HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) An addition or correction has been published Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Shimoda, Y. Articles by Sanai, Y. Search for Related Content PubMed PubMed Citation Articles by Shimoda, Y. Articles by Sanai, Y.

J Biol Chem, Vol. 274, Issue 24, 17115-17122, June 11, 1999

Cloning and Expression of a Novel Galactoside 1,3-Glucuronyltransferase Involved in the Biosynthesis of HNK-1 Epitope

Yasushi Shimoda, Youichi Tajima, Takashi Nagase^§¶, Kiyonori Harii^¶, Noriko Osumi^§, and Yutaka Sanai

From the  Department of Biochemical Cell Research, Tokyo Metropolitan Institute of Medical Science (RINSHOKEN), Tokyo 113-8613, Japan, the ^¶ Department of Plastic and Reconstructive Surgery, Graduate School of Medicine, University of Tokyo, Tokyo 113-0033, Japan, and the ^§ Division of Biochemistry and Cell Biology, National Institute of Neuroscience, National Center of Neurology and Psychiatry, 4-1-1 Ogawahigashi, Kodaira, Tokyo 187-8502, Japan

We isolated a cDNA encoding a novel glucuronyltransferase, designated GlcAT-D, involved in the biosynthesis of the HNK-1 carbohydrate epitope from rat embryo cDNA by the degenerate polymerase chain reaction method. The new cDNA sequence revealed an open reading frame coding for a protein of 324 amino acids with type II transmembrane protein topology. The amino acid sequence of GlcAT-D displayed 50.0% identity to rat GlcAT-P, which is involved in the biosynthesis of the HNK-1 epitope on glycoproteins. Expression of GlcAT-D in COS-7 cells resulted in the formation of the HNK-1 epitope on the cell surface. The enzyme expressed in COS-7 cells transferred a glucuronic acid (GlcA) not only to asialo-orosomucoid, a glycoprotein bearing terminal N-acetyllactosamine structure, but also to paragloboside (lacto-N-neotetraosylceramide), a precursor of the HNK-1 epitope on glycolipids. Furthermore, substrate specificity analysis using a soluble chimeric form of GlcAT-D revealed that GlcAT-D transfers a GlcA not only to Gal1-4GlcNAc1-3Gal1-4Glc-pyridylamine but also to Gal1-3GlcNAc1-3Gal1-4Glc-pyridylamine. Enzymatic hydrolysis and Smith degradation of the reaction product indicated that GlcAT-D transfers a GlcA through a 1,3-linkage to a terminal galactose. The GlcAT-D transcripts were detected in embryonic, postnatal, and adult rat brain. In situ hybridization analysis revealed that the expression pattern of GlcAT-D transcript in embryo is similar to that of GlcAT-P, but distinct expression of GlcAT-D was observed in the embryonic pallidum and retina. Regions that expressed GlcAT-D and/or GlcAT-P were always HNK-1-positive, indicating that both GlcATs are involved in the synthesis of the HNK-1 epitope in vivo.

---

Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.

This article has been cited by other articles:

				S. Kakuda, Y. Sato, Y. Tonoyama, S. Oka, and T. Kawasaki Different acceptor specificities of two glucuronyltransferases involved in the biosynthesis of HNK-1 carbohydrate Glycobiology, February 1, 2005; 15(2): 203 - 210. [Abstract] [Full Text] [PDF]

				S. Sawada, H. Suzuki, F. Ichimaida, M.-a. Yamaguchi, T. Iwashita, Y. Fukui, H. Hemmi, T. Nishino, and T. Nakayama UDP-glucuronic Acid:Anthocyanin Glucuronosyltransferase from Red Daisy (Bellis perennis) Flowers: ENZYMOLOGY AND PHYLOGENETICS OF A NOVEL GLUCURONOSYLTRANSFERASE INVOLVED IN FLOWER PIGMENT BIOSYNTHESIS J. Biol. Chem., January 14, 2005; 280(2): 899 - 906. [Abstract] [Full Text] [PDF]

				K.-i. Inamori, T. Endo, J. Gu, I. Matsuo, Y. Ito, S. Fujii, H. Iwasaki, H. Narimatsu, E. Miyoshi, K. Honke, et al. N-Acetylglucosaminyltransferase IX Acts on the GlcNAc{beta}1,2-Man{alpha}1-Ser/Thr Moiety, Forming a 2,6-Branched Structure in Brain O-Mannosyl Glycan J. Biol. Chem., January 23, 2004; 279(4): 2337 - 2340. [Abstract] [Full Text] [PDF]

				X. Wu, S.-T. Pang, L. Sahlin, A. Blanck, G. Norstedt, and A. Flores-Morales Gene Expression Profiling of the Effects of Castration and Estrogen Treatment in the Rat Uterus Biol Reprod, October 1, 2003; 69(4): 1308 - 1317. [Abstract] [Full Text] [PDF]

				B.-T. Kim, K. Tsuchida, J. Lincecum, H. Kitagawa, M. Bernfield, and K. Sugahara Identification and Characterization of Three Drosophila melanogaster Glucuronyltransferases Responsible for the Synthesis of the Conserved Glycosaminoglycan-Protein Linkage Region of Proteoglycans. TWO NOVEL HOMOLOGS EXHIBIT BROAD SPECIFICITY TOWARD OLIGOSACCHARIDES FROM PROTEOGLYCANS, GLYCOPROTEINS, AND GLYCOSPHINGOLIPIDS J. Biol. Chem., March 7, 2003; 278(11): 9116 - 9124. [Abstract] [Full Text] [PDF]

				M. NAGASE, S. KANAME, T. NAGASE, G. WANG, K. ANDO, T. SAWAMURA, and T. FUJITA Expression of LOX-1, an Oxidized Low-Density Lipoprotein Receptor, in Experimental Hypertensive Glomerulosclerosis J. Am. Soc. Nephrol., October 1, 2000; 11(10): 1826 - 1836. [Abstract] [Full Text]

				D. A. Bulik, G. Wei, H. Toyoda, A. Kinoshita-Toyoda, W. R. Waldrip, J. D. Esko, P. W. Robbins, and S. B. Selleck sqv-3, -7, and -8, a set of genes affecting morphogenesis in Caenorhabditis elegans, encode enzymes required for glycosaminoglycan biosynthesis PNAS, September 26, 2000; 97(20): 10838 - 10843. [Abstract] [Full Text] [PDF]

				Y. Shimoda, Y. Tajima, T. Osanai, A. Katsume, M. Kohara, T. Kudo, H. Narimatsu, N. Takashima, Y. Ishii, S. Nakamura, et al. Pax6 Controls the Expression of Lewis x Epitope in the Embryonic Forebrain by Regulating alpha 1,3-Fucosyltransferase IX Expression J. Biol. Chem., January 11, 2002; 277(3): 2033 - 2039. [Abstract] [Full Text] [PDF]