Turnbull, Stuart and Tabner, Brian J. and Brown, David R. and Allsop, David (2003) Quinacrine acts as an antioxidant and reduces the toxicity of the prion peptide PrP106-126. NeuroReport, 14 (13). pp. 1743-1745. ISSN 1473-558XFull text not available from this repository.
The accumulation of protein aggregates in the brain is a central feature of several different neurodegenerative diseases. We have recently shown that A[beta] and [alpha]-synuclein, associated with Alzheimer's disease, Parkinson's disease and related disorders, can both induce the formation of hydroxyl radicals following incubation in solution, upon addition of Fe(II). PrP106-126, a model peptide for the study of prion protein-mediated cell death, shares the same property. In this study we show that quinacrine (an anti-malarial drug and inhibitor of prion replication) acts as an effective antioxidant, readily scavenging hydroxyl radicals formed from hydrogen peroxide via the Fenton reaction or generated during incubation of the PrP106-126 peptide. Furthermore, the toxicity of PrP106-126 to cultured cells was significantly inhibited by quinacrine.
|Journal or Publication Title:||NeuroReport|
|Subjects:||Q Science > QH Natural history > QH301 Biology|
|Departments:||Faculty of Science and Technology > Lancaster Environment Centre|
Faculty of Health and Medicine > Biomedical & Life Sciences
|Deposited By:||Prof David Allsop|
|Deposited On:||15 May 2008 11:44|
|Last Modified:||17 Mar 2016 01:14|
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