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...

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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
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description 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.
doi_str_mv 10.1093/glycob/10.12.1277
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subjects Blotting, Western
Carbohydrate Metabolism, Inborn Errors - metabolism
Glycosylation
Humans
Immunoglobulin G - metabolism
Isoelectric Focusing
title Defect in N-glycosylation of proteins is tissue-dependent in congenital disorders of glycosylation Ia
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