title: Soluble derivatives of beta/A4 amyloid protein precursor in human cerebrospinal fluid are both N- and O-glycosylated.
abstract: The linkage of the glycan chain to the beta/A4 amyloid protein precursor (APP) in cerebrospinal fluid (CSF) was studied by Western blot analysis. The apparent molecular weight of APP in CSF was reduced from 103 to 100 kDa by N-glycanase, and to 96 kDa by O-glycanase treatment, respectively. These data indicate that APP is both N- and O-glycosylated in one molecule. The extent of glycosylation of APP was not altered in the CSF from patients with Alzheimer's disease.
authors.affiliation: Department of Neurology, School of Medicine, Tokyo Medical and Dental University, Japan.
authors.forename: F
authors.initials: F
authors.lastname: Saito
authors.forename: K
authors.initials: K
authors.lastname: Yanagisawa
authors.forename: T
authors.initials: T
authors.lastname: Miyatake
mesh_terms: D000328:Adult; D000368:Aged; D000544:Alzheimer Disease / Q000134:cerebrospinal fluid*; D016564:Amyloid beta-Protein Precursor / Q000031:analogs & derivatives* / Q000134:cerebrospinal fluid* / Q000302:isolation & purification; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D006026:Glycoside Hydrolases; D006031:Glycosylation; D006801:Humans; D008297:Male; D008970:Molecular Weight; D009439:Neuraminidase; D012016:Reference Values
chemical_list: D016564:Amyloid beta-Protein Precursor; D006026:Glycoside Hydrolases; C020668:glycanase; D009439:Neuraminidase