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J. Biol. Chem., Vol. 279, Issue 4, 2337-2340, January 23, 2004

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ACCELERATED PUBLICATIONS

N-Acetylglucosaminyltransferase IX Acts on the GlcNAc1,2-Man1-Ser/Thr Moiety, Forming a 2,6-Branched Structure in Brain O-Mannosyl Glycan^*

Kei-ichiro Inamori, Takeshi Endo, Jianguo Gu, Ichiro Matsuo, Yukishige Ito, Shigeru Fujii¶, Hiroko Iwasaki||, Hisashi Narimatsu||, Eiji Miyoshi, Koichi Honke**, and Naoyuki Taniguchi

From the Department of Biochemistry, Osaka University Medical School, 2-2 Yamadaoka, Suita, Osaka 565-0871, Japan, the RIKEN (The Institute of Physical and Chemical Research), 2-1 Hirosawa, Wako-shi, Saitama 351-0198, Japan, the ^¶Laboratory of Chemistry, Kansai Medical University, 18-89 Uyama-Higashi, Hirakata, Osaka 573-1136, Japan, the ^||Glycogene Function Team, Research Center for Glycoscience, National Institute of Advanced Industrial Science and Technology, Open Space Laboratory C-2, 1-1-1 Umezono, Tsukuba, Ibaraki 305-8568, Japan, and the ^**Department of Molecular Genetics, Kochi Medical School, Kohasu, Oko-cho, Nankoku, Kochi 783-8505, Japan

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 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-pyridylaminoethylsuccinamyl (PAES). 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.

Received for publication, October 31, 2003 , and in revised form, November 13, 2003.

^* This work was supported by the New Energy and Industrial Technology Development Organization (NEDO) as a part of Biotechnology Foundation Research Program for Health Maintenance and Improvement and by a Grant-in-aid for Scientific Research (S) No. 13854010 from the Japan Society for the promotion of Science and by the 21st Century COE Program by the Ministry of Education, Science, Culture, Sports and Technology in Japan. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence may be addressed. Tel.: 81-88-880-2313; Fax: 81-88-880-2314; E-mail: khonke{at}med.kochi-ms.ac.jp. To whom correspondence may be addressed. Tel.: 81-6-6879-3420; Fax: 81-6-6879-3429; E-mail: proftani{at}biochem.med.osaka-u.ac.jp.

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