NR ASIS
AU Brown,D.R.; Kozlowski,H.
TI Biological inorganic and bioinorganic chemistry of neurodegeneration based on prion and Alzheimer diseases
QU Dalton Transactions 2004 Jul 7(13): 1907-17
PT journal article; review
AB A change of the prion protein conformation results in a class of neurodegenerative diseases called the transmissible spongiform encephalopathies (like mad cow and Creutzfeldt-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.
ZR 163
MH Alzheimer Disease/*metabolism/pathology; Amyloid beta-Protein Precursor/chemistry/metabolism; Animals; *Chemistry, Bioinorganic; Humans; Metals/chemistry/metabolism; Nerve Degeneration/*metabolism/pathology; Prions/*chemistry/*metabolism; Research Support, Non-U.S. Gov't
AD Department of Biology and Biochemistry, University of Bath, UK BA2 7AY. bssdrb@bath.ac.uk
SP englisch
PO England