PLoS ONE · 2013 · 64 citations · 37 references
Life SciencesBiochemistryOncologyGlycobiologyMolecular OncologyProteomicsCancer GlycobiologyCancer ProteomicsCell-surface GlycansGlycan AnalysisGlycan StructureGlycoproteomicsAberrant Glycosylation In CancerBreast Cancer ProgressionCancer Cell Surface GlycansHigh-mannose GlycansHigh-mannose N-glycansN-glycan AnalysisN-glycan ProfilingN-glycosylation In Cancer
Aberrant changes in specific glycans have been shown to be associated with immunosurveillance, tumorigenesis, tumor progression and metastasis. In this study, the N-glycan profiling of membrane proteins from human breast cancer cell lines and tissues was detected using modified DNA sequencer-assisted fluorophore-assisted carbohydrate electrophoresis (DSA-FACE). The N-glycan profiles of membrane proteins were analyzed from 7 breast cancer cell lines and MCF 10A, as well as from 100 pairs of breast cancer and corresponding adjacent tissues. The results showed that, compared with the matched adjacent normal tissue samples, two biantennary N-glycans (NA2 and NA2FB) were significantly decreased (p <0.0001) in the breast cancer tissue samples, while the triantennary glycan (NA3FB) and a high-mannose glycan (M8) were dramatically increased (p = 0.001 and p <0.0001, respectively). Moreover, the alterations in these specific N-glycans occurred through the oncogenesis and progression of breast cancer. These results suggested that the modified method based on DSA-FACE is a high-throughput detection technology that is suited for analyzing cell surface N-glycans. These cell surface-specific N-glycans may be helpful in recognizing the mechanisms of tumor cell immunologic escape and could be potential targets for new breast cancer drugs.
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SEER Cancer Statistics Review, 1975-2003
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