作者
Ying-Chih Liu, Hsin-Yung Yen, Chien-Yu Chen, Chein-Hung Chen, Ping-Fu Cheng, Yi-Hsiu Juan, Chung-Hsuan Chen, Kay-Hooi Khoo, Chong-Jen Yu, Pan-Chyr Yang, Tsui-Ling Hsu, Chi-Huey Wong
发表日期
2011/7/12
期刊
Proceedings of the National Academy of Sciences
卷号
108
期号
28
页码范围
11332-11337
出版商
National Academy of Sciences
简介
Protein glycosylation is an important posttranslational process, which regulates protein folding and functional expression. Studies have shown that abnormal glycosylation in tumor cells affects cancer progression and malignancy. In the current study, we have identified sialylated proteins using an alkynyl sugar probe in two different lung cancer cell lines, CL1-0 and CL1-5 with distinct invasiveness derived from the same parental cell line. Among the identified sialylated proteins, epidermal growth factor receptor (EGFR) was chosen to understand the effect of sialylation on its function. We have determined the differences in glycan sequences of EGFR in both cells and observed higher sialylation and fucosylation of EGFR in CL1-5 than in CL1-0. Further study suggested that overexpression of sialyltransferases in CL1-5 and α1,3-fucosyltransferases (FUT4 or FUT6) in CL1-5 and A549 cells would suppress EGFR …
引用总数
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