Aims: Lewis antigen plays an important role in the progression of gastric cancer (GC), FUT3 is a key enzyme in the synthesis of Lewis antigen, but the molecular mechanism of its promotion of GC progression remains unclear.
Main Methods: We used Lea-antibody capturing coupled with mass spectrometry to identify the target proteins of FUT3, immunofluorescence (IF), molecular biology and cell function experiments were conducted to clarify the molecular mechanism of FUT3 promoting the migration and invasion of GC cells by regulating Lea glycosylation on ITGA6 and GLG1.
Key Findings: FUT3 promote migration and invasion of GC cells. FUT3 silencing in GC cells led to the aggregation of integrin α6β4 on the plasma membrane, associated with focal adhesion and hemidesmosome, and decreased GLG1 distribution in cellular vesicles. IGP analysis revealed Lea structure in 10 N-glycans of 2 glycosites for ITGA6 and 31 N-glycans of 4 glycosites for GLG1. Silencing ITGA6 promoted migration and invasion, while silencing GLG1 inhibited these processes in GC cells, regulated by FUT3-mediated Lea synthesis.
Significance: In conclusion, FUT3's promotion of GC cell migration and invasion is attributed to Lea synthesis on ITGA6, impacting cell adhesion, and on GLG1, influencing distribution in intracellular vesicles. These findings may contribute to developing novel therapeutic targets for inhibiting or controlling the metastatic behavior of GC cells and enhancing our understanding of Lea's role in regulating protein functions.
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| http://dx.doi.org/10.1016/j.lfs.2024.123193 | DOI Listing |
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