Cell-surface glycans bearing terminal galactose

Cell-surface glycans bearing terminal galactose are carbohydrate structures where a galactose residue occupies the non-reducing end of the glycan chain. These residues are typically exposed when terminal sialic acids are removed by neuraminidases, a process known as desialylation, which serves as a biological clock for protein clearance (Ashwell & Harford, 1982). The primary physiological receptor for these glycans is the asialoglycoprotein receptor (ASGPR) on hepatocytes, which mediates the endocytosis and degradation of desialylated glycoproteins (D'Souza & Devarajan, 2015). In oncology and chronic inflammation, altered glycosylation leads to an abundance of terminal galactose, which interacts with galectins to promote tumor progression, metastasis, and immune evasion (Pinho & Reis, 2015). Therapeutic strategies include the use of galectin inhibitors like Belapectin to block these interactions, as well as the exploitation of the ASGPR for liver-specific delivery of GalNAc-conjugated oligonucleotides (Nair et al., 2014; Zhou et al., 2018). Consequently, these glycans are pivotal in both natural protein homeostasis and the development of targeted therapeutic platforms.

Other names

Terminal galactose residuesGalactose-terminated glycansDesialylated glycansAsialoglycansBeta-galactoside-terminated glycans

Competitive inhibition of galectin binding to terminal galactose residues on cell-surface glycoproteins or utilization as a recognition motif for receptor-mediated endocytosis.