Metal ions and prion diseases.
Recent data demonstrate that transition metal ions such as copper not only bind the prion protein with high affinities, but also modify its biochemical properties. This has important consequences for the potential function of the protein in metal-ion transport or as an anti-oxidant molecule. In addition, this relationship between the prion protein and metal ions is likely to play a critical role in the physiopathology of prion diseases.
Lehmann
Sylvain
S
Institut de Génétique Humaine, CNRS U.P.R. 1142, 141, rue de la Cardonille, 34396 Cedex 5, Montpellier, France. Sylvain.Lehmann@igh.cnrs.fr
D000818:Animals; D001665:Binding Sites; D003300:Copper / Q000378:metabolism; D006801:Humans; D017096:Prion Diseases / Q000209:etiology*; D011328:Prions / Q000235:genetics / Q000378:metabolism; D014131:Trace Elements / Q000378:metabolism*
D011328:Prions; D014131:Trace Elements; D003300:Copper