Abstract
BACKGROUND AND OBJECTIVE: Fucosyltranferase 8 (FUT8), which catalyzes core fucosylation of glycopeptides, plays important roles in cancer development. In this study, we aimed to explore the influence of FUT8 expression on migration ability of human breast cancer cells and its potential mechanisms. METHODS: The core fucosylation levels in normal and FUT8 deficient MCF-7 cells were analyzed by lectin LCA blots. Then, the cell adhesion assay, transwell and wound healing experiments were conducted. The phosphorylation of FAK and core fucosylation of E-cadherin and its downstream integrins in the FAK/integrin pathway were measured. Moreover, the expression levels of nuclear β-catenin, MMP-2, and MMP-9 were also measured. RESULTS: The core fucosylation levels were significantly reduced by inhibited FUT8. FUT8 deficiency suppressed the adhesion, migration and invasion of MCF-7 cells; the potential mechanisms might involve three aspects. FUT8 deficiency inhibited FAK/integrin pathway by suppressing core fucosylation of E-cadherin. In addition, FUT8 deficiency reduced nuclear β-catenin accumulation. The suppression of MMP-2 and MMP-9 expression also accounted for FUT8 deficiency inhibiting breast cancer cells migration. CONCLUSIONS: FUT8 deficiency suppressed migration of MCF-7 cells by impacting core fucosylation of E-cadherin and the downstream FAK/integrin pathway. Therefore, FUT8 is a potential biomarker for breast cancer detection and treatment.