Journal
FEBS LETTERS
Volume 579, Issue 19, Pages 4099-4106Publisher
WILEY
DOI: 10.1016/j.febslet.2005.06.037
Keywords
prion; neuropathology; amyloidoses; intracellular kinases; oxidative stress
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Prion diseases are characterised by severe neural lesions linked to the presence of an abnormal protease-resistant isoform of cellular prion protein (PrPc). The peptide PrP(106-126) is widely used as a model of neurotoxicity in prion diseases. Here, we examine in detail the intracellular signalling cascades induced by PrP(106-126) in cortical neurons and the participation of PrPc. We show that PrP(106-126) induces the activation of subsets of intracellular kinases (e.g., ERK1/2), early growth response 1 synthesis and induces caspase-3 activity, all of which are mediated by nicotinamide adenine dinucleotide phosphate hydrogen-oxidase activity and oxidative stress. However, cells lacking PrPc are similarly affected after peptide exposure, and this questions the involvement of PrPc in these effects. (c) 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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