages
Research Article

Development of a Novel System for Mass Spectrometric Analysis of Cancer-Associated Fucosylation in Plasma α1-Acid Glycoprotein

1Department of General Surgical Science, Gunma University Graduate School of Medicine, Maebashi 371-8511, Japan
2Tokushima Research Institute, Otsuka Pharmaceutical Co., Ltd., Tokushima 771-0192, Japan
3Institute of Biomedical Innovation, Otsuka Pharmaceutical Co., Ltd., Tokushima 771-0192, Japan
4S-BIO Business Division, Sumitomo Bakelite Co., Ltd., Tokyo 140-0002, Japan
5JIMRO Co., Ltd., Tokyo 151-0063, Japan

Received 3 November 2012; Accepted 13 December 2012

Academic Editor: Tavan Janvilisri

Copyright © 2013 Takayuki Asao et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


Human plasma α1-acid glycoprotein (AGP) from cancer patients and healthy volunteers was purified by sequential application of ion-exchange columns, and N-linked glycans enzymatically released from AGP were labeled and applied to a mass spectrometer. Additionally, a novel software system for use in combination with a mass spectrometer to determine N-linked glycans in AGP was developed. A database with 607 glycans including 453 different glycan structures that were theoretically predicted to be present in AGP was prepared for designing the software called AGPAS. This AGPAS was applied to determine relative abundance of each glycan in the AGP molecules based on mass spectra. It was found that the relative abundance of fucosylated glycans in tri- and tetra-antennary structures (FUCAGP) was significantly higher in cancer patients as compared with the healthy group ( ). Furthermore, extremely elevated levels of FUCAGP were found specifically in patients with a poor prognosis but not in patients with a good prognosis. In conclusion, the present software system allowed rapid determination of the primary structures of AGP glycans. The fucosylated glycans as novel tumor markers have clinical relevance in the diagnosis and assessment of cancer progression as well as patient prognosis.