Abstract
Prion diseases are progressive neurodegenerative maladies that are characterised by changes in the physical properties and turnover of a glycosylphosphatidyl-inositol (GPI)-linked membrane glycoprotein (cellular prion protein, PrPC). The conversion of the normal, detergent-soluble, proteinase K (PK)- sensitive PrPSc to the abnormal, detergent-insoluble, partially PK-resistant isoform, PrPse is a common feature of all these transmissible encephalophies including scrapie in sheep, Creutzfeldt-Jakob disease (CJD) of humans and bovine spongiform encephalopathy (BSE) of cattle [1]. Direct interaction between PrPC and PrPSc is implicated by in vivo studies and features in current ideas of molecular pathogenesis and transmissibility such as the heterodimer (template-assisted) and nucleation (seed)-dependent conversion models (Fig. 1). In 1994, Caughey and co-workers introduced a new tool for investigating this process by showing that PrPSc isolated from the brains of scrapieaffected animals could induce the conversion of radiolabelled recombinant PrP (rPrP) into a PK-resistant isoform, PrPres, in vitro [1-5].
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Kirby, L., Hope, J. (2004). Cell-Free Conversion of Prion Proteins. In: Lehmann, S., Grassi, J. (eds) Techniques in Prion Research. Methods and Tools in Biosciences and Medicine. Birkhäuser, Basel. https://doi.org/10.1007/978-3-0348-7949-1_12
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DOI: https://doi.org/10.1007/978-3-0348-7949-1_12
Publisher Name: Birkhäuser, Basel
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