Microheterogeneity of serum glycoproteins and their liver precursors in patients with carbohydrate-deficient glycoprotein syndrome type I: apparent deficiencies in clusterin and serum amyloid P

Détails

ID Serval
serval:BIB_B3FFF804EAE5
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Microheterogeneity of serum glycoproteins and their liver precursors in patients with carbohydrate-deficient glycoprotein syndrome type I: apparent deficiencies in clusterin and serum amyloid P
Périodique
Journal of Laboratory and Clinical Medicine
Auteur(s)
Henry  H., Tissot  J. D., Messerli  B., Markert  M., Muntau  A., Skladal  D., Sperl  W., Jaeken  J., Weidinger  S., Heyne  K., Bachmann  C.
ISSN
0022-2143 (Print)
Statut éditorial
Publié
Date de publication
04/1997
Volume
129
Numéro
4
Pages
412-21
Notes
Journal Article --- Old month value: Apr
Résumé
Serum and liver protein patterns were studied, respectively, in 5 patients (serum) and 1 patient (liver) with carbohydrate-deficient glycoprotein syndrome (CDGS) type I by high-resolution two-dimensional electrophoresis (2-DE) and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The pattern of serum glycoproteins in all 5 patients presented abnormal trains of isoforms with decreased mass (delta molecular weight 3000) and all showed a cathodal shift. Two-dimensional electrophoresis and SDS-PAGE mass analysis of transferrin, alpha1 -antitrypsin, haptoglobin beta-chain, and alpha1-acid glycoprotein after neuraminidase and N-glycosidase F treatments demonstrated that the additional trains of the isoforms found in CDGS type I contain homologous species of isoforms. Some of them still showed charge differences, and all still contained glycans except for transferrin, with some unusual nonglycosylated isoforms. In addition, deficiencies in clusterin and serum amyloid P, not described so far, have been found in all 5 patients. The two-dimensional pattern of immunodetected precursors of serum proteins in liver cells from 1 patient with CDGS showed abnormal low-mass precursors and the absence of the precursors normally found in controls. These results suggest that these abnormal precursors accumulate during the early oligosaccharide processing of the nascent protein-bound oligosaccharides and that glycoprotein precursors undergo an altered intracellular transport while the post-translational processing along the normal pathway is still apparently functioning in patients with CDGS.
Mots-clé
Amyloid/blood/*deficiency Carbohydrate-Deficient Glycoprotein Syndrome/*metabolism Clusterin Electrophoresis, Gel, Two-Dimensional Female Glycoproteins/*deficiency Humans Liver/*metabolism Male *Molecular Chaperones Protein Precursors/*metabolism
Pubmed
Web of science
Création de la notice
25/01/2008 15:34
Dernière modification de la notice
20/08/2019 15:22
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