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Originally published In Press as doi:10.1074/jbc.M011560200 on January 3, 2001

J. Biol. Chem., Vol. 276, Issue 14, 10861-10869, April 6, 2001
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Molecular Cloning and Expression of an N-Acetylgalactosamine-4-O-sulfotransferase That Transfers Sulfate to Terminal and Non-terminal beta 1,4-Linked N-Acetylgalactosamine*

Hyung-Gyoo KangDagger §, Matthias R. Evers§, Guoqing Xia§, Jacques U. BaenzigerDagger , and Melitta Schachner||

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

We have identified and characterized an N-acetylgalactosamine-4-O-sulfotransferase designated GalNAc-4-ST2 (GenBankTM accession number AF332472) based on its homology to HNK-1 sulfotransferase (HNK-1 ST). The cDNA predicts an open reading frame encoding a type II membrane protein of 443 amino acids with a 12-amino acid cytoplasmic domain, a 23-amino acid transmembrane domain, and a 408-amino acid luminal domain containing four potential N-linked glycosylation sites. GalNAc-4-ST2 displays a high degree of amino acid sequence identity with GalNAc-4-ST1 (46%), HNK-1 ST (23%), chondroitin 4-O-sulfotransferase-1 (C4ST-1) (27%), and chondroitin 4-O-sulfotransferase-2 (C4ST-2) (24%). GalNAc-4-ST2 transfers sulfate to the C-4 hydroxyl of terminal beta 1,4-linked GalNAc in the sequence GalNAc-beta 1,4GlcNAcbeta -R found on N-linked oligosaccharides and nonterminal beta 1,4-linked GalNAc in chondroitin and dermatan. The translated region of GalNAc-4-ST2 is encoded by five exons located on human chromosome 18q11.2. Northern blot analysis reveals a 2.1-kilobase transcript. GalNAc-4-ST2 message is most highly expressed in trachea and to a lesser extent in heart, liver, pancreas, salivary gland, and testis. The I.M.A.G.E. cDNA clone 49547 contains a putative GalNAc-4-ST2 splice form with an open reading frame encoding a protein of 358 amino acids that lacks the transmembrane domain and the stem region. This form of GalNAc-4-ST2 is not retained by transfected cells and is active against chondroitin but not terminal beta 1,4-linked GalNAc. Thus, as with GalNAc-4-ST1, sequences N-terminal to the catalytic domain contribute to the specificity of GalNAc-4-ST2 toward terminal beta 1,4-linked GalNAc.

* This work was supported by National Institutes of Health Grant R01-DK41738 (to J. U. B.), by Deutsche Forschungsgemeinschaft Grant SCHAI85/15-1 (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) AF332472 and AF332473.

§ These authors contributed equally to this work.

|| To whom correspondence should be addressed: Zentrum fuer Molekulare Neurobiologie, Universitaet Hamburg, Martinistrasse 52, 20246 Hamburg, Germany. Tel.: 49-40-42803-6246; Fax: 49-40-42803-6248; E-mail: melitta.schachner@zmnh.uni-hamburg.de.

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