Beta-1,4-galactosyltransferase 3 (B4GALT3)

Beta-1,4-galactosyltransferase 3 (B4GALT3) is an enzyme belonging to a family of beta-1,4-galactosyltransferases responsible for transferring galactose to N-acetylglucosamine in a beta-1,4 linkage, which is a key step in the biosynthesis of glycoproteins and glycolipids. B4GALT3 is a type II membrane protein localized mainly to the Golgi apparatus, containing a catalytic domain and involved in forming poly-N-acetyllactosamine chains. Its expression is implicated in cancer prognosis, tumor immune microenvironment modulation, and immune cell function, particularly altering glycosylation of proteins such as integrin alpha-L (ITGAL) on CD8+ T cells, thereby impacting anti-tumor immunity. B4GALT3 is under investigation as a potential therapeutic target and prognostic biomarker in oncology, with emerging evidence suggesting its inhibition could enhance anti-tumor immune responses with a potentially favorable safety profile[1][3][4].

Other names

Beta-1,4-GalTase 3Beta4Gal-T3beta4Gal-T3Beta-N-acetylglucosaminyl-glycolipid beta-1,4-galactosyltransferaseBeta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferaseN-acetyllactosamine synthaseNal synthaseNeolactotriaosylceramide beta-1,4-galactosyltransferaseUDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 3UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 3epididymis secretory sperm binding protein

Inhibition of B4GALT3 can modulate glycosylation of immune proteins, enhancing CD8+ T cell-mediated anti-tumor activity. Possible intervention via siRNA to reduce B4GALT3 expression in tumors.