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Originally published In Press as doi:10.1074/jbc.M006414200 on August 23, 2000

J. Biol. Chem., Vol. 275, Issue 51, 40226-40234, December 22, 2000
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Sulfation of N-Acetylglucosamine by Chondroitin 6-Sulfotransferase 2 (GST-5)*

Sunil BhaktaDagger , Alexander BartesDagger , Kendra G. Bowman§, Wei-Ming Kao§, Irene PolskyDagger , Jin Kyu Lee||**, Brian N. Cook§, Richard E. BruehlDagger ||Dagger Dagger , Steven D. Rosen||, Carolyn R. Bertozzi§, and Stefan HemmerichDagger §§

From the Dagger  Department of Respiratory Diseases, Roche Bioscience, Palo Alto, California 94304, the § Departments of Chemistry and Molecular and Cell Biology, and Howard Hughes Medical Institute, University of California, Berkeley, California 94720, and the || Department of Anatomy and Program in Immunology, University of California, San Francisco, California 94143

Based on sequence homology with a previously cloned human GlcNAc 6-O-sulfotransferase, we have identified an open reading frame (ORF) encoding a novel member of the Gal/GalNAc/GlcNAc 6-O-sulfotransferase (GST) family termed GST-5 on the human X chromosome (band Xp11). GST-5 has recently been characterized as a novel GalNAc 6-O-sulfotransferase termed chondroitin 6-sulfotransferase-2 (Kitagawa, H., Fujita, M., Itio, N., and Sugahara K. (2000) J. Biol. Chem. 275, 21075-21080). We have coexpressed a human GST-5 cDNA with a GlyCAM-1/IgG fusion protein in COS-7 cells and observed four-fold enhanced [35S]sulfate incorporation into this mucin acceptor. All mucin-associated [35S]sulfate was incorporated as GlcNAc-6-sulfate or Galbeta 1right-arrow4GlcNAc-6-sulfate. GST-5 was also expressed in soluble epitope-tagged form and found to catalyze 6-O-sulfation of GlcNAc residues in synthetic acceptor structures. In particular, GST-5 was found to catalyze 6-O-sulfation of beta -benzyl GlcNAc but not alpha - or beta -benzyl GalNAc. In the mouse genome we have found a homologous ORF that predicts a novel murine GlcNAc 6-O-sulfotransferase with 88% identity to the human enzyme. This gene was mapped to mouse chromosome X at band XA3.1-3.2. GST-5 is the newest member of an emerging family of carbohydrate 6-O-sulfotransferases that includes chondroitin 6-sulfotransferase (GST-0), keratan-sulfate galactose 6-O-sulfotransferase (GST-1), the ubiquitously expressed GlcNAc 6-O-sulfotransferase (GST-2), high endothelial cell GlcNAc 6-O-sulfotransferase (GST-3), and intestinal GlcNAc 6-O-sulfotransferase (GST-4).

* This work was supported in part by National Institutes of Health Grant Merit Awards R37GM23547 and RO1GM5741 (to S. D. R.) and RO1 GM59907-01 (to C. R. B.), American Cancer Society Grant RPG9700501BE (to C. R. B.), and Roche Bioscience (to S. D. R. and C. R. B.).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 reported in this paper for the mouse GST5 intronless genomic coding sequence has been submitted to the GenBankTM/EBI/Data Bank under accession number AF280089.

Supported by a predoctoral fellowship from Boehringer Ingelheim.

** Supported by a postdoctoral fellowship from the Arthritis Foundation.

Dagger Dagger Present address: Lawrence Berkeley National Laboratory, Material Sciences Division, 1 Cyclotron Rd., Mail Stop 66, Berkeley, CA 94720.

§§ To whom correspondence should be addressed: Thios Biotechnologies, 828 Clayton St., San Francisco, CA 94117. Tel.:/Fax: 510-548-1310; E-mail: stefan@thiosbiotech.com.

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