Characterization of recombinant human glucuronyltransferase I involved in the biosynthesis of the glycosaminoglycan-protein linkage region of proteoglycans

FEBS Lett. 1999 Oct 15;459(3):415-20. doi: 10.1016/s0014-5793(99)01287-9.


We characterized the recombinant glucuronyltransferase I (GlcAT-I) involved in the glycosaminoglycan-protein linkage region biosynthesis. The enzyme showed strict specificity for Galbeta1-3Galbeta1-4Xyl, exhibiting negligible incorporation into other galactoside substrates including Galbeta1-3Galbeta1-O-benzyl, Galbeta1-4GlcNAc and Galbeta1-4Glc. A comparison of the GlcAT-I with another beta1,3-glucuronyltransferase involved in the HNK-1 epitope biosynthesis revealed that the two beta1,3-glucuronyltransferases exhibited distinct and no overlapping acceptor substrate specificities in vitro. Nevertheless, the transfection of the GlcAT-I cDNA into COS-1 cells induced the significant expression of the HNK-1 epitope. These results suggested that the high expression of the GlcAT-I gene rendered the cells capable of synthesizing the HNK-1 epitope.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • COS Cells
  • Glucuronosyltransferase / biosynthesis
  • Glucuronosyltransferase / genetics
  • Glucuronosyltransferase / metabolism*
  • Glycosaminoglycans / metabolism*
  • Humans
  • Proteins / metabolism
  • Proteoglycans / biosynthesis*
  • Proteoglycans / metabolism
  • Recombinant Proteins / metabolism
  • Substrate Specificity


  • Glycosaminoglycans
  • Proteins
  • Proteoglycans
  • Recombinant Proteins
  • galactosylgalactoylxylosylprotein 3-beta-glucuronosyltransferase
  • Glucuronosyltransferase