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Originally published In Press as doi:10.1074/jbc.M105848200 on July 24, 2001

J. Biol. Chem., Vol. 276, Issue 39, 36344-36353, September 28, 2001
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Molecular Cloning and Characterization of a Dermatan-specific N-Acetylgalactosamine 4-O-Sulfotransferase*

Matthias R. EversDagger §, Guoqing XiaDagger §, Hyung-Gyoo Kang§, Melitta SchachnerDagger , and Jacques U. Baenziger||

From the  Department of Pathology, Washington University School of Medicine, St. Louis, Missouri 63110 and Dagger  Zentrum fuer Molekulare Neurobiologie, Universitaet Hamburg, Martinistr. 52, D-20246 Hamburg, Germany

We have identified and characterized an N-acetylgalactosamine-4-O-sulfotransferase designated dermatan-4-sulfotransferase-1 (D4ST-1) (GenBankTM accession number AF401222) based on its homology to HNK-1 sulfotransferase. The cDNA predicts an open reading frame encoding a type II membrane protein of 376 amino acids with a 43-amino acid cytoplasmic domain and a 316-amino acid luminal domain containing two potential N-linked glycosylation sites. D4ST-1 has significant amino acid identity with HNK-1 sulfotransferase (21.4%), N-acetylgalactosamine-4-O-sulfotransferase 1 (GalNAc-4-ST1) (24.7%), N-acetylgalactosamine-4-O-sulfotransferase 2 (GalNAc-4-ST2) (21.0%), chondroitin-4-O-sulfotransferase 1 (27.3%), and chondroitin-4-O-sulfotransferase 2 (22.8%). D4ST-1 transfers sulfate to the C-4 hydroxyl of beta 1,4-linked GalNAc that is substituted with an alpha -linked iduronic acid (IdoUA) at the C-3 hydroxyl. D4ST-1 shows a strong preference in vitro for sulfate transfer to IdoUAalpha 1,3GalNAcbeta 1,4 that is flanked by GlcUAbeta 1,3GalNAcbeta 1,4 as compared with IdoUAalpha 1,3GalNAcbeta 1,4 flanked by IdoUAalpha 1,3GalNAcbeta 1,4. The specificity of D4ST-1 when assayed in vitro suggests that the addition of sulfate to GalNAc occurs immediately after epimerization of GlcUA to IdoUA. The open reading frame of D4ST-1 is encoded by a single exon located on human chromosome 15q14. Northern blot analysis reveals a single 2.4-kilobase transcript. D4ST-1 message is expressed in virtually all tissues at some level but is most highly expressed in pituitary, placenta, uterus, and thyroid. The properties of D4ST-1 indicate that sulfation of the GalNAc moieties in dermatan is mediated by a distinct GalNAc-4-O-sulfotransferase and occurs following epimerization of GlcUA to IdoUA.

* This work was supported by National Institutes of Health Grant R01-DK41738 (to J. U. B.), by Deutsche Forschungsgemeinschaft Grant SCHA185/15-1 (to M. S.), and by a German Academic Exchange Service postdoctoral fellowship (to G. X.).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) AF401222.

§ These three authors contributed equally to this work.

|| To whom correspondence should be addressed: Washington University School of Medicine, Dept. of Pathology, 660 S. Euclid Ave., St. Louis, MO 63110. Tel.: 314-362-8730; Fax: 314-362-8888; E-mail: Baenziger@Pathology.wustl.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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