Galactose-containing glycans

Galactose-containing glycans are complex carbohydrate structures covalently attached to proteins or lipids, characterized by the presence of galactose residues, often in terminal positions or within N-acetyllactosamine (LacNAc) repeats. These glycans serve as the primary biological ligands for galectins, a family of animal lectins that modulate cell signaling, adhesion, and immune responses by cross-linking glycans into functional surface lattices (Barondes et al., 1994; Johannes et al., 2018). In pathological states such as cancer, fibrosis, and chronic inflammation, alterations in the branching and density of these glycans—often referred to as the glycome—drive disease progression by altering cell-cell interactions and promoting immune evasion (Pinho & Reis, 2015). Therapeutic strategies targeting these glycans primarily involve the development of galectin inhibitors, such as Belapectin (GR-MD-02) and GB1211, which competitively block the carbohydrate-recognition domains of galectins to prevent their binding to endogenous galactose-containing motifs (Traber et al., 2013). Additionally, the high-affinity interaction between terminal galactose/N-acetylgalactosamine (GalNAc) and the hepatic asialoglycoprotein receptor (ASGPR) is exploited for the targeted delivery of siRNA and antisense oligonucleotide drugs, such as Givosiran and Inclisiran, to hepatocytes (Nair et al., 2014). Furthermore, specific tumor-associated galactose-containing glycans, such as the GD2 ganglioside, are directly targeted by monoclonal antibodies like Dinutuximab in oncology (Yu et al., 2010).

Other names

Galactosylated glycansGalactansBeta-galactosidesN-acetyllactosamine (LacNAc) sequencesTerminal galactose residues

Competitive inhibition of galectin-glycan binding, antibody-mediated targeting of tumor-associated carbohydrate antigens, and ASGPR-mediated hepatic uptake.