O-glycan biosynthesis pathways and proposed O-glycan structures of selected glycosyltransferases, overview. Core 1 dominates the O-glycan repertoire. Core 1 can be further elongated by extended C1 beta3GnT3 enzyme to form extended core 1 structure, or be modified by C2 beta6GnT1 enzyme, EC 18.104.22.168, to form core 2 O-glycans. Regulation of O-glycan biosynthesis, overview. The extended C1 beta3GnT3 is competing withthe endogenous ST3Gal
gene B3GNT3, recombinant expression in CHO-K1 cells. Glycosylation-related genes in CHO-K1 cells are present, but strictly suppressed and regulated. CHO cells are transiently co-transfected with plasmids encoding extended C1 beta3GnT3, C2 beta6GnT1, or C3 beta3GnT6 with or without ST6Gal I or CHST4, respectively, and resulting O-glycan and core chain spectrum, overview
Brockhausen, I.; Rachaman, E.S.; Matta, K.L.; Schachter, H.
The separation by liquid chromatography (under elevated pressure) of phenyl, benzyl, and O-nitrophenyl glycosides of oligosaccharides. Analysis of substrates and products for four N-acetyl-D-glucosaminyl-transferases involved in mucin synthesis
Biosynthesis of O-glycans in leukocytes from normal donors and from patients with leukemia: increase in O-glycan core 2 UDP-GlcNAc:Galbeta3GalNAcalpha-R (GlcNAc to GalNAc) beta(1,6)-N-acetylglucosaminyltransferase in leikemic cells