Biological inorganic and bioinorganic chemistry of neurodegeneration based on prion and Alzheimer diseases.
A change of the prion protein conformation results in a class of neurodegenerative diseases called the transmissible spongiform encephalopathies (like mad cow and Creutzfeld-Jakob diseases). The function of the normal prion protein is unknown, although much of recent research demonstrates the it may be a copper binding protein selective for Cu(II). Amyloid precursor protein (APP) releases the 39-42 amino acid peptide, a major constituent of the deposit in plaques of Alzheimer disease brain. Also APP is a metal binding protein, including copper ions. The link between copper and both proteins may provide insight into the role of metals in neurodegenerative pathologies.
Brown
David R
DR
Department of Biology and Biochemistry, University of Bath, UK BA2 7AY. bssdrb@bath.ac.uk
Kozlowski
Henryk
H
D000544:Alzheimer Disease / Q000378:metabolism* / Q000473:pathology; D016564:Amyloid beta-Protein Precursor / Q000737:chemistry / Q000378:metabolism; D000818:Animals; D015393:Chemistry, Bioinorganic; D006801:Humans; D008670:Metals / Q000737:chemistry / Q000378:metabolism; D009410:Nerve Degeneration / Q000378:metabolism* / Q000473:pathology; D011328:Prions / Q000737:chemistry* / Q000378:metabolism*
D016564:Amyloid beta-Protein Precursor; D008670:Metals; D011328:Prions