title: Alzheimer's disease. Molecular consequences of presenilin-1 mutation.
abstract: Alzheimer's disease is characterized by accumulation in the brain of a family of insoluble amyloid peptides (Abeta peptides), which are produced as a result of the normal processing of beta-amyloid precursor protein (beta-APP). Russo et al. claim that a truncated Abeta peptide that lacks the first ten amino acids accumulates in the brains of patients carrying a mutant form of pre-senilin 1 (PS1), a protein that is involved in cleavage of beta-APP. However, we have found that this same species is also overrepresented in Alzheimer's patients with mutations in beta-APP itself. Our findings do not support the conclusion of Russo et al. that pathogenic PS1 mutations may control cleavage of beta-APP by beta-secretase.
authors.affiliation: Sir James McCusker Alzheimer Research Unit, University of Western Australia, Perth, Australia and Department of Psychiatry, New York University School of Medicine, New York 10962, USA. samgandy@earthlink.net
authors.forename: S
authors.initials: S
authors.lastname: Gandy
authors.forename: J
authors.initials: J
authors.lastname: Naslund
authors.forename: C
authors.initials: C
authors.lastname: Nordstedt
mesh_terms: D000368:Aged; D000544:Alzheimer Disease / Q000235:genetics*; D000682:Amyloid / Q000378:metabolism; D053829:Amyloid Precursor Protein Secretases; D016564:Amyloid beta-Protein Precursor / Q000378:metabolism; D016282:Aspartic Acid Endopeptidases; D001921:Brain / Q000378:metabolism; D010450:Endopeptidases / Q000378:metabolism; D006801:Humans; D008565:Membrane Proteins / Q000235:genetics* / Q000378:metabolism; D009154:Mutation; D053764:Presenilin-1
chemical_list: D000682:Amyloid; D016564:Amyloid beta-Protein Precursor; D008565:Membrane Proteins; C508853:PSEN1 protein, human; D053764:Presenilin-1; D053829:Amyloid Precursor Protein Secretases; D010450:Endopeptidases; D016282:Aspartic Acid Endopeptidases; C509280:BACE1 protein, human