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Originally published In Press as doi:10.1074/jbc.M204907200 on June 21, 2002

J. Biol. Chem., Vol. 277, Issue 38, 34766-34772, September 20, 2002
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Molecular Cloning and Characterization of Chondroitin-4-O-sulfotransferase-3
A NOVEL MEMBER OF THE HNK-1 FAMILY OF SULFOTRANSFERASES*

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

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

We have identified and characterized an N-acetylgalactosamine-4-O-sulfotransferase designated chondroitin-4-sulfotransferase-3 (C4ST-3) (GenBankTM accession number AY120869) 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 341 amino acids with a 12-amino acid cytoplasmic domain and a 311-amino acid luminal domain containing a single potential N-linked glycosylation site. C4ST-3 has the greatest amino acid sequence identity when aligned with chondroitin-4-O-sulfotransferase 1 (C4ST-1) (45%) but also shows significant amino acid identity with chondroitin-4-O-sulfotransferase 2 (C4ST-2) (27%), dermatan-4-O-sulfotransferase 1 (29%), HNK-1 ST (26%), N-acetylgalactosamine-4-O-sulfotransferase 1 (26%), and N-acetylgalactosamine-4-O-sulfotransferase 2 (23%). C4ST-3 transfers sulfate to the C-4 hydroxyl of beta 1,4-linked GalNAc that is substituted with a beta -linked glucuronic acid at the C-3 hydroxyl. The open reading frame of C4ST-3 is encoded by three exons located on human chromosome 3q21.3. Northern blot analysis reveals a single 2.1-kilobase transcript. C4ST-3 message is expressed in adult liver and at lower levels in adult kidney, lymph nodes, and fetal liver. Although C4ST-3 and C4ST-1 have similar specificities, the highly restricted pattern of expression seen for C4ST-3 suggests that it has a different role than C4ST-1.


* This work was supported by National Institutes of Health Grant R01-DK41738 (to J. U. B.), Deutsche Forschungsgemeinschaft Grant SCHA185/15-1 (to M. S.), and 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/EBI Data Bank with accession number(s) AY120869.

§ These three authors contributed equally to this work.

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


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