The transcellular spread of cytosolic amyloids, prions, and prionoids

Neuron. 2009 Dec 24;64(6):783-90. doi: 10.1016/j.neuron.2009.12.016.

Abstract

Recent reports indicate that a growing number of intracellular proteins are not only prone to pathological aggregation but can also be released and "infect" neighboring cells. Therefore, many complex diseases may obey a simple model of propagation where the penetration of seeds into hosts determines spatial spread and disease progression. We term these proteins prionoids, as they appear to infect their neighbors just like prions--but how can bulky protein aggregates be released from cells and how do they access other cells? The widespread existence of such prionoids raises unexpected issues that question our understanding of basic cell biology.

Publication types

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

MeSH terms

  • Amyloid / chemistry
  • Amyloid / genetics
  • Amyloid / metabolism*
  • Animals
  • Cell Communication / physiology
  • Cell Membrane / chemistry
  • Cell Membrane / metabolism
  • Cytosol / chemistry
  • Cytosol / metabolism
  • Disease Transmission, Infectious*
  • Endocytosis / physiology
  • Exocytosis / physiology
  • Humans
  • Prion Diseases / genetics
  • Prion Diseases / metabolism*
  • Prion Diseases / physiopathology
  • Prions / chemistry
  • Prions / genetics
  • Prions / metabolism*
  • Protein Transport / physiology

Substances

  • Amyloid
  • Prions