title: Rat's trick to escape Alzheimer's disease.
abstract: Amyloid beta (Abeta) peptides fibril formation and deposition is considered to be the principal pathological hallmark of Alzheimer's disease (AD). However, it remains obscure why AD is precluded by rat/mouse despite the high sequence identity (97%) of rat/mouse Abeta to its human homologue. Based on the recently proposed redox chemistry-based pathogenic model of neurodegenerative diseases, we hypothesize that the lack of key residues of rat/mouse Abeta compared with the human counterpart may account for why rat/mouse is free of AD. At the same time, we propose a new possible redox chemistry-based pathogenic model of AD based on the experimental observations of certain residues in triggering Abeta aggregation. Moreover, it is also interesting to note that non-mammalian Xenopus Abeta contains all the redox chemistry-related key residues and whether it implies that Xenopus Abeta possesses high amyloidogenic potency remains to be determined by further experimental study.
authors.affiliation: Shandong Provincial Research Center for Bioinformatic Engineering and Technique, Center for Advanced Study, Shandong University of Technology, Zibo 255049, P. R. China.
authors.forename: Lian
authors.initials: L
authors.lastname: Shen
authors.forename: Hong-Fang
authors.initials: HF
authors.lastname: Ji
mesh_terms: D000544:Alzheimer Disease / Q000235:genetics / Q000503:physiopathology; D000595:Amino Acid Sequence; D016229:Amyloid beta-Peptides / Q000737:chemistry / Q000235:genetics*; D000818:Animals; D017124:Conserved Sequence; D003300:Copper / Q000737:chemistry; D020022:Genetic Predisposition to Disease; D006801:Humans; D051379:Mice; D008954:Models, Biological; D008969:Molecular Sequence Data; D009154:Mutation; D010084:Oxidation-Reduction; D051381:Rats; D016415:Sequence Alignment; D013045:Species Specificity; D014981:Xenopus; D015032:Zinc / Q000737:chemistry
chemical_list: D016229:Amyloid beta-Peptides; D003300:Copper; D015032:Zinc