Galectin-3 and Galectin-8 (Gal-3/Gal-8)

Galectin-3 and Galectin-8 are soluble carbohydrate-binding proteins belonging to the galectin family, characterized by their affinity for beta-galactosides (UniProt P17931; UniProt O00214). Galectin-3 is a chimera-type protein that acts as a critical mediator in fibrosis, inflammation, and cancer progression by cross-linking glycoproteins on the cell surface (PubMed: 24508530). Galectin-8 is a tandem-repeat galectin that serves as a vital sensor for endosomal damage and regulates cell adhesion and autophagy (PubMed: 22246324). In various diseases, including nonalcoholic steatohepatitis (NASH), idiopathic pulmonary fibrosis, and metastatic cancer, these proteins are upregulated and contribute to pathological remodeling and immune evasion (PubMed: 30103529). Pharmacological intervention typically focuses on small-molecule or polysaccharide inhibitors that target the carbohydrate-recognition domains (CRDs) of these proteins to block their interaction with ligands. Clinical-stage candidates like Belapectin and GB1211 aim to mitigate fibrotic and oncogenic signaling by selectively or potently inhibiting these galectins (Galectin Therapeutics; Galecto Biotech).

Other names

LGALS3LGALS8Mac-2 antigenL-31GalaptinCBP35PCTAIRE-binding protein 1Po66-CBP

Competitive inhibition of the carbohydrate-recognition domain (CRD) to prevent binding to beta-galactoside-containing glycoconjugates (PubMed: 30103529).