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Glycan epitopes on vascular surfaces are specific carbohydrate structures (often terminally sialylated glycans) embedded in the cell membrane glycocalyx of endothelial cells, glycolipids, glycoproteins, and proteoglycans[1][4]. These motifs mediate cell–cell interactions, prevent unwanted adhesion (e.g., erythrocytes), and facilitate recognition by endogenous and exogenous glycan-binding proteins including immune cells and pathogens[1][2][4]. Their composition and presentation regulate vascular barrier integrity, immune responses, and pathological processes like cancer metastasis (via hypersialylation) and inflammation[4][2]. While not traditional therapeutic targets, modulation of vascular glycan epitopes is being explored for disease intervention, especially in cancer, infection, and inflammation[1][4]. Their complexity and diversity make them challenging as direct drug targets compared to classical receptors or enzymes.
Desialylation to modulate cell–cell or immune interactions (e.g., neuraminidase enzymes) Blocking glycan recognition by glycan-binding proteins (lectin antagonists) Modulating glycan presentation on vascular surfaces to regulate adhesion, immune cell binding, and clearance
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