Sialylation and Fucosylation of Epidermal Growth Factor Receptor Suppress its Dimerization and Activation in Lung Cancer Cells
Date Issued
2011
Date
2011
Author(s)
Liu, Ying-Chih
Abstract
Glycosylation is an important post-translational modification, which regulates proteins folding and functional expression. Previous studies have shown that, abnormal glycosylation in tumor cells can participate in cancer progression and malignancy. In the current study, we compared the sialylated and fucosylated proteins with alkynyl sugars in different lung cancer cell lines, CL1-0 and CL1-5, two subpopulations derived from the same parental cell line but with distinct invasiveness. Our initial experiments demonstrated that CL1-5, the highly aggressive cells, expressed more sialylated and fucosylated proteins than CL1-0. At next step, we identified the unique sialylated proteins in CL1-5. Among them, we chose epidermal growth factor receptor (EGFR) to further study the role of sialylation on its function. Based on glycan analysis, we validated the distinct sialylation level of EGFR in both cells. Interestingly, we also observed higher fucosylation of EGFR in CL1-5 than in CL1-0, corresponding to the comparison of whole proteins glycosylation in both cells using alkynyl fucose. Further study suggested that overexpression of sialyltranssferases in CL1-5 and
Subjects
Sialic acid
Fucose
EGFR
Glycoproteomics
glycan sequencing
SDGs
Type
thesis
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