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Comparative Glycomic Profiling in Esophageal Adenocarcinoma
Zane Hammoud1, Yehia Mechref2, Ahmed Hussein2, Slavka Bekesova2, Min Zhang2, Kenneth Kesler3, Robert Hickey3, Milos Novotny2; 1Cardiothoracic Surgery, Henry Ford Health System, Detroit, MI; 2Indiana University, Bloomington, IN; 3Indiana University School of Medicine, Indianapolis, IN
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Objective: Aberrant glycosylation has been implicated in various types of cancers and changes in glycosylation may be associated with signaling pathways during malignant transformation. Cancerous cells with altered glycosylation of their surface proteins shed such proteins into the circulating fluids. Glycomic profiling of such fluids would reveal the altered glycosylation. We performed glycomic profiling of serum from patients with no known disease, patients with high grade dysplasia, and patients with esophageal adenocarcinoma in an attempt to delineate distinct differences in glycosylation between these groups.
Methods: Serum samples from patients with Barrett's metaplasia (N=5), high-grade dysplasia (HGD, N=11) and esophageal adenocarcinoma (EAC, N=50) were collected; samples from 18 healthy volunteers were used as control. Serum N-glycans were enzymatically released using PNGase F. Samples were then applied to both C18 Sep-Pak® cartridges and activated charcoal cartridges. N-glycans were permethylated and then spotted directly on the MALDI plate and mixed with equal volume of DHB-matrix. Mass spectra were acquired using the Applied Biosystems 4800 MALDI TOF/TOF Analyzer. The obtained MALDI-MS data were processed using DataExplorer files listing m/z values and intensities.
Results: The intensities of 98 glycans were significantly different among the 3 groups; 26 of these correspond to known glycan structures. Pairwise comparisons showed that 8 glycans are significantly different in all three pairwise comparisons. Figure 1 shows the mass spectra plots obtained for each category.
Conclusion: We have demonstrated that comparative glycomic profiling of EAC reveals a subset of glycans that can be selected as candidate biomarkers. These markers can differentiate normal from HGD, normal from EAC, and HGD from EAC. Further validation will be necessary to determine the clinical utility of these glycan biomarkers.

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