Mass spectrometric strategies for the N-glycosylation analisys of serum glycoproteins in patients with congenital disorders of glycosylation (CDG) and galactosemia (Articolo in rivista)

Type
Label
  • Mass spectrometric strategies for the N-glycosylation analisys of serum glycoproteins in patients with congenital disorders of glycosylation (CDG) and galactosemia (Articolo in rivista) (literal)
Anno
  • 2005-01-01T00:00:00+01:00 (literal)
Alternative label
  • L.Sturiale, R.Barone, M.Perez, G.Sorge, J.Jaeken, D.Garozzo (2005)
    Mass spectrometric strategies for the N-glycosylation analisys of serum glycoproteins in patients with congenital disorders of glycosylation (CDG) and galactosemia
    in Glycoconjugate journal
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • L.Sturiale, R.Barone, M.Perez, G.Sorge, J.Jaeken, D.Garozzo (literal)
Pagina inizio
  • 202 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 22 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#note
  • No. Citazione=0; Autocitazione=0; Motore utilizzato per le citazioni=Isiwebofknowledge.com (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • CNR, UNIVERSITA'. (literal)
Titolo
  • Mass spectrometric strategies for the N-glycosylation analisys of serum glycoproteins in patients with congenital disorders of glycosylation (CDG) and galactosemia (literal)
Abstract
  • Congenital disorders of glycosylation (CDG) and galactosemia are inherited metabolic diseases which have in common the occurrence of an abnormal glycosylation pattern of some serum glycoproteins. CDG are due to defects in the synthesis of N-glycans and less frequently affect the O-glycosylation pathway. As glycoproteins are ubiquitous molecules, CDG present as multisystemic disorders with a prominent central nervous system involvement and a variable clinical spectrum. CDG type I defines defects owing to impaired synthesis of the lipid-linked oligosaccharide and/or its transfer to the nascent glycoprotein in the cytosol and in the endoplasmic reticulum, CDG type II refers to abnormalities in the glycoprotein processing at the Golgi level. The most common form of galactosemia, due to a deficiency of galactose-1-phosphate uridyltransferase (GalT), causes accumulation of galactose and galactose-1-phosphate in blood and tissues, and if untreated, produces severe symptoms as mental retardation, cirrhosis of the liver, and cataracts. In both CDG and galactosemia an abnormal glycosylation pattern involving multiple serum glycoproteins may be promptly detectable by the isoelectric focusing (IEF) of serum proteins following by immunodetection of transferrin isoforms which show a cathodal shift due to the absence of terminal negatively charged sialic acid residues. Although IEF allows the measurements of the sialylation degree in serum transferrin, it is uninformative about the presence of isoforms due to the partial occupancy of one or both transferrin glycosylation sites and the detailed analysis of the N-glycan structures. In order to identify glycosylation abnormalities both in CDG and in galactosemia patients, additional techniques such as matrix assisted laser-desorption ionisation (MALDI) and Electrospray mass spectrometry may be essential. We used mass spectrometry based strategy to define the glycosylation degree of intact glycoproteins and to detect changes in serum protein N-glycan profiles. These findings open the way to a better understanding of the biochemical mechanisms of defective glycosylation. (literal)
Prodotto di
Autore CNR

Incoming links:


Autore CNR di
Prodotto
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi
data.CNR.it