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J Biol Chem, Vol. 274, Issue 12, 7857-7864, March 19, 1999
1,3-Glucuronosyltransferases
From the Division of Cellular and Molecular Medicine, Glycobiology
Research and Training Program, University of California at San Diego,
La Jolla, California 92093-0687
While expression-cloning
enzymes involved in heparan sulfate biosynthesis, we isolated a
cDNA that encodes a protein 65% identical to the
UDP-GlcUA:glycoprotein 
1,3-glucuronosyltransferase (GlcUAT-P) involved in forming HNK-1 carbohydrate epitopes
(3OSO3GlcUA1,3Gal-) on glycoproteins. The
cDNA contains an open reading frame coding for a protein of 335 amino acids with a predicted type II transmembrane protein orientation.
Cotransfection of the cDNA with HNK-1
3-O-sulfotransferase produced HNK-1 carbohydrate epitopes
in Chinese hamster ovary (CHO) cells and COS-7 cells. In
vitro, a soluble recombinant form of the enzyme transferred GlcUA
in -linkage to
Gal1,3/4GlcNAc-O-naphthalenemethanol, which resembles
the core oligosaccharide on which the HNK-1 epitope is assembled.
However, the enzyme greatly preferred
Gal1,3Gal-O-naphthalenemethanol, a disaccharide
component found in the linkage region tetrasaccharide in chondroitin
sulfate and heparan sulfate. During the course of this study, a human
cDNA clone was described that was thought to encode
UDP-GlcUA:Gal1,3Gal-R glucuronosyltransferase (GlcUAT-I), involved
in the formation of the linkage region of glycosaminoglycans (Kitagawa,
H., Tone, Y., Tamura, J., Neumann, K. W., Ogawa, T., Oka, S.,
Kawasaki, T., and Sugahara, K. (1998) J. Biol. Chem. 273, 6615-6618). The deduced amino acid sequences of the CHO and human
cDNAs are 95% identical, suggesting that they are in fact homologues of the same gene. Transfection of a CHO cell mutant defective in GlcUAT-I with the hamster cDNA restored
glycosaminoglycan assembly in vivo, confirming its
identity. Interestingly, transfection of the mutant with GlcUAT-P also
restored glycosaminoglycan synthesis. Thus, both GlcUAT-P and GlcUAT-I
have overlapping substrate specificities. However, the expression of
the two genes was entirely different, with GlcUAT-I expressed in all
tissues tested and GlcUAT-P expressed only in brain. These findings
suggest that, in neural tissues, GlcUAT-P may participate in both HNK-1
and glycosaminoglycan production.
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