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Papers In Press, published online ahead of print November 14, 2003
Biochemistry, Osaka University Medical School, Suita, Osaka 565-0871
Corresponding Author: proftani{at}biochem.med.osaka-u.ac.jp
Mammals contain O-linked mannose residues with 2-mono- and 2,6-di-substitutions by GlcNAc in brain glycoproteins. It has been demonstrated that the transfer of GlcNAc to the 2-OH position of the mannose residue is catalyzed by the enzyme, protein O-mannose
J. Biol. Chem, 10.1074/jbc.C300480200
Submitted on October 31, 2003
Revised on November 13, 2003
Accepted on November 14, 2003
N-acetylglucosaminyltransferase IX acts on the GlcNAc
1,2-Man
1-Ser/Thr moiety, forming a 2,6-branched structure in brain O-mannosyl glycan
1,2-N-acetylglucosaminyltransferase (POMGnT1), but the enzymatic basis of the transfer to the 6-OH position is unknown. We recently reported on a brain-specific 1,6-N-acetylglucosaminyltransferase, GnT-IX, that catalyzes the transfer of GlcNAc to the 6-OH position of the mannose residue of GlcNAc1,2-Man
on both the 1,3- and 1,6-linked mannose arms in the core structure of N-glycan (Inamori, K., Endo, T., Ide, Y., Fujii, S., Gu, J., Honke, K., and Taniguchi, N. (2003), J. Biol. Chem. 278, 43102-43109). Here we examined the issue of whether GnT-IX is able to act on the same sequence of the GlcNAc1,2-Man in O-mannosyl glycan. Using three synthetic Ser-linked mannose-containing saccharides: Man1-Ser, GlcNAc1,2-Man1-Ser, and Gal1,4-GlcNAc1,2-Man1-Ser as acceptor substrates, the findings show that [14C]-labeled GlcNAc was incorporated only into GlcNAc1,2-Man1-Ser, after separation by thin layer chromatography. To simplify the assay, high performance liquid chromatography was employed, using a fluorescence-labeled acceptor substrate GlcNAc1,2-Man1-Ser-PAES (pyridylaminoethylsuccinamyl). Consistent with the above data, GnT-IX generated a new product which was identified as GlcNAc1,2-(GlcNAc1,6-)Man1-Ser-PAES by mass spectrometry and 1H-NMR. Furthermore, incorporation of an additional GlcNAc residue into a synthetic mannosyl peptide Ac-Ala-Ala-Pro-Thr(Man)-Pro-Val-Ala-Ala-Pro-NH2 by GnT-IX was only observed in the presence of POMGnT1. Collectively, these results strongly suggest that GnT-IX may be a novel 1,6-N-acetylglucosaminyltransferase that is responsible for the formation of the 2,6-branched structure in the brain O-mannosyl glycan.
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