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

Yuko Tone, Hiroshi Kitagawa, Kimiyuki Imiya, Shogo Oka, Toshisuke Kawasaki, Kazuyuki Sugahara

Research output: Contribution to journalArticlepeer-review

42 Citations (Scopus)

Abstract

We characterized the recombinant glucuronyltransferase I (GlcAT-I) involved in the glycosaminoglycan-protein linkage region biosynthesis. The enzyme showed strict specificity for Galβ1-3Galβ1-4Xyl, exhibiting negligible incorporation into other galactoside substrates including Galβ1-3Galβ1-O-benzyl, Galβ1-4GlcNAc and Galβ1-4Glc. A comparison of the GlcAT-I with another β1,3-glucuronyltransferase involved in the HNK-1 epitope biosynthesis revealed that the two β1,3-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. Copyright (C) 1999 Federation of European Biochemical Societies.

Original languageEnglish
Pages (from-to)415-420
Number of pages6
JournalFEBS Letters
Volume459
Issue number3
DOIs
Publication statusPublished - 15-10-1999
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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