Prion-like spread of protein aggregates in neurodegeneration

J Exp Med. 2012 May 7;209(5):889-93. doi: 10.1084/jem.20120741.

Abstract

Protein misfolding is common to most neurodegenerative diseases, including Alzheimer's and Parkinson's diseases. Recent work using animal models with intracellular α-synuclein and tau inclusions adds decisively to a growing body of evidence that misfolded protein aggregates can induce a self-perpetuating process that leads to amplification and spreading of pathological protein assemblies. When coupled with the progressive nature of neurodegeneration, recognition of such cell-to-cell aggregate spread suggests a unifying mechanism underlying the pathogenesis of these disorders.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Humans
  • Mice
  • Neurodegenerative Diseases / etiology*
  • Neurodegenerative Diseases / physiopathology*
  • Neurofibrillary Tangles / chemistry*
  • Neurofibrillary Tangles / pathology
  • Prions / chemistry*
  • Proteostasis Deficiencies / complications*
  • Proteostasis Deficiencies / physiopathology*
  • alpha-Synuclein / chemistry*
  • tau Proteins / chemistry*

Substances

  • Prions
  • alpha-Synuclein
  • tau Proteins