When amyloids become prions

Prion. 2014;8(3):233-9. doi: 10.4161/19336896.2014.968464. Epub 2014 May 15.

Abstract

The conformational diseases, linked to protein aggregation into amyloid conformations, range from non-infectious neurodegenerative disorders, such as Alzheimer disease (AD), to highly infectious ones, such as human transmissible spongiform encephalopathies (TSEs). They are commonly known as prion diseases. However, since all amyloids could be considered prions (from those involved in cell-to-cell transmission to those responsible for real neuronal invasion), it is necessary to find an underlying cause of the different capacity to infect that each of the proteins prone to form amyloids has. As proposed here, both the intrinsic cytotoxicity and the number of nuclei of aggregation per cell could be key factors in this transmission capacity of each amyloid.

Keywords: Alzheimer disease; Creutzfeldt–Jakob disease; amyloid; amyloid cytotoxicity; amyloid transmission; prion; transmissible spongiform encephalopathy.

MeSH terms

  • Alzheimer Disease / metabolism
  • Alzheimer Disease / physiopathology
  • Amyloid / metabolism*
  • Animals
  • Biomedical Research
  • Creutzfeldt-Jakob Syndrome / metabolism
  • Creutzfeldt-Jakob Syndrome / physiopathology
  • Humans
  • Mice
  • Prions / metabolism*
  • Protein Structure, Tertiary

Substances

  • Amyloid
  • Prions