The expanding realm of prion phenomena in neurodegenerative disease

Bess Frost, Marc I. Diamond

Research output: Contribution to journalComment/debate

25 Scopus citations

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 languageEnglish (US)
Pages (from-to)74-77
Number of pages4
JournalPrion
Volume3
Issue number2
StatePublished - Jan 1 2009

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Keywords

  • Amyloid β
  • Fibril
  • Neurodegeneration
  • Polyglutamine
  • Prion
  • Propagation
  • Tau
  • α-synuclein

ASJC Scopus subject areas

  • Biochemistry
  • Cellular and Molecular Neuroscience
  • Cell Biology
  • Infectious Diseases

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