1. Amyloid formation: age-related mechanism in Creutzfeldt-Jakob disease?
- Author
-
Luers L, Panza G, Henke F, Agyenim T, Weiss J, Willbold D, and Birkmann E
- Subjects
- Aging physiology, Benzothiazoles, Circular Dichroism, Congo Red pharmacology, Creutzfeldt-Jakob Syndrome etiology, Creutzfeldt-Jakob Syndrome pathology, Humans, In Vitro Techniques, Microscopy, Electron, Transmission, Models, Biological, PrPSc Proteins chemistry, PrPSc Proteins metabolism, Recombinant Proteins analysis, Recombinant Proteins chemistry, Recombinant Proteins metabolism, Staining and Labeling, Thiazoles pharmacology, Aging metabolism, Amyloid metabolism, Creutzfeldt-Jakob Syndrome metabolism
- Abstract
Protein aggregation occurs in many age-related neurodegenerative diseases, where it can lead to deposits of naturally occurring proteins in the brain. In case of Creutzfeldt-Jakob disease (CJD), these deposits consist of prion protein (PrP). CJD has three etiologies: spontaneous, genetic, or caused by infection. A polymorphism within the PrP gene is associated with susceptibility of infection. The main event in prion diseases is the conversion of PrP from its naturally occurring isoform to its disease-associated isoform. Here, we present the adaption of a previously reported in vitro conversion system based on hamster recombinant PrP to analyze amyloid fibril formation of human recombinant PrP. We further compare the aggregation characteristics of the human PrP according to the polymorphism variants M129 and V129.
- Published
- 2010
- Full Text
- View/download PDF