Determination of membrane glycoconjugate glycosylation profile on A427 human lung adenocarcinoma cell line by lectins
José Antonio Serrato, Ricardo Lascurain, David García-Herrera, Patricia Gorocica Rosete
2011, Number 4
2011; 70 (4)
ABSTRACT
Due to recent advances in glycobiology, cell surface glycoconjugate molecules have arisen as potential biomarkers for the early and specific lung cancer diagnosis. However, the inherent ubiquity of cellular glycans makes difficult the identification of tumor specific saccharidic structures. The use of cell lines is an approach that helps to identify tumor-related saccharidic structures for the development of a diagnostic method. Our objective was to evaluate the glycosylation profile on cell membrane glycoconjugates of the human lung adenocarcinoma cell line A427. The identification of specific N- and O-glycan structures was carried out by the use of nine different lectins. Glycosylation profile analysis showed an increase in the relative abundance of sialylated structures, specifically Sialyl-Tn glycans, as well as lactosamine and short O-glycans like T-antigen in comparison with complex, hybrid and high mannose type N-glycans. Our data suggest these structures are well candidate molecules to search for glycans specific of lung adenocarcinoma.
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