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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
Molecular Cloning and Characterization of
Chondroitin-4-O-sulfotransferase-3
A NOVEL MEMBER OF THE HNK-1 FAMILY OF SULFOTRANSFERASES*
Hyung-Gyoo
Kang §,
Matthias R.
Evers§¶,
Guoqing
Xia§¶,
Jacques U.
Baenziger , and
Melitta
Schachner¶
From the 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 1,4-linked
GalNAc that is substituted with a -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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Copyright © 2002 by the American Society for Biochemistry and Molecular Biology.
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