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Originally published In Press as doi:10.1074/jbc.M004800200 on October 19, 2000

J. Biol. Chem., Vol. 276, Issue 5, 3498-3507, February 2, 2001
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Identification and Characterization of Three Novel beta 1,3-N-Acetylglucosaminyltransferases Structurally Related to the beta 1,3-Galactosyltransferase Family*

Norihiko ShiraishiDagger §, Ayumi NatsumeDagger §, Akira Togayachi||, Tetsuo EndoDagger , Tomohiro Akashima**, Yoji YamadaDagger , Nobuyuki ImaiDagger , Satoshi NakagawaDagger , Satoshi KoizumiDagger , Susumu SekineDagger , Hisashi Narimatsu, and Katsutoshi SasakiDagger Dagger Dagger

From the Dagger  Tokyo Research Laboratories, Kyowa Hakko Kogyo Company, Limited, 3-6-6 Asahi-machi, Machida-shi, Tokyo 194-8533, the  Division of Cell Biology, Institute of Life Science, Soka University, 1-236 Tangi-cho, Hachioji, Tokyo 192-8577, the || Laboratory of Cancer Biology and Molecular Immunology, Graduate School of Pharmaceutical Sciences, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113, and the ** Laboratory of Animal Resources, Faculty of Bioindustry, Tokyo University of Agriculture, 196 Aza-Yasaka, Abashiri-shi, Hokkaido 099-2422, Japan

We have isolated three types of cDNAs encoding novel beta 1,3-N-acetylglucosaminyltransferases (designated beta 3Gn-T2, -T3, and -T4) from human gastric mucosa and the neuroblastoma cell line SK-N-MC. These enzymes are predicted to be type 2 transmembrane proteins of 397, 372, and 378 amino acids, respectively. They share motifs conserved among members of the beta 1,3-galactosyltransferase family and a beta 1,3-N-acetylglucosaminyltransferase (designated beta 3Gn-T1), but show no structural similarity to another type of beta 1,3-N-acetylglucosaminyltransferase (iGnT). Each of the enzymes expressed by insect cells as a secreted protein fused to the FLAG peptide showed beta 1,3-N-acetylglucosaminyltransferase activity for type 2 oligosaccharides but not beta 1,3-galactosyltransferase activity. These enzymes exhibited different substrate specificity. Transfection of Namalwa KJM-1 cells with beta 3Gn-T2, -T3, or -T4 cDNA led to an increase in poly-N-acetyllactosamines recognized by an anti-i-antigen antibody or specific lectins. The expression profiles of these beta 3Gn-Ts were different among 35 human tissues. beta 3Gn-T2 was ubiquitously expressed, whereas expression of beta 3Gn-T3 and -T4 was relatively restricted. beta 3Gn-T3 was expressed in colon, jejunum, stomach, esophagus, placenta, and trachea. beta 3Gn-T4 was mainly expressed in brain. These results have revealed that several beta 1,3-N-acetylglucosaminyltransferases form a family with structural similarity to the beta 1,3-galactosyltransferase family. Considering the differences in substrate specificity and distribution, each beta 1,3-N-acetylglucosaminyltransferase may play different roles.

* The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide sequences reported in this paper have been submitted to the DDBJ/GenBankTM/EBI Data Bank with accession numbers AB049584 (beta 3Gn-T2), AB049585 (beta 3Gn-T3), and AB049586 (beta 3Gn-T4).

§ These authors contributed equally to this work and should be considered as first authors.

Dagger Dagger To whom correspondence should be addressed. Tel.: 81-427-25-2555; Fax: 81-427-26-8330; E-mail: ksasaki@kyowa.co.jp.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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