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 GalNAcresidue of Galβ1-3GalNAcα-benzyl substrates were important for activity. Sulphated prouctusing Galβ1-3GalNAcα-benzyl as substrate was analysed by ion spray mass spectrometry, methylation analysis, high-pH anion-exchange chromatography and β-galactosidase digestion. Theresults suggested that sulphate was added to the 3-position of the Gal residue. The synthesis of core2 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.
| Original language | English |
|---|---|
| Pages (from-to) | 689-697 |
| Number of pages | 9 |
| Journal | Glycobiology |
| Volume | 5 |
| Issue number | 7 |
| DOIs | |
| State | Published - Oct 1995 |
Keywords
- Colonic tissue
- Mucin
- Mucin biosynthesis
- O-glycans
- Sulphotransferases
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