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Originally published In Press as doi:10.1074/jbc.M007821200 on September 14, 2000

J. Biol. Chem., Vol. 275, Issue 49, 38402-38409, December 8, 2000
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Molecular Cloning and Expression of the Pituitary Glycoprotein Hormone N-Acetylgalactosamine-4-O-sulfotransferase*

Guoqing XiaDagger §, Matthias R. EversDagger §, 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, Martinistrasse 52, D-20246 Hamburg, Germany

N-Linked oligosaccharides terminating with the sequence SO4-4-GalNAcbeta 1,4GlcNAcbeta 1,2Manalpha are present on the pituitary hormones lutropin (LH), thyrotropin, and pro-opiomelanocortin. The sulfated structures on LH are essential for expression of its biologic function in vivo. We have cloned the N-acetylgalactosamine-4-sulfotransferase (GalNAc-4-ST1, GenBankTM accession number AF300612), which mediates sulfate addition to the N-linked oligosaccharides on LH and other pituitary glycoproteins with terminal (beta 1,4-linked GalNAc based on its homology to HNK-1 sulfotransferase (HNK-1 ST). GalNAc-4-ST1 displays 23% identity to HNK-1 ST and 28% to chondroitin 4-sulfotransferase 1 (C4ST-1) and 26% to chondroitin 4-sulfotransferase 2 (C4ST-2). The cDNA predicts a type II transmembrane protein of 424 amino acids with four potential N-linked glycosylation sites and a single membrane-spanning domain. GalNAc-4-ST1 has putative 5'-phosphosulfonate and 3'-phosphate binding sites. Three more carboxyl-terminal regions of unknown function also show a high degree of identity with HNK-1 ST, C4ST-1, and C4ST-2. The membrane-bound form of GalNAc-4-ST1 transfers sulfate to GalNAcbeta 1,4GlcNAcbeta -R but not to chondroitin, whereas truncated forms of GalNAc-4-ST1 that are released into the medium transfer sulfate to both GalNAcbeta 1,4GlcNAcbeta -R and chondroitin. The first 118 amino acids of GalNAc-4-ST1 appear to contribute to both its activity and specificity for terminal beta 1,4-linked GalNAc. GalNAc-4-ST1 also efficiently transfers sulfate to N-linked oligosaccharides on native LH and other glycoproteins terminating with beta 1,4-linked GalNAc. A single transcript of 2.4 kilobases is most highly expressed in the pituitary and other regions of the central nervous system. The GalNAc-4-ST1 gene is located on human chromosome 19q13.1.

* This work was supported by National Institutes of Health Grant R01-DK41738 (to J. U. B.), by Deutsche Forschungsgemeinschaft Grant SFB 470 (to M. S.), and by a German Academic Exchange Service (DAAD) 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) AF300612.

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