Mutation of N-linked glycosylation in EpCAM affected cell adhesion in breast cancer cells.
Epithelial cell adhesion molecule (EpCAM) expression is elevated in breast cancer tissue, and correlates with the cancer metastasis and cell adhesion. Although EpCAM glycosylation is supposed to be associated with its function, the contribution of N-glycosylation to its function remains unclear. Here we analyzed cell adhesion ability of EpCAM in breast cancer cells. The results showed that EpCAM expression was associated with cell adhesion and N-glycosylation mutation of EpCAM decreased adhesion capacity. N-glycosylation mutation of EpCAM was correlated with lower levels of integrin β1 and fibronectin. We also found that effect of N-glycosylation of EpCAM on cell adhesion was regulated via FAK/Akt/Gsk-3β/β-catenin signaling pathway, which further adjusted MMP2/9 expression and activities. Our studies identified the characteristics and function of EpCAM glycosylation sites on breast cancer cell adhesion. These data could potentially clarify molecular regulation of EpCAM by N-glycosylation and intensify our understanding of the utility of glycosylated EpCAM as a target for breast cancer therapy.
Xue
X
Liu
Jiujiao
J
Gao
Yan
Y
Sun
Dandan
D
Zhang
Tingjiao
T
Liu
Qiu
Q
Yan
Xuesong
X
Yang
D001943:Breast Neoplasms / Q000235:genetics* / Q000378:metabolism / Q000473:pathology*; D002448:Cell Adhesion / Q000235:genetics*; D000071858:Epithelial Cell Adhesion Molecule / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D005260:Female; D006031:Glycosylation; D006801:Humans; D009154:Mutation; D014407:Tumor Cells, Cultured
C499379:EPCAM protein, human; D000071858:Epithelial Cell Adhesion Molecule
EpCAM; N-glycosylation; breast cancer; cell adhesion; signaling pathway