Fucosylated cell-surface glycans

Fucosylated cell-surface glycans are complex carbohydrate structures characterized by the addition of fucose sugar units to glycoproteins and glycolipids on the cell membrane. These glycans are essential for various biological processes, including cell-cell recognition, leukocyte trafficking via selectin binding, and the modulation of signaling pathways like Notch and TGF-beta (NCBI, PMID: 29038312). In oncology, aberrant fucosylation—often mediated by the upregulation of fucosyltransferases—is a recognized driver of tumor progression, facilitating metastasis and helping cancer cells evade immune detection (PubMed, PMID: 33431134). Consequently, these glycans, particularly the Lewis antigen family (e.g., Sialyl-Lewis X, Lewis Y), are significant targets for therapeutic intervention (Nature, doi:10.1038/s41416-018-0214-x). Current drug development strategies include the use of glycomimetics like uproleselan to block adhesion, small molecule inhibitors like 2-fluorofucose to prevent glycan synthesis, and monoclonal antibodies designed to selectively eliminate cells expressing high levels of these tumor-associated carbohydrate antigens (GlycoMimetics; PubMed, PMID: 30655270).

Other names

Fucosylated glycansFucosylated carbohydratesLewis antigensSialyl-Lewis antigensFucose-containing glycoconjugatesTumor-associated carbohydrate antigens (TACA)

Inhibition of cell adhesion via E-selectin antagonism, depletion of intracellular GDP-fucose to inhibit fucosyltransferases, and direct antibody-mediated targeting of tumor-associated carbohydrate antigens.