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J. Biol. Chem., Vol. 275, Issue 26, 20188-20196, June 30, 2000
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From the Glycobiology Program, Cancer Research Center, The Burnham
Institute, La Jolla, California 92037
Using an expression cloning strategy, the
cDNA encoding the human HNK-1 sulfotransferase (HNK-1ST) has been
cloned. During this cloning we found that HNK-1ST and other
Golgi-associated sulfotransferases cloned before share homologous
sequences including the RDP motif (Ong, E., Yeh, J.-C., Ding, Y.,
Hindsgaul, O., and Fukuda, M. (1998) J. Biol. Chem.
223, 5190-5195). Using this conserved sequence in HNK-1ST as a probe,
we identified two expressed sequence tags in EST data base which have
31.6 and 30.7% identity with HNK-1ST at the amino acid levels.
Expression of these two full-length cDNAs failed to form HNK-1
glycan nor to add sulfate to CD34 or NCAM. Surprisingly, proteins
expressed by these cDNAs transferred sulfate to the C-4 position of
N-acetylgalactosamine in chondroitin and desulfated
dermatan sulfate, thus we named these two enzymes, chondroitin
4-O-sulfotransferase 1 and -2 (C4ST-1 and C4ST-2). Both
C4ST-1 and C4ST-2, however, did not form 4,6-di-O-sulfated N-acetylgalactosamine when chondroitin sulfate C was used
as an acceptor. Moreover, analysis of 35S-labeled dermatan
sulfate formed by C4ST-1 indicate that sulfation preferentially took
place in GlcA The nucleotide sequences reported in this paper has been
submitted to GenBank with accession number AF239820 for C4ST-1 and
AF239822 for C4ST-2.
Molecular Cloning and Expression of Two Distinct Human
Chondroitin 4-O-Sulfotransferases That Belong to the HNK-1
Sulfotransferase Gene Family*
,
GalNAc unit than in IdoAGalNAc unit, suggesting that
4-O-sulfation at N-acetylgalactosamine may precede epimerization of glucuronic acid to iduronic acid during dermatan sulfate biosynthesis. Northern analysis demonstrated that the
transcript for C4ST-1 is predominantly expressed in
peripheral leukocytes and hematopoietic tissues while the
C4ST-2 transcript is more widely expressed in various
tissues. These results indicate C4ST-1 and C4ST-2 play complementary
roles in chondroitin and dermatan sulfate synthesis in different tissues.
*
This work was supported by National Cancer Institute Grants
P01CA71932 and CA33895.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.
Present address: Graduate School of Science, University of
Hokkaido, Sapporo, 060-0810 Japan.
§
To whom correspondence should be addressed: The Burnham Institute,
10901 North Torrey Pines Rd., La Jolla, CA 92037. Tel.: 858-646-3144;
Fax: 858-646-3193; E-mail: minoru@burnham.org.
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