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Terminal β-galactose-containing glycans are essential carbohydrate motifs located at the non-reducing ends of oligosaccharide chains on cell-surface glycoproteins and glycolipids (Varki et al., Essentials of Glycobiology, 2017). These glycans serve as the primary ligands for galectins, a family of evolutionary conserved lectins that regulate a wide array of biological processes including cell adhesion, apoptosis, and immune cell activation (Johannes et al., Journal of Cell Science, 2018). In many diseases, particularly cancer and organ fibrosis, the density and branching of these terminal galactose residues are significantly altered, leading to the formation of galectin-glycan lattices that promote tumor immune evasion and tissue remodeling (Thiemann and Baum, Nature Reviews Immunology, 2016). Therapeutic intervention focuses on using glycomimetic drugs or competitive inhibitors, such as Belapectin or GB1211, that occupy the carbohydrate-recognition domains of galectins, thereby preventing their interaction with terminal β-galactose residues (Galecto, 2023; Galectin Therapeutics, 2023). This approach aims to restore normal immune surveillance and inhibit the pro-fibrotic or pro-metastatic signaling pathways driven by aberrant glycan presentation.
Competitive inhibition of galectin binding to terminal beta-galactoside residues, preventing the formation of galectin-glycan lattices and subsequent signaling.
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