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

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 hypog...

Full description

Saved in:
Bibliographic Details
Published in:Glycobiology (Oxford) 2000-12, Vol.10 (12), p.1277-1281
Main Authors: Dupré, T, Barnier, A, de Lonlay, P, Cormier-Daire, V, Durand, G, Codogno, P, Seta, N
Format: Article
Language:English
Subjects:
Blotting, Western
Carbohydrate Metabolism, Inborn Errors - metabolism
Glycosylation
Humans
Immunoglobulin G - metabolism
Isoelectric Focusing
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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.
ISSN:0959-6658
1460-2423
DOI:10.1093/glycob/10.12.1277