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J. Biol. Chem., Vol. 278, Issue 41, 39711-39725, October 10, 2003

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Chondroitin Sulfate Synthase-3

MOLECULAR CLONING AND CHARACTERIZATION^*

Toshikazu Yada   ¶, Takashi Sato ¶ ||, Hiromi Kaseyama  , Masanori Gotoh || **, Hiroko Iwasaki || **, Norihiro Kikuchi || , Yeon-Dae Kwon ||, Akira Togayachi || , Takashi Kudo ||, Hideto Watanabe , Hisashi Narimatsu || and Koji Kimata  ¶¶

From the Institute for Molecular Science of Medicine, Aichi Medical University, Nagakute, Aichi 480-1195, Seikagaku Corp., 1253 Tateno 3-Chome, Higashiyamato, Tokyo 207-0021, ^||Laboratory of Gene Function Analysis, Institute of Molecular and Cell Biology, National Institute of Advanced Industrial Science and Technology, OSL C-2, 1-1-1 Umezono, Tsukuba, Ibaraki 305-8568, ^**Amersham Biosciences KK, 3-25-1, Hyakunincho, Shinjuku-ku, Tokyo 169-0073, Mitsui Knowledge Industry Co., Ltd., 2-7-14 Higashinakano, Nakano, Tokyo 164-8555, and New Energy and Industrial Technology Development Organization, Sunshine 60 Building, 3-1-1 Higashi Ikebukuro, Toshima-ku, Tokyo 170-6028, Japan

Recently, it has become evident that chondroitin sulfate (CS) glycosyltransferases, which transfer glucuronic acid and/or N-acetylgalactosamine residues from each UDP-sugar to the nonreducing terminus of the CS chain, form a gene family. We report here a novel human gene (GenBank^TM accession number AB086062) that possesses a sequence homologous with the human chondroitin sulfate synthase-1 (CSS1) gene, formerly known as chondroitin synthase. The full-length open reading frame consists of 882 amino acids and encodes a typical type II membrane protein. This enzyme contains a 3-glycosyltransferase motif and a 4-glycosyltransferase motif similar to that found in CSS1. Both the enzymes were expressed in COS-7 cells as soluble proteins, and their enzymatic natures were characterized. Both glucuronyltransferase and N-acetylgalactosaminyltransferase activities were observed when chondroitin, CS polymer, and their corresponding oligosaccharides were used as the acceptor substrates, but no polymerization reaction was observed as in the case of CSS1. The new enzyme was thus designated chondroitin sulfate synthase-3 (CSS3). However, the specific activity of CSS3 was much lower than that of CSS1. The reaction products were shown to have a GlcUA1–3GalNAc linkage and a GalNAc1–4GlcUA linkage in the nonreducing terminus of chondroitin resulting from glucuronyltransferase activity and N-acetylgalactosaminyltransferase activity, respectively. Quantitative real time PCR analysis revealed that the transcript level of CSS3 was much lower than that of CSS1, although it was ubiquitously expressed in various human tissues. These results indicate that CSS3 is a glycosyltransferase having both glucuronyltransferase and N-acetylgalactosaminyltransferase activities. It may make a contribution to CS biosynthesis that differs from that of CSS1.

Received for publication, April 28, 2003 , and in revised form, August 5, 2003.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EBI Data Bank with accession number(s) AB086062.

^* This work was performed as part of the R & D Project of the 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. 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.

^¶ Both authors contributed equally to this work.

^¶¶ To whom correspondence should be addressed. Tel.: 81-561-62-3311; Fax: 81-561-63-3532; E-mail: kimata{at}aichi-med-u.ac.jp.

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