The propagation of prion-like protein inclusions in neurodegenerative diseases

Trends Neurosci. 2010 Jul;33(7):317-25. doi: 10.1016/j.tins.2010.04.003. Epub 2010 May 20.


The most common neurodegenerative diseases, including Alzheimer's disease and Parkinson's disease, are characterized by the misfolding of a small number of proteins that assemble into ordered aggregates in affected brain cells. For many years, the events leading to aggregate formation were believed to be entirely cell-autonomous, with protein misfolding occurring independently in many cells. Recent research has now shown that cell non-autonomous mechanisms are also important for the pathogenesis of neurodegenerative diseases with intracellular filamentous inclusions. The intercellular transfer of inclusions made of tau, alpha-synuclein, huntingtin and superoxide dismutase 1 has been demonstrated, revealing the existence of mechanisms reminiscent of those by which prions spread through the nervous system.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Humans
  • Inclusion Bodies / chemistry
  • Inclusion Bodies / metabolism*
  • Neurodegenerative Diseases / genetics
  • Neurodegenerative Diseases / metabolism*
  • Neurodegenerative Diseases / pathology*
  • Prion Diseases / genetics
  • Prion Diseases / metabolism
  • Prion Diseases / pathology
  • Prions / genetics
  • Prions / metabolism*
  • Protein Folding
  • tau Proteins / genetics
  • tau Proteins / metabolism


  • Prions
  • tau Proteins