Beta-1,3-N-acetylgalactosaminyltransferase 2 (B3GALNT2)

Beta-1,3-N-acetylgalactosaminyltransferase 2 (B3GALNT2) is an enzyme and member of the glycosyltransferase 31 family that synthesizes GalNAc-beta-1,3GlcNAc, a unique carbohydrate structure found on N- and O-glycans[1][2]. B3GALNT2 is essential for the glycosylation of certain proteins, most notably alpha-dystroglycan, a process crucial for cellular interactions with the extracellular matrix and for the binding of laminin G-like domain-containing proteins[2]. Mutations in the B3GALNT2 gene cause muscular dystrophy-dystroglycanopathy with severe brain and eye anomalies (MDDGA11)[1][2]. The enzyme is overexpressed in several cancer types, including breast cancer and hepatocellular carcinoma, where it promotes tumor cell growth and survival, partly by regulating apoptosis and cell proliferation[3][6]. Overexpression also correlates with increased recruitment of pro-tumor immune cells in the tumor microenvironment[6]. B3GALNT2 is therefore under investigation as both a potential therapeutic target and a diagnostic/prognostic biomarker in oncology[3][6]. No drugs are currently approved targeting B3GALNT2, but inhibition of its enzymatic activity is under research as a strategy for molecular therapy in select cancers[3].

Other names

Beta-1,3-GalNAc-T2MGC39558Beta-1,3-N-acetylgalactosaminyltransferase IIB3GalNAc-T2MDDGA11UDP-GalNAc:beta-1,3-N-acetylgalactosaminyltransferase 2UDP-GalNAc:betaGlcNAc beta-1,3-galactosaminyltransferase, polypeptide 2B3GALNT2

Targeted inhibition (potential, via suppression of glycosyltransferase activity leading to reduced proliferation and increased apoptosis in certain cancers)