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Originally published In Press as doi:10.1074/jbc.M112367200 on April 29, 2002

J. Biol. Chem., Vol. 277, Issue 27, 24030-24038, July 5, 2002
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Molecular Cloning and Expression of a Sixth Type of alpha 2,8-Sialyltransferase (ST8Sia VI) That Sialylates O-Glycans*

Shou TakashimaDagger §, Hide-ki Ishida, Toshiyuki Inazu, Takayuki Ando||, Hideharu Ishida||, Makoto Kiso||, Shuichi Tsuji**, and Masafumi TsujimotoDagger Dagger Dagger

From the Dagger  Laboratory of Cellular Biochemistry, RIKEN (Institute of Physical and Chemical Research), 2-1 Hirosawa, Wako, Saitama 351-0198, Japan, the  Noguchi Institute, 1-8-1 Kaga, Itabashi-ku, Tokyo 173-0003, Japan, the || Department of Applied Bio-organic Chemistry, Faculty of Agricultural and Life Sciences, Gifu University, Gifu 501-1193, Japan, and the ** Department of Chemistry, Faculty of Science, Ochanomizu University, Otuka, Bunkyo-ku, Tokyo 112-8610, Japan

A novel member of the mouse alpha 2,8-sialyltransferase (ST8Sia) family, designated ST8Sia VI, was identified by BLAST analysis of expressed sequence tags. The sequence of ST8Sia VI encodes a protein of 398 amino acids and shows 42.0 and 38.3% amino acid sequence identities to mouse alpha 2,8-sialyltransferases ST8Sia I (GD3 synthase) and ST8Sia V (GD1c, GT1a, GQ1b, and GT3 synthases), respectively. The recombinant soluble form of ST8Sia VI expressed in COS-7 cells exhibited alpha 2,8-sialyltransferase activity toward both glycolipids and glycoproteins that have the NeuAcalpha 2,3(6)Gal sequence at the nonreducing end of their carbohydrate groups. This enzyme formed NeuAcalpha 2,8NeuAc structures, but not oligosialic or polysialic acid structures. Analysis of the fetuin sialylated by ST8Sia VI indicated that ST8Sia VI prefers O-glycans to N-glycans as acceptor substrates. Substrate specificities and kinetic properties also showed that ST8Sia VI prefers O-glycans to glycolipids as acceptor substrates. ST8Sia VI also exhibited activity toward oligosaccharides such as sialyllactose and sialyllactosamine, and the structure of the minimal acceptor substrate for ST8Sia VI was determined as the NeuAcalpha 2,3(6)Gal sequence. The expression of the ST8Sia VI gene was ubiquitous, and the highest expression was observed in kidney, with three major transcripts of 8.2, 3.8, and 2.7 kb. This is the first report of a mammalian alpha 2,8-sialyltransferase that sialylates O-glycans preferentially.

* This work was supported in part by a grant for the Multibioprobe Research Program from RIKEN (Institute of Physical and Chemical Research).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 DDBJ/GenBankTM/EBI Data Bank with accession number(s) AB059554.

§ Special postdoctoral researcher from RIKEN (Institute of Physical and Chemical Research).

Dagger Dagger To whom correspondence should be addressed. Tel.: 81-48-467-9370; Fax: 81-48-462-4670; E-mail: tsujimot@postman.riken.go.jp.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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Copyright © 2002 by the American Society for Biochemistry and Molecular Biology.