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J. Biol. Chem., Vol. 278, Issue 44, 43102-43109, October 31, 2003

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Molecular Cloning and Characterization of Human GnT-IX, a Novel 1,6-N-Acetylglucosaminyltransferase That Is Specifically Expressed in the Brain^*

Kei-ichiro Inamori, Takeshi Endo, Yoshihito Ide, Shigeru Fujii, Jianguo Gu, Koichi Honke¶||, and Naoyuki Taniguchi

From the Department of Biochemistry, Osaka University Medical School, 2-2 Yamadaoka, Suita, Osaka 565-0871, Japan, the Laboratory of Chemistry, Kansai Medical University, 18-89 Uyama-Higashi, Hirakata, Osaka 573-1136, Japan, and the ^¶Department of Molecular Genetics, Kochi Medical School, Kohasu, Oko-cho, Nankoku, Kochi 783-8505, Japan

A novel 1,6-N-acetylglucosaminyltransferase (1, 6GnT) cDNA was identified by a BLAST search using the amino acid sequence of human GnT-V as a query. The full-length sequence was determined by a combination of 5'-rapid amplification of cDNA end analysis and a further data base search. The open reading frame encodes a 792 amino acid protein with a type II membrane protein structure typical of glycosyltransferases. The entire sequence identity to human GnT-V is 42%. When pyridylaminated (PA) agalacto biantennary N-linked oligosaccharide was used as an acceptor substrate, the recombinant enzyme generated a novel product other than the expected GnT-V product, (GlcNAc1,2-Man1,3-)[GlcNAc1,2-(GlcNAc1,6-)Man1,6-]Man1,4-GlcNAc1,4-GlcNAc-PA. This new product was identified as [GlcNAc1,2-(GlcNAc1,6-)Man1,3-][Glc-NAc1,2-(GlcNAc1,6-)Man1,6-]Man1,4-GlcNAc1,4-GlcNAc-PA by mass spectrometry and ¹H NMR. Namely, the new GnT (designated as GnT-IX) has 1,6GnT activity not only to the 1,6-linked mannose arm but also to the 1,3-linked mannose arm of N-glycan, forming a unique structure that has not been reported to date. Northern blot analysis showed that the GnT-IX gene is exclusively expressed in the brain, whereas the GnT-V gene is expressed ubiquitously. These results suggest that GnT-IX is responsible for the synthesis of a unique oligosaccharide structure in the brain.

Received for publication, July 29, 2003 , and in revised form, August 21, 2003.

The nucleotide sequence(s) reported in this paper has been submitted to the DDBJ/GenBank^TM/EBI Data Bank with accession number(s) AB109185.

^* This work was supported by the New Energy and Industrial Technology Development Organization as a part of Biotechnology Foundation Research Program for Health Maintenance and Improvement and by a Grant-in-aid for Scientific Research (S) 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 should be addressed. Tel.: 81-88-880-2313; Fax: 81-88-880-2314; E-mail: khonke{at}med.kochi-ms.ac.jp.

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