Congenital disorders of glycosylation type I leads to altered processing of N-linked glycans, as well as underglycosylation

Biochem J. 2001 Oct 15;359(Pt 2):249-54. doi: 10.1042/0264-6021:3590249.

Abstract

The N-linked glycans on transferrin and alpha(1)-antitrypsin from patients with congenital disorders of glycosylation type I have increased fucosylation and branching relative to normal controls. The elevated levels of monofucosylated biantennary glycans are probably due to increased alpha-(1-->6) fucosylation. The presence of bi- and trifucosylated triantennary and tetra-antennary glycans indicated that peripheral alpha-(1-->3), as well as core alpha-(1-->6), fucosylation is increased. Altered processing was observed on both the fully and underglycosylated glycoforms.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amidohydrolases
  • Carbohydrate Metabolism, Inborn Errors / classification
  • Carbohydrate Metabolism, Inborn Errors / metabolism*
  • Carbohydrate Sequence
  • Case-Control Studies
  • Electrophoresis, Gel, Two-Dimensional
  • Fucose / chemistry
  • Fucose / metabolism
  • Glycosylation
  • Humans
  • Molecular Sequence Data
  • Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase
  • Polysaccharides / chemistry
  • Polysaccharides / metabolism*
  • Protein Processing, Post-Translational
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
  • Transferrin / chemistry
  • Transferrin / metabolism
  • alpha 1-Antitrypsin / chemistry
  • alpha 1-Antitrypsin / metabolism

Substances

  • Polysaccharides
  • Transferrin
  • alpha 1-Antitrypsin
  • Fucose
  • Amidohydrolases
  • Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase