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J Biol Chem, Vol. 275, Issue 12, 8975-8981, March 24, 2000
§,
From the Department of Life Science, Aichi University of Education,
Kariya, Aichi 448-8542, Japan and ¶ Institute for Molecular
Medical Science, Aichi Medical University, Nagakute, Aichi
480-1195, Japan
Chondroitin 4-sulfotransferase (C4ST) catalyzes
the transfer of sulfate from 3'-phosphoadenosine 5'-phosphosulfate to
position 4 of N-acetylgalactosamine residue of chondroitin.
The enzyme has been previously purified to apparent homogeneity from
the serum-free culture medium of rat chondrosarcoma cells (Yamauchi, A., Hirahara, Y., Usui, H., Takeda, Y., Hoshino, M., Fukuta, M., Kimura, J. H., and Habuchi, O. (1999) J. Biol.
Chem. 274, 2456-2463). The purified enzyme also catalyzed the
sulfation of partially desulfated dermatan sulfate. We have now cloned
the cDNA of the mouse C4ST on the basis of the amino acid sequences
of peptides obtained from the purified enzyme by protease digestion.
This cDNA contains a single open reading frame that predicts a
protein composed of 352 amino acid residues. The protein predicts a
Type II transmembrane topology. The predicted sequence of the protein contains all of the known amino acid sequence and four potential sites
for N-glycosylation, which corresponds to the observation that the purified C4ST is an N-linked glycoprotein. The
amino acid sequence of mouse C4ST showed significant sequence homology to HNK-1 sulfotransferase. Comparison of the sequence of mouse C4ST
with human HNK-1 sulfotransferase revealed ~29% identity and ~48%
similarity at the amino acid level. When the cDNA was introduced in
a eukaryotic expression vector and transfected in COS-7 cells, the
sulfotransferase activity that catalyzes the transfer of sulfate to
position 4 of GalNAc residue of both chondroitin and desulfated
dermatan sulfate was overexpressed. Northern blot analysis showed that,
among various mouse adult tissues, 5.7-kilobase message of C4ST was
mainly expressed in the brain and kidney.
The nucleotide sequence reported in this paper has been submitted to the DDBJ/GenBankTM/EBI Data Bank with accession number AB030378.
Present address: Dept. of Perinatology and Neuroglycoscience,
Institute for Developmental Research, Kasugai, Aichi 480-0392, Japan.
§
These authors contributed equally to this work.
To whom correspondence should be addressed: Dept. of Life
Science, Aichi University of Education, Kariya, Aichi 448-8542, Japan.
Fax: 81-566-26-2649; E-mail: ohabuchi@auecc.aichi-edu.ac.jp.
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