Journal
PROTEOMICS CLINICAL APPLICATIONS
Volume 3, Issue 5, Pages 609-622Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/prca.200800213
Keywords
Cirrhosis; Glycomics; Glycoproteomics; Glycosylation disorders; IgA
Funding
- Centre National de la Recherche
- Unite Mixte de Recherche CNRS/UST [8576]
- Ministre de la Recherche et de l'Enseignement Superieur
- Mass Spectrometry facility
- European Community (FEDER)
- Region Nord-Pas de Calais (France)
- Universite des Sciences et Technologies de Lille
Ask authors/readers for more resources
Many modifications in N-glycosylation have been demonstrated in hepatic cirrhosis. These modifications correspond to an increase of a bisecting core alpha (1,6)-fucosylated biantermary glycan, an increase in core fucosylation, and the presence of an important population of neutral oligosaccharides in human serum of cirrhotic patients. In this study, a glycoproteomic approach which consists of lectin affinity chromatography, MALDI-TOF MS for the characterization of N-glycans released from glycoproteins, one- and 2-D PAGE, electrospray ionization quadrupole ion trap (ESI-QIT) MS was used to identify serum fucosylated glycoproteins related to cirrhosis. Employing this method, we have shown that IgA is one of the major proteins that is responsible of the glycosylation modifications observed in the serum N-glycome of cirrhotic patients. To our knowledge, this is the first time that aberrant N-glycosylation of IgA in cirrhosis is described.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available