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J Biol Chem, Vol. 274, Issue 14, 9271-9276, April 2, 1999

Expression Cloning of Mouse cDNA of CMP-NeuAc:Lactosylceramide 2,3-Sialyltransferase, an Enzyme That Initiates the Synthesis of Gangliosides

Satoshi Fukumoto^§, Hiroshi Miyazaki, George Goto^§, Takeshi Urano, Keiko Furukawa, and Koichi Furukawa

From the  Department of Biochemistry II, Nagoya University School of Medicine, 65 Tsurumai, Nagoya 466-0065 and the ^§ Department of Pediatric Dentistry, Nagasaki University School of Dentistry, 1-7-1, Sakamoto, Nagasaki 852-8102, Japan

Expression cloning of a cDNA for the 2,3-sialyltransferase (GM3 synthase) (EC 2.4.99.-) gene was performed using a GM3-lacking mouse fibroblast line L cell and anti-GM3 monoclonal antibody. Plasmids from a cDNA library generated with poly(A)⁺ RNA of a mouse fibrosarcoma line CMS5j and pdl3027 (polyoma T antigen) were co-transfected into L cells. The isolated cDNA clone pM3T-7 predicted a type II membrane protein with 13 amino acids of cytoplasmic domain, 17 amino acids of transmembrane region, and a large catalytic domain with 329 amino acids. Introduction of the cDNA clone into L cells resulted in the neo-synthesis of GM3 and high activity of 2,3-sialyltransferase. Among glycosphingolipids, only lactosylceramide showed significant activity as an acceptor, indicating that this gene product is a sialyltransferase specific for the synthesis of GM3. An amino acid sequence deduced from the cloned cDNA showed the typical sialyl motif with common features among 2,3-sialyltransferases. Among various mouse tissues, brain, liver, and testis showed relatively high expression of a 2.3-kilobase mRNA, whereas all tissues, more or less, expressed this gene.

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

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