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 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.
Dupré
T
T
Biochimie A, Hôpital Bichat, 75877 Paris cedex 18, France.
Barnier
A
A
de Lonlay
P
P
Cormier-Daire
V
V
Durand
G
G
Codogno
P
P
Seta
N
N
D015153:Blotting, Western; D002239:Carbohydrate Metabolism, Inborn Errors / Q000378:metabolism*; D006031:Glycosylation; D006801:Humans; D007074:Immunoglobulin G / Q000378:metabolism; D007525:Isoelectric Focusing
D007074:Immunoglobulin G