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J Biol Chem, Vol. 273, Issue 12, 6615-6618, March 20, 1998
,,§,
From the Department of Biochemistry, Kobe Pharmaceutical
University, Higashinada-ku, Kobe 658, Japan, We isolated a cDNA encoding a novel
glucuronyltransferase from human placenta cDNA with the use of the
degenerate reverse transcriptase-polymerase chain reaction method.
Degenerate primers were designed based upon the amino acid sequence
alignment of rat glucuronyltransferase (GlcAT-P) involved in the
biosynthesis of the carbohydrate epitope HNK-1 with putative proteins
in Caenorhabditis elegans and Schistosoma
mansoni. The new cDNA sequence revealed an open reading frame
coding for a protein of 335 amino acids with a type II transmembrane
protein topology. The amino acid sequence displayed 43% identity to
the rat GlcAT-P, and the highest sequence identity was found in the
COOH-terminal catalytic domain. The expression of a soluble recombinant
form of the protein in COS-1 cells produced an active
glucuronyltransferase with marked specificity for a glycoserine
Gal RIKEN (The
Institute of Physical and Chemical Research), Wako-shi, Saitama 351-01, Japan, the § Graduate School for Agriculture and Life
Science, University of Tokyo, Yayoi, Bunkyo-ku, Tokyo 113, Japan, and
the ¶ Department of Biological Chemistry, Faculty of
Pharmaceutical Sciences, Kyoto University, Sakyo-ku, Kyoto
606-01, Japan
1-3Gal1-4Xyl1-O-Ser. In contrast, asialoorosomucoid, which contains the Gal1-4GlcNAc sequence and is
a good acceptor substrate for the GlcAT-P, did not serve as an
acceptor. The reaction product was sensitive to -glucuronidase digestion and co-chromatographed with authentic
GlcA1-3Gal1-3Gal1-4Xyl1-O-Ser in
high-performance liquid chromatography, suggesting that the enzyme is a
1,3-glucuronyltransferase. These results indicate that this new
member of the glucuronyltransferase gene family is the enzyme
previously described as glucuronyltransferase I that forms the
glycosaminoglycan-protein linkage region,
GlcA1-3Gal1-3Gal1-4Xyl1-O-Ser, of
proteoglycans.
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