Amyloid formation: age-related mechanism in Creutzfeldt-Jakob disease?

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.

• Authors: L Luers, G Panza, F Henke, T Agyenim, J Weiss, D Willbold, E Birkmann
• Journal: Rejuvenation research (Rejuvenation Res) 2010 Apr-Jun Vol. 13 Issue 2-3 Pg. 214-6 ISSN: 1557-8577 [Electronic] United States
• PMID: 20017612 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Amyloid
• Benzothiazoles
• PrPSc Proteins
• Recombinant Proteins
• Thiazoles
• thioflavin T
• Congo Red

Topics

• Aging (metabolism, physiology)
• Amyloid (metabolism)
• Benzothiazoles
• Circular Dichroism
• Congo Red (pharmacology)
• Creutzfeldt-Jakob Syndrome (etiology, metabolism, pathology)
• Humans
• In Vitro Techniques
• Microscopy, Electron, Transmission
• Models, Biological
• PrPSc Proteins (chemistry, metabolism)
• Recombinant Proteins (analysis, chemistry, metabolism)
• Staining and Labeling
• Thiazoles (pharmacology)