Increased α3‐fucosylation of α1‐acid glycoprotein in patients with congenital disorder of glycosylation type IA (CDG‐Ia)

FEBS Letters

Poland, Dennis¹  Koeleman, Carolien¹  Van het Hof, Bert¹  Jakobs, Cornelis³  Van Dijk, Willem¹  Jaeken, Jaak² 

[1]Glycoimmunology Group, Department of Molecular Cell Biology, Research Institute Immunology and Inflammatory Disease, VU Medical Centre, Van der Boechorststraat 7, 1081 BT Amsterdam, The Netherlands

[2]Department of Paediatrics, University Hospital Gasthuisberg, Herestraat 29, B-3000 Leuven, Belgium

[3]Department of Clinical Chemistry, VU Medical Centre, P.O. Box 7047, 1007 MB Amsterdam, The Netherlands

关键词: Congenital disorder of glycosylation type IA;    α1-Acid glycoprotein;    Sialyl Lewisx;    Fucosylation;    Inflammation;    Branching;   

DOI  :  10.1016/S0014-5793(01)02349-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Increased fucosylation of the type (sialyl) Lewis^x was detected on the acute-phase plasma protein α₁-acid glycoprotein (AGP) in patients with the congenital disorder of glycosylation type IA. This is remarkable, because in these patients the biosynthesis of guanosine 5′-diphosphate (GDP)-D-mannose is strongly decreased, and GDP-D-mannose is the direct precursor for GDP-L-fucose, the substrate for fucosyltransferases. The concomitantly occurring increased branching of the glycans of AGP and the increased fucosyltransferase activity in plasma suggest that a chronic hepatic inflammatory reaction has induced the increase in fucosylation.

【 授权许可】

Unknown