JBC Transcription and Nuclear Factor Monoclonals

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Originally published In Press as doi:10.1074/jbc.M208886200 on November 20, 2002

J. Biol. Chem., Vol. 278, Issue 5, 3063-3071, January 31, 2003
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Differential Roles of Two N-Acetylgalactosaminyltransferases, CSGalNAcT-1, and a Novel Enzyme, CSGalNAcT-2
INITIATION AND ELONGATION IN SYNTHESIS OF CHONDROITIN SULFATE*

Takashi SatoDagger , Masanori GotohDagger §, Katsue KiyoharaDagger , Tomohiro AkashimaDagger , Hiroko IwasakiDagger §, Akihiko KameyamaDagger §, Hideo MochizukiDagger , Toshikazu Yada||, Niro InabaDagger **, Akira TogayachiDagger , Takashi KudoDagger Dagger Dagger , Masahiro Asada§§, Hideto Watanabe||, Toru Imamura§§, Koji Kimata||, and Hisashi NarimatsuDagger ¶¶

From the Dagger  Glycogene Function Team, Research Center for Glycoscience, National Institute of Advanced Industrial Science and Technology (AIST), Open Space Laboratory C-2, 1-1-1 Umezono, Tsukuba, Ibaraki 305-8568, Japan, § Amersham Biosciences KK, 3-25-1, Hyakunincho, Shinjuku-ku, Tokyo 169-0073, Japan, the  Seikagaku Corporation, 1253 Tateno 3-Chome, Higashi-yamato, Tokyo 207-0021, Japan, the || Institute for Molecular Science of Medicine, Aichi Medical University, Nagaute, Aichi 480-1195, Japan, ** JGS Japan Genome Solutions, Inc., 51 Kamiyacho, Hachioji, Tokyo 192-0031, Japan, the §§ Cell Regulation Team, Age Dimension Research Center, AIST, 1-1-1 Higashi, Tsukuba, Ibaraki 305-8566, Japan, the Dagger Dagger  New Energy and Industrial Technology Development Organization (NEDO), Sunshine 60 Bldg., 3-1-1 Higashi Ikebukuro, Toshima-ku Tokyo, 170-6028, Japan

By a tblastn search with beta 1,4-galactosyltransferases as query sequences, we found an expressed sequence tag that showed similarity in beta 1,4-glycosyltransferase motifs. The full-length complementary DNA was obtained by a method of 5'-rapid amplification of complementary DNA ends. The predicted open reading frame encodes a typical type II membrane protein comprising 543 amino acids, the sequence of which was highly homologous to chondroitin sulfate N-acetylgalactosaminyltransferase (CSGalNAcT-1), and we designated this novel enzyme CSGalNAcT-2. CSGalNAcT-2 showed much stronger N-acetylgalactosaminyltransferase activity toward glucuronic acid of chondroitin poly- and oligosaccharides, and chondroitin sulfate poly- and oligosaccharides with a beta 1-4 linkage, i.e. elongation activity for chondroitin and chondroitin sulfate, but showed much weaker activity toward a tetrasaccharide of the glycosaminoglycan linkage structure (GlcA-Gal-Gal-Xyl-O-methoxyphenyl), i.e. initiation activity, than CSGalNAcT-1. Transfection of the CSGalNAcT-1 gene into Chinese hamster ovary cells yielded a change of glycosaminoglycan composition, i.e. the replacement of heparan sulfate on a syndecan-4/fibroblast growth factor-1 chimera protein by chondroitin sulfate, however, transfection of the CSGalNAcT-2 gene did not. The above results indicated that CSGalNAcT-1 is involved in the initiation of chondroitin sulfate synthesis, whereas CSGalNAcT-2 participates mainly in the elongation, not initiation. Quantitative real-time PCR analysis revealed that CSGalNAcT-2 transcripts were highly expressed in the small intestine, leukocytes, and spleen, however, both CSGalNAcTs were ubiquitously expressed in various tissues.

* This work was performed as part of the R&D Project of Industrial Science and Technology Frontier Program (R&D for Establishment and Utilization of a Technical Infrastructure for Japanese Industry) supported by the New Energy and Industrial Technology Development Organization (NEDO).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 sequence(s) reported in this paper has been submitted to the GenBankTM/EBI Data Bank with accession number(s) AB079252.

¶¶ To whom correspondence should be addressed: Glycogene Function Team, Research Center for Glycoscience (RCG), National Institute of Advanced Industrial Science and Technology (AIST), Central-2 C-2, 1-1-1 Umezono, Tsukuba, Ibaraki 305-8568, Japan. Tel.: 81-298-61-3200; Fax: 81-298-61-3201; E-mail: h.narimatsu@aist.go.jp.

Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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