title: Delineating common molecular mechanisms in Alzheimer's and prion diseases.
abstract: The structure of the infectious agent responsible for prion diseases has not been fully characterized, but evidence points to a beta-rich conformer of the host-encoded prion protein. Amyloid-beta peptide (Abeta), a proteolytic fragment generated from the amyloid precursor protein, has been implicated as the toxic molecule involved in the pathogenesis of Alzheimer's disease. The mechanism of Abeta toxicity might be mediated through the coordination of redox-active transition-metal ions such as copper leading to the generation of reactive oxygen species, coupled with the propensity to interact with lipid bilayers. Key sequence and chemical similarities between prion protein (PrP) and Abeta indicate that similar therapeutic strategies might be applicable for the treatment of Alzheimer's and prion diseases.
authors.affiliation: Department of Pathology, and Bio21 Molecular Science and Biotechnology Institute, The University of Melbourne, VIC 3010, Australia.
authors.forename: Kevin J
authors.initials: KJ
authors.lastname: Barnham
authors.forename: Roberto
authors.initials: R
authors.lastname: Cappai
authors.forename: Konrad
authors.initials: K
authors.lastname: Beyreuther
authors.forename: Colin L
authors.initials: CL
authors.lastname: Masters
authors.forename: Andrew F
authors.initials: AF
authors.lastname: Hill
mesh_terms: D000544:Alzheimer Disease / Q000378:metabolism*; D016229:Amyloid beta-Peptides / Q000737:chemistry / Q000378:metabolism / Q000502:physiology; D000818:Animals; D003300:Copper / Q000378:metabolism; D006801:Humans; D010084:Oxidation-Reduction; D017096:Prion Diseases / Q000378:metabolism*; D011328:Prions / Q000737:chemistry / Q000378:metabolism / Q000502:physiology; D017433:Protein Structure, Secondary
chemical_list: D016229:Amyloid beta-Peptides; D011328:Prions; D003300:Copper