Breakthroughs and views - Prion disease: A loss of antioxidant function?

Citation
Bs. Wong et al., Breakthroughs and views - Prion disease: A loss of antioxidant function?, BIOC BIOP R, 275(2), 2000, pp. 249-252
Citations number
32
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Biochemistry & Biophysics
Journal title
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
ISSN journal
0006-291X → ACNP
Volume
275
Issue
2
Year of publication
2000
Pages
249 - 252
Database
ISI
SICI code
0006-291X(20000828)275:2<249:BAV-PD>2.0.ZU;2-E
Abstract
Prion disease, a neurodegenerative disorder, is widely believed to arise wh en a cellular prion protein (PrPC) undergoes conformational changes to a pa thogenic isoform (PrPSc), Recent data have shown PrPC to be copper binding and that it acquires antioxidant activity as a result. This enzymatic prope rty is dependent mainly on copper binding to the octarepeats region. In nor mal human brain and human prion disease, there is a population of brain-der ived PrP that has been truncated at the N-terminal which encompassed the oc tarepeats region. Increasing evidences have suggested imbalances of metal-c atalyzed reactions to be the common denominator for several neurodegenerati ve diseases. Therefore, we propose that one of the causative factors for pr ion disease could be due to the imbalances in metal-catalyzed reactions res ulting in an alteration of the antioxidant function. These result in an inc rease level of oxidative stress and, as such, trigger the neurodegenerative cascade. (C) 2000 Academic Press.