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Originally published In Press as doi:10.1074/jbc.M006902200 on September 18, 2000

J. Biol. Chem., Vol. 275, Issue 51, 40498-40503, December 22, 2000
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Expression Cloning of Human Globoside Synthase cDNAs
IDENTIFICATION OF beta 3Gal-T3 AS UDP-N-ACETYLGALACTOSAMINE:GLOBOTRIAOSYLCERAMIDE beta 1,3-N-ACETYLGALACTOSAMINYLTRANSFERASE*

Tetsuya OkajimaDagger ||, Yoko NakamuraDagger , Makoto Uchikawa§, David B. Haslam, Shin-ichiro NumataDagger , Keiko FurukawaDagger , Takeshi UranoDagger , and Koichi FurukawaDagger **

From the Dagger  Department of Biochemistry II, Nagoya University School of Medicine, 65 Tsurumai, Nagoya 466-0065, the § Japanese Red Cross Central Blood Center, Hiroo 4-1-31, Shibuya-ku, Tokyo 150, Japan, and the  Department of Pediatrics, Child Health Research Center of Excellence in Developmental Biology, Washington University School of Medicine, St. Louis, Missouri 63110

By using a eukaryocytic cell expression cloning system, we have isolated cDNAs of the globoside synthase (beta 1,3-N-acetylgalactosaminyltransferase) gene. Mouse fibroblast L cells transfected with SV40 large T antigen and previously cloned Gb3/CD77 synthase cDNAs were co-transfected with a cDNA library prepared from mRNA from human kidney together with Forssman synthase cDNA, and Forssman antigen-positive cells were panned using an anti-Forssman monoclonal antibody. The isolated cDNAs contained a single open reading frame predicting a type II membrane protein with 351 amino acids. Surprisingly, the cDNA clones turned out to be identical with previously reported beta 3Gal-T3, which had been cloned by sequence homology with other galactosyltransferases. Substrate specificity analysis with extracts from cDNA-transfected L cells confirmed that the gene product was actually beta 1,3-N-acetylgalactosaminyltransferase that specifically catalyzes the transfer of N-acetylgalactosamine onto globotriaosylceramide. Results of TLC immunostaining of neutral glycolipids from the cDNA-transfected cells also supported the identity of the newly synthesized component as globoside. The results show that glycosyltransferases apparently belonging to a single glycosyltransferase family do not necessarily catalyze reactions utilizing the same acceptor or even the same sugar donor. The globoside synthase gene was expressed in many tissues, such as heart, brain, testis, etc. We propose the designation beta 3GalNAc-T1 for the cloned globoside synthase gene.

* This work was supported by Grants-in-aid for Scientific Research 10470029 and 12670111, for Priority Areas 10178104, 12215058, and 12204055, and for Center of Excellence 10CE2006 from the Ministry of Education, Science, Sports, and Culture of Japan.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/EMBL Data Bank with accession number(s) AB050855 and AB050856.

|| Research Fellow of the Japan Society for the Promotion of Science.

** To whom correspondence should be addressed: Dept.of Biochemistry II, Nagoya University School of Medicine, 65 Tsurumai, Showa-ku, Nagoya 466-0065, Japan. Tel.: 81-52-744-2070; Fax: 81-52-744-2069; E-mail: koichi@med.nagoya-u.ac.jp.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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