Cell-surface glycans bearing D-galactose (Gal-glycans)

Cell-surface glycans bearing D-galactose are complex carbohydrate structures attached to proteins (glycoproteins) or lipids (glycolipids) on the plasma membrane, characterized by terminal or accessible galactose residues (Varki et al., Essentials of Glycobiology, 2017). These glycans serve as critical recognition motifs for endogenous lectins, particularly the galectin family, which regulate diverse biological processes including cell adhesion, immune cell activation, and apoptosis (Johannes et al., J Cell Sci, 2018). In pathological states such as cancer and chronic fibrosis, the expression and branching of these galactose-bearing glycans are often altered, promoting tumor metastasis, immune evasion, and tissue remodeling (Pinho & Reis, Nat Rev Cancer, 2015). Therapeutic strategies targeting these glycans typically involve galectin inhibitors, such as Belapectin, which mimic the galactose structure to block protein-glycan interactions (Blanchard et al., Chem Rev, 2022). Additionally, the galactose motif is exploited for targeted drug delivery to the liver via the asialoglycoprotein receptor (ASGPR), which specifically recognizes and internalizes galactose-terminated glycoconjugates (D'Souza & Devarajan, J Control Release, 2015).

Other names

Galactose-terminated glycansGalactosyl-glycansTerminal D-galactose residuesGalactose-containing cell surface carbohydratesGalactosylated glycoconjugates

Competitive inhibition of galectin binding to terminal galactose residues, thereby modulating galectin-mediated lattice formation, cell signaling, and adhesion (Blanchard et al., 2022).