Skip Navigation

This Article
Right arrow Full Text Freely available
Right arrow FREE Full Text (PDF) Freely available
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (14)
Right arrowRequest Permissions
Right arrow Disclaimer
Google Scholar
Right arrow Articles by Dupré, T.
Right arrow Articles by Seta, N.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Dupré, T.
Right arrow Articles by Seta, N.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Glycobiology, 2000, Vol. 10, No. 12 1277-1281
© 2000 Oxford University Press

Defect in N-glycosylation of proteins is tissue-dependent in Congenital Disorders of Glycosylation Ia

Thierry Dupré1,2, Anne Barnier2, Pascale de Lonlay3, Valérie Cormier-Daire4, Geneviève Durand2,6, Patrice Codogno5 and Nathalie Seta2,7

2Biochimie A, Hôpital Bichat, 75877 Paris cedex 18, France, 3Service de Pédiatrie et maladies métaboliques, 4Service de Génétique Médicale, INSERM U393, Hôpital Necker, 75743 Paris cedex 15, France, 5INSERM U504, 94807 Villejuif cedex, France, 6Faculté de Pharmacie, Université Paris XI, 92260 Châtenay-Malabry cedex, France, and 7Faculté de Pharmacie, Université Paris V, 75270 Paris cedex 06, France

The biochemical hallmark of Congenital Disorders of Glycosylation (CDG) including type Ia is a defective N-glycosylation of serum glycoproteins. Hypoglycosylated forms of {alpha}1-antitrypsin have been detected by Western blot in serum from CDG Ia patients. In contrast we were not able to detect hypoglycosylation in {alpha}1-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.

1 To whom correspondence should be addressed at: Laboratoire de Biochimie A Hôpital Bichat–Claude Bernard, 46 rue H. Huchard, 75877 Paris cédex 18, France


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
N. Gao, J. Shang, and M. A. Lehrman
Analysis of Glycosylation in CDG-Ia Fibroblasts by Fluorophore-assisted Carbohydrate Electrophoresis: IMPLICATIONS FOR EXTRACELLULAR GLUCOSE AND INTRACELLULAR MANNOSE 6-PHOSPHATE
J. Biol. Chem., May 6, 2005; 280(18): 17901 - 17909.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
J. Shang and M. A. Lehrman
Metformin-stimulated Mannose Transport in Dermal Fibroblasts
J. Biol. Chem., March 12, 2004; 279(11): 9703 - 9712.
[Abstract] [Full Text] [PDF]

Home page
 GlycobiologyHome page
M. Butler, D. Quelhas, A. J. Critchley, H. Carchon, H. F. Hebestreit, R. G. Hibbert, L. Vilarinho, E. Teles, G. Matthijs, E. Schollen, et al.
Detailed glycan analysis of serum glycoproteins of patients with congenital disorders of glycosylation indicates the specific defective glycan processing step and provides an insight into pathogenesis
Glycobiology, September 1, 2003; 13(9): 601 - 622.
[Abstract] [Full Text] [PDF]

Home page
 GlycobiologyHome page
N. Callewaert, E. Schollen, A. Vanhecke, J. Jaeken, G. Matthijs, and R. Contreras
Increased fucosylation and reduced branching of serum glycoprotein N-glycans in all known subtypes of congenital disorder of glycosylation I
Glycobiology, May 1, 2003; 13(5): 367 - 375.
[Abstract] [Full Text] [PDF]

Home page
 GlycobiologyHome page
Y. Wang, J. Tan, M. Sutton-Smith, D. Ditto, M. Panico, R. M. Campbell, N. M. Varki, J. M. Long, J. Jaeken, S. R. Levinson, et al.
Modeling human congenital disorder of glycosylation type IIa in the mouse: conservation of asparagine-linked glycan-dependent functions in mammalian physiology and insights into disease pathogenesis
Glycobiology, December 1, 2001; 11(12): 1051 - 1070.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.