Defect in N-glycosylation of proteins is tissue-dependent in congenital disorders of glycosylation Ia

Glycobiology. 2000 Dec;10(12):1277-81. doi: 10.1093/glycob/10.12.1277.

Abstract

The biochemical hallmark of Congenital Disorders of Glycosylation (CDG) including type Ia is a defective N-glycosylation of serum glycoproteins. Hypoglycosylated forms of alpha1-antitrypsin have been detected by Western blot in serum from CDG Ia patients. In contrast we were not able to detect hypoglycosylation in alpha1-antitrypsin synthesized by fibroblasts, keratinocytes, enterocytes, and leukocytes. Similarly no hypoglycosylation was detectable in a membrane-associated N-linked glycoprotein, the facilitative glucose transporter GLUT-1 and also in serum immunoglobulin G isolated from sera of CDG Ia patients. We conclude that the phenotypic expression of CDG Ia is tissue-dependent.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Blotting, Western
  • Carbohydrate Metabolism, Inborn Errors / metabolism*
  • Glycosylation
  • Humans
  • Immunoglobulin G / metabolism
  • Isoelectric Focusing

Substances

  • Immunoglobulin G