Cell-to-cell transmission of non-prion protein aggregates

Nat Rev Neurol. 2010 Dec;6(12):702-6. doi: 10.1038/nrneurol.2010.145. Epub 2010 Oct 12.


Neurodegenerative disorders such as Alzheimer disease, Parkinson disease, frontotemporal dementia, Huntington disease and Creutzfeldt-Jakob disease (CJD) are characterized by progressive accumulation of protein aggregates in selected brain regions. Protein misfolding and templated assembly into aggregates might result from an imbalance between protein synthesis, aggregation and clearance. Although protein misfolding and aggregation occur in most neurodegenerative disorders, the concept of spreading and infectivity of aggregates in the CNS has, until now, been confined to prion diseases such as CJD and bovine spongiform encephalopathy. Emerging evidence, however, suggests that prion-like spreading, involving secreted proteins such as amyloid-β and cytosolic proteins such as tau, huntingtin and α-synuclein, can occur in other neurodegenerative disorders. The underlying molecular mechanisms and the therapeutic implications of the new data are discussed in this article.

Publication types

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

MeSH terms

  • Animals
  • Humans
  • Nerve Tissue Proteins / metabolism*
  • Neurodegenerative Diseases* / etiology
  • Neurodegenerative Diseases* / metabolism
  • Neurodegenerative Diseases* / pathology
  • Neurons / metabolism*
  • Neurons / pathology*
  • Plaque, Amyloid* / etiology
  • Plaque, Amyloid* / metabolism
  • Plaque, Amyloid* / pathology


  • Nerve Tissue Proteins