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Originally published In Press as doi:10.1074/jbc.M909620199 on March 9, 2000
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J Biol Chem, Vol. 275, Issue 20, 15152-15156, May 19, 2000

Molecular Cloning of Globotriaosylceramide/CD77 Synthase, a Glycosyltransferase That Initiates the Synthesis of Globo Series Glycosphingolipids*

Yoshinao KojimaDagger §, Satoshi FukumotoDagger §, Keiko FurukawaDagger , Tetsuya OkajimaDagger , Joelle Wiels||, Keiko Yokoyama**, Yasuo SuzukiDagger Dagger , Takeshi UranoDagger , Michio Ohta**, and Koichi FurukawaDagger Dagger Dagger

From the Dagger  Department of Biochemistry II and ** Department of Bacteriology, Nagoya University School of Medicine, Tsurumai, Nagoya 466-0065,  Department of Pediatric Dentistry, Nagasaki University School of Dentistry, Sakamoto, Nagasaki 852-8588, Dagger Dagger  Department of Biochemistry, University of Shizuoka School of Pharmaceutical Sciences, Shizuoka 422-8526, Japan, || CNRS UMR 1598, Institut Gustave Roussy, Villejuif Cedex, 94805 France

The expression cloning of a cDNA for globotriaosylceramide (Gb3)/CD77 synthase (alpha 1,4-galactosyltransferase) was achieved using an anti-Gb3 antibody and mouse L cells as a recipient cell line for the transfection. The isolated cDNA clone designated pVTR1 predicted a type II membrane protein with 19 amino acids of cytoplasmic domain, 26 amino acids of transmembrane region, and a catalytic domain with 308 amino acids. Introduction of the cDNA clone into L cells resulted in the neosynthesis of Gb3/CD77, and the extracts of the transfectant cells showed alpha 1,4-galactosyltransferase activity only on lactosylceramide and galactosylceramide. In Northern blotting, a 2.3-kilobase mRNA was strongly expressed in heart, kidney, spleen, and placenta and weakly in colon, small intestine, and brain. Transfection of the cDNA into L cells resulted in the constitution of sensitivity to the apoptosis with Shiga-like toxins (verotoxins). Since Gb3/CD77 synthase initiates the synthesis of globo series glycolipids, the isolation of this cDNA will make possible further investigations into the function of its important series of glycolipids.

* This work was supported by grants-in-aid for the Center of Excellence Research, Scientific Research and Scientific Research of Priority Areas from the Ministry of Education, Science, Sports and Culture of Japan and also a Research Grant on Human Genome and Gene Therapy from the Ministry of Health and Welfare 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 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) AB 037883.

§ These authors contributed equally to this work.

Dagger Dagger To whom correspondence and reprint requests should be addressed. 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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