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J. Biol. Chem., Vol. 275, Issue 51, 40605-40613, December 22, 2000
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From the We have previously cloned
chondroitin-4-sulfotransferase (C4ST) cDNA from mouse brain. In
this paper, we report cloning and characterization of GalNAc
4-sulfotransferase (GalNAc4ST), which transfers sulfate to position 4 of the nonreducing terminal GalNAc residue. The obtained cDNA
contains a single open reading frame that predicts a type II
transmembrane protein composed of 424 amino acid residues. Identity of
the amino acid sequence between GalNAc4ST and human C4ST was 30%. When
the cDNA was transfected in COS-7 cells, sulfotransferase activity
toward carbonic anhydrase VI was overexpressed but no sulfotransferase
activity toward chondroitin or desulfated dermatan sulfate was
increased over the control. Sulfation of carbonic anhydrase VI by the
recombinant GalNAc4ST occurred at position 4 of the GalNAc residue of
N-linked oligosaccharides. The recombinant GalNAc4ST
transferred sulfate to position 4 of GalNAc residue of
p-nitrophenyl GalNAc, indicating that this sulfotransferase transfers sulfate to position 4 at the nonreducing terminal GalNAc residue. Dot blot analysis showed that the message of GalNAc4ST was
expressed strongly in the human pituitary, suggesting that the cloned
GalNAc4ST may be involved in the synthesis of the nonreducing terminal
GalNAc 4-sulfate residues found in the N-linked
oligosaccharides of pituitary glycoprotein hormones.
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AB047801.
Molecular Cloning and Characterization of GalNAc
4-Sulfotransferase Expressed in Human Pituitary Gland*
,,§,,
Department of Life Science,
¶ Department of Chemistry, Aichi University of Education, Kariya,
Aichi 448-8542, Japan
*
This work was supported by grants-in-aid for Scientific
Research on Priority Areas No. 10178102 and grants-in-aid for
Scientific Research No. 12680610 from the Ministry of Education,
Science, Sports and Culture of Japan, grants-in-Aid of Mizutani
Foundation for Glycoscience, and by a special research fund from
Seikagaku Corporation.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.
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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