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PrP(106-126) activates neuronal intracellular kinases and Egr1 synthesis through activation of NADPH-oxidase independently of PrPc.

Gavín, R; Braun, N; Nicolas, O; Parra, B; Ureña, J M; Mingorance, A; Soriano, E; Torres, J M; Aguzzi, A; del Río, J A (2005). PrP(106-126) activates neuronal intracellular kinases and Egr1 synthesis through activation of NADPH-oxidase independently of PrPc. FEBS Letters, 579(19):4099-4106.

Abstract

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.

Additional indexing

Item Type:Journal Article, refereed, original work
Communities & Collections:04 Faculty of Medicine > University Hospital Zurich > Institute of Neuropathology
Dewey Decimal Classification:570 Life sciences; biology
610 Medicine & health
Scopus Subject Areas:Life Sciences > Biophysics
Life Sciences > Structural Biology
Life Sciences > Biochemistry
Life Sciences > Molecular Biology
Life Sciences > Genetics
Life Sciences > Cell Biology
Uncontrolled Keywords:Biophysics, Genetics, Cell Biology, Biochemistry, Molecular Biology, Structural Biology
Language:English
Date:1 August 2005
Deposited On:11 Feb 2008 12:27
Last Modified:01 Jul 2025 03:44
Publisher:Elsevier
ISSN:0014-5793
OA Status:Closed
Publisher DOI:https://doi.org/10.1016/j.febslet.2005.06.037
PubMed ID:16023105
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