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J Biol Chem, Vol. 273, Issue 41, 26265-26268, October 9, 1998
From the Department of Medical Biochemistry and Microbiology,
Uppsala University, The Biomedical Center, Box 575, S-751 23 Uppsala,
Sweden and § Department of Microbiology and Immunology,
University of British Columbia, Vancouver V6T 1Z3, Canada
Hereditary multiple exostoses, characterized by
multiple cartilaginous tumors, is ascribed to mutations at three
distinct loci, denoted EXT1-3. Here, we report the purification of a
protein from bovine serum that harbored the
D-glucuronyl (GlcA) and
N-acetyl-D-glucosaminyl (GlcNAc) transferase
activities required for biosynthesis of the glycosaminoglycan, heparan
sulfate (HS). This protein was identified as EXT2. Expression of EXT2
yielded a protein with both glycosyltransferase activities. Moreover,
EXT1, previously found to rescue defective HS biosynthesis (McCormick,
C., Leduc, Y., Martindale, D., Mattison, K., Esford, L. E., Dyer,
A. P., and Tufaro, F. (1998) Nat. Genet. 19, 158-161), was shown to elevate the low GlcA and GlcNAc transferase levels of mutant cells. Thus at least two members of the EXT family of
tumor suppressors encode glycosyltransferases involved in the chain
elongation step of HS biosynthesis.
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