NR AVCH
AU Barnham,K.J.; Cappai,R.; Beyreuther,K.; Masters,C.L.; Hill,A.F.
TI Delineating common molecular mechanisms in Alzheimer's and prion diseases
QU Trends in Biochemical Sciences 2006 Aug; 31(8): 465-72
PT journal article; review
AB 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.
ZR 89
MH Alzheimer Disease/*metabolism; Amyloid beta-Protein/chemistry/metabolism/physiology; Animals; Copper/metabolism; Humans; Oxidation-Reduction; Prion Diseases/*metabolism; Prions/chemistry/metabolism/physiology; Protein Structure, Secondary; Research Support, Non-U.S. Gov't
AD Department of Pathology, and Bio21 Molecular Science and Biotechnology Institute, The University of Melbourne, VIC 3010, Australia.
SP englisch
PO England