Cytotoxicity of prion protein peptide (PrP106-126) differs in mechanism from the cytotoxic activity of the Alzheimer's disease amyloid peptide, Aβ25-35

Hope, James, Shearman, Mark S., Baxter, Helen C., Chong, Angela, Kelly, Sharon M. and Price, Nicholas C. (1996) Cytotoxicity of prion protein peptide (PrP106-126) differs in mechanism from the cytotoxic activity of the Alzheimer's disease amyloid peptide, Aβ25-35. Neurodegeneration, 5 (1). pp. 1-11. ISSN 1055-8330

Full text not available from this repository. (Request a copy)

Abstract

The abnormal form of the prion protein (PrP(Sc)), a synthetic prion protein peptide fragment (PrP106-126) and fragments of the Alzheimer's protein precursor, APP, have been shown to be cytotoxic in vitro. We have used synchronous, clonal cell models originally developed to study the toxicity of the Alzheimer's disease amyloid peptide, Aβ25-35, to investigate the actions of PrP peptides. We found that the cytotoxicity of the PrP106-126 depends on its state of aggregation and the cellular expression of PrP(C), and is independent of a loss of MTT reduction activity in the absence of cell death associated with the cellular effects of Aβ25-35. These factors may play a role in the lesion specificity of different pathological phenotypes of prion-protein related diseases.

Item Type:	Article
Uncontrolled Keywords:	amyloid,circular dichroism,cytotoxicity,mtt reduction,prion protein,pathology and forensic medicine,neuropsychology and physiological psychology,clinical neurology ,/dk/atira/pure/subjectarea/asjc/2700/2734
Faculty \ School:	Faculty of Science > School of Biological Sciences
Related URLs:	http://www.scopus.com/inward/record.url?...
Depositing User:	LivePure Connector
Date Deposited:	28 Nov 2025 11:30
Last Modified:	10 Dec 2025 14:30
URI:	https://ueaeprints.uea.ac.uk/id/eprint/101146
DOI:	10.1006/neur.1996.0001

Actions (login required)

View Item