Abstract
The aggregation of a soluble protein into insoluble, β-sheet rich amyloid fibrils is a defining characteristic of many neurodegenerative diseases, including prion disorders. The prion protein has so far been considered unique because of its infectious nature. Recent investigations, however, suggest that other amyloidforming proteins associated with much more common diseases, such as tau, α-synuclein, amyloid β and polyglutamine proteins, while not infectious in the classical sense, share certain essential properties with prions that may explain phenotypic diversity, and patterns of spread within the nervous system. We suggest a common mechanism of pathogenesis of myriad sporadic and inherited neurodegenerative diseases based on templated conformational change.
Original language | English (US) |
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Pages (from-to) | 23-26 |
Number of pages | 4 |
Journal | Prion |
Volume | 3 |
Issue number | 2 |
State | Published - Apr 2009 |
Keywords
- α-synuclein
- Amyloid β
- Fibril
- Neurodegeneration
- Polyglutamine
- Prion
- Propagation
- Tau
ASJC Scopus subject areas
- Biochemistry
- Cell Biology
- Infectious Diseases
- Cellular and Molecular Neuroscience