Oncotarget

Research Papers:

Identification of aberrantly expressed glycans in gastric cancer by integrated lectin microarray and mass spectrometric analyses

Xiang Li, Feng Guan, Dongliang Li, Zengqi Tan, Ganglong Yang, Yanli Wu and Zhaohui Huang _

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Oncotarget. 2016; 7:87284-87300. https://doi.org/10.18632/oncotarget.13539

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Abstract

Xiang Li1,2, Feng Guan2,3, Dongliang Li3,4, Zengqi Tan3, Ganglong Yang3, Yanli Wu3, Zhaohui Huang1

1Wuxi Oncology Institute, Affiliated Hospital of Jiangnan University, Wuxi, Jiangsu, China

2College of Life Science, Northwest University, Xi’an, Shannxi, China

3The Key Laboratory of Carbohydrate Chemistry & Biotechnology, Ministry of Education, School of Biotechnology, Jiangnan University, Wuxi, China

4Bioimaging Core, Faculty of Health Sciences, University of Macau, Taipa, Macau SAR, China

Correspondence to:

Zhaohui Huang, email: [email protected]

Keywords: gastric cancer, lectin microarray, lectin histochemistry, mass spectrometry, N-glycan

Received: May 12, 2016    Accepted: November 01, 2016    Published: November 24, 2016

ABSTRACT

Cancer progression is usually associated with alterations of glycan expression patterns. Little is known regarding global glycomics in gastric cancer, the most common type of epithelial cancer. We integrated lectin microarray and mass spectrometry (MS) methods to profile glycan expression in three gastric cancer cell lines (SGC-7901, HGC-27, and MGC-803) and one normal gastric epithelial cell line (GES-1). Significantly altered glycans were confirmed by lectin staining and MALDI-TOF/TOF-MS. The three cancer cell lines showed increased levels of core-fucosylated N-glycans, GalNAcα-Ser/Thr (Tn antigen), and Sia2-6Galβ1-4GlcNAc N-glycans, but reduced levels of biantennary N-glycans, Galβ1-3GalNAcα-Ser/Thr (T antigen), and (GlcNAc)n N-glycans. Lectin histochemistry was used to validate aberrant expression of four representative glycans (core-fucosylation, Sia2-6Galβ1-4GlcNAc, biantennary N-glycans, T antigen, recognized respectively by lectins LCA, SNA, PHA-E+L, and ACA) in clinical gastric cancer samples. Lower binding capacity for ACA was correlated with significantly poorer patient prognosis. Our findings indicate for the first time that glycans recognized by LCA, ACA, and PHA-E+L are aberrantly expressed in gastric cancer, and suggest that ACA is a potential prognostic factor for gastric cancer.


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