title: Copper brain homeostasis: role of amyloid precursor protein and prion protein.
abstract: The main proteins associated with Alzheimer's and prion diseases (amyloid precursor protein (APP) and prion protein (PrP(C)), respectively, have binding sites for copper and it has therefore been suggested that they play a role in copper metabolism. Here, we review evidence indicating that the copper binding domains (CuBD) of APP and PrP(C) are able to modulate the oxidation state of copper, and prevent neurotoxic effects and memory impairments induced by copper. Results with transgenic and other animal models have established the relation between these pathogenic proteins and copper. In particular, APP transgenic models, suggest a beneficial effect for copper in AD.
authors.affiliation: Centro de Regulacion Celular y Patología Joaquin V. Luco (CRCP), MIFAB, Facultad de Ciencias Biológicas, Pontificia Universidad Católica de Chile, Santiago, Chile. ninestr@bio.puc.cl
authors.forename: Nibaldo C
authors.initials: NC
authors.lastname: Inestrosa
authors.forename: Waldo
authors.initials: W
authors.lastname: Cerpa
authors.forename: Lorena
authors.initials: L
authors.lastname: Varela-Nallar
mesh_terms: D000544:Alzheimer Disease / Q000378:metabolism; D016564:Amyloid beta-Protein Precursor / Q000737:chemistry / Q000378:metabolism*; D000818:Animals; D001665:Binding Sites; D001921:Brain / Q000378:metabolism*; D003300:Copper / Q000737:chemistry / Q000378:metabolism*; D006706:Homeostasis; D051379:Mice; D008822:Mice, Transgenic; D011328:Prions / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D017434:Protein Structure, Tertiary
chemical_list: D016564:Amyloid beta-Protein Precursor; D011328:Prions; D003300:Copper