Core 2 beta-1,6-N-acetylglucosaminyltransferase 1 (GCNT1)

Core 2 beta-1,6-N-acetylglucosaminyltransferase 1 (GCNT1) is a type II membrane-bound Golgi enzyme in the glycosyltransferase family that catalyzes the transfer of N-acetylglucosamine from UDP-GlcNAc onto mucin-type core 1 O-glycans, forming branched core 2 O-glycan structures[2][3][5]. These branched glycans are key scaffolds for selectin ligands (such as sialyl Lewis X) on glycoproteins and glycolipids, which are critical for cell adhesion, immune cell recruitment, and regulation of inflammation[1][2][3]. GCNT1 is overexpressed in several cancers, particularly prostate cancer, where it modulates tumor cell glycosylation, influencing tumor progression, invasion, and metastatic potential[2][3][7]. Disruption or mislocalization of GCNT1 impairs proper glycosylation, altering cellular interactions and potentially increasing susceptibility to infections (e.g., tuberculosis)[6]. Potential as a therapeutic target is being investigated, especially for precision oncology and modulation of glyco-immune pathways[2][7].

Other names

Glucosaminyl (N-acetyl) transferase 1Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferaseCore 2 GnTC2GnT-LNACGT2C2GlcNAcTC2GNTNAGCT2G6NTCore 2-branching enzymeLeukocyte type core 2 beta-1,6-N-acetylglucosaminyltransferase

Inhibition or modulation of GCNT1 would alter O-glycan branching and downstream glycoprotein function, potentially affecting cell adhesion, immune evasion, and metastatic behavior in cancers[2][7].