Characterization of a novel mucin sulphotransferase activity synthesizing sulphated O-glycan core 1, 3-sulphate-Galβ1-3GalNAcα-R

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Abstract
A novel sulphotransferase (sulpho-T) activity from rat colonic mucosa was characterized using O-glycan core 1 substrate, Galβ1-3GalNAcα-benzyl. Derivatives of Galβ1-3GalNAc- were used to demonstrate that the 3- and 4-hydroxyl of Gal and the 2-acetamido group of the GalNAc residue of Galβ1-3GalNAcα-benzyl substrates were important for activity. Sulphated product using Galβ1-3GalNAcα-benzyl as substrate was analysed by ion spray mass spectrometry, methylation analysis, high-pH anion-exchange chromatography and β-galactosidase digestion. The results suggested that sulphate was added to the 3-position of the Gal residue. The synthesis of core 2 from core 1 by UDP-GlcNAc: Galβ1-3GalNAc36-GlcNAc-trans-ferase was inhibited by sulphation of the Gal residue, indicating that GlcNAcβ1-6 branching has to precede sulphation in the O-glycan core 1 processing pathway. These data demonstrate several novel pathways in the synthesis of sulphated mucin-type oligosaccharides.

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