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

• Published in: Glycobiology (Oxford) Vol. 10; no. 12; pp. 1277 - 1281
• Main Authors: Dupré, T, Barnier, A, de Lonlay, P, Cormier-Daire, V, Durand, G, Codogno, P, Seta, N
• Format: Journal Article
• Language: English
• Published: England Oxford Publishing Limited (England) 01-12-2000
• Subjects: Blotting, Western; Carbohydrate Metabolism, Inborn Errors - metabolism; Glycosylation; Humans; Immunoglobulin G - metabolism; Isoelectric Focusing
• ISSN: 0959-6658; 1460-2423
• DOI: 10.1093/glycob/10.12.1277

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.