NR ASLB
AU Rachidi,W.; Riondel,J.; McMahon,H.M.; Favier,A.
TI [Prion protein and copper: a mysterious relationship]
OT La proteine du prion et le cuivre: un lien mysterieux.
QU Pathologie Biologie 2005 May; 53(4): 244-50
PT journal article; review
AB Prion diseases form a group of fatal neurodegenerative disorders including Creutzfeldt-Jakob disease in humans and bovine spongiform encephalopathy in animals. All of which are characterized by the accumulation of abnormally folded isoform of the cellular prion protein (PrPc), denoted PrPsc, which is the major component of infectious prion diseases. The function of PrPc remains elusive. Its amino-terminal region contains a repeated five octapeptide domain that binds copper. The protein is believed to display a superoxide dismutase like activity, and hence a possible protective function against oxidative stress. In this review, relationship between PrP, copper and oxidative stress was analysed. Thus, metal ions and oxidative stress would play an essential role in the pathogenesis of prion diseases and represent important targets for future therapeutic targets or a novel diagnostic marker.
ZR 59
MH Animals; Biological Transport; Brain Chemistry; Chelating Agents/metabolism; Copper/analysis/*chemistry/metabolism/physiology; English Abstract; Humans; Manganese/analysis; Models, Biological; Neurodegenerative Diseases/metabolism; Oxidative Stress; PC12 Cells/drug effects/metabolism; PrPc Proteins/chemistry/metabolism; PrPsc Proteins/chemistry; Prions/*chemistry/metabolism/pathogenicity; Protein Binding; Protein Conformation; Protein Folding; Protein Structure, Tertiary; Rats; Repetitive Sequences, Amino Acid; Solubility; Superoxide Dismutase/metabolism; Virulence
AD Industrial Microbiology, University College Dublin (UCD), Belfield, Ireland. wrachidi@yahoo.com
SP französisch
PO Frankreich