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Copper brain homeostasis: Role of amyloid precursor protein and prion protein
Author(s) -
Inestrosa Nibaldo C.,
Cerpa Waldo,
VarelaNallar Lorena
Publication year - 2005
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216540500264620
Subject(s) - copper , amyloid precursor protein , prion protein , genetically modified mouse , copper metabolism , transgene , chemistry , amyloid (mycology) , homeostasis , biochemistry , microbiology and biotechnology , biology , alzheimer's disease , medicine , gene , inorganic chemistry , disease , organic chemistry
The main proteins associated with Alzheimer's and prion diseases (amyloid precursor protein (APP) and prion protein (PrPC), 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 PrPC 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.IUBMB Life, 57: 645‐650, 2005