title: Aggregation of amyloid precursor proteins by aluminum in vitro.
abstract: The effect of various metal ions on aggregation of human recombinant amyloid precursor protein (APP) in vitro was investigated based on characterizations of altered migration on SDS-PAGE or immunoblots. Most biological metal ions tested had no significant effect on aggregation of APP. In contrast, AlCl3 in particular promoted aggregation of APP or APP-CT105 in a dose dependent manner. This effect of AlCl3 on APP mobility shift was prevented or reversed by the metal chelator, EDTA. Amorphous aggregates were observed in AlCl3 treated APP when examined by EM. These results suggest that aluminum may play a role in the pathogenesis of AD by directly promoting aggregation of APP.
authors.affiliation: Department of Pharmacology, College of Medicine, Seoul National University, South Korea.
authors.forename: Y H
authors.initials: YH
authors.lastname: Chong
authors.forename: Y H
authors.initials: YH
authors.lastname: Suh
mesh_terms: D000535:Aluminum / Q000494:pharmacology*; D017607:Aluminum Compounds / Q000494:pharmacology; D016564:Amyloid beta-Protein Precursor / Q000187:drug effects*; D015153:Blotting, Western; D006801:Humans; D015151:Immunoblotting; D066298:In Vitro Techniques; D008670:Metals / Q000494:pharmacology
chemical_list: D017607:Aluminum Compounds; D016564:Amyloid beta-Protein Precursor; D008670:Metals; D000535:Aluminum