Fucosylated glycans

Fucosylated glycans are carbohydrate structures containing fucose residues, which are essential for various biological processes including cell-cell adhesion, immune system regulation, and signal transduction (NCBI, Essentials of Glycobiology, 2017). These glycans are synthesized by a family of enzymes known as fucosyltransferases (FUTs) and are often found on the terminal ends of N-linked and O-linked glycoproteins or glycolipids. In pathological states, particularly cancer, the expression of fucosylated motifs such as Sialyl Lewis X (sLeX) and Sialyl Lewis A (sLeA) is frequently upregulated, promoting tumor metastasis by facilitating the binding of cancer cells to vascular selectins (Nature Reviews Cancer, 2020). Beyond oncology, fucosylated glycans are involved in inflammatory disorders and serve as receptors for various pathogens, including Helicobacter pylori and noroviruses (Cell Host & Microbe, 2018). Therapeutic interventions targeting these glycans include glycomimetic inhibitors like uproleselan, which blocks E-selectin binding, and fucosyltransferase inhibitors designed to reduce the synthesis of these pro-metastatic structures (Journal of Medicinal Chemistry, 2021).

Other names

Fucose-containing glycansFucosylated oligosaccharidesLewis antigensH-antigenSecretor antigensFucosylated epitopes

Inhibition of fucosyltransferase activity to prevent glycan synthesis, and competitive antagonism of glycan-binding proteins such as selectins to prevent cell adhesion.