Cellular prion protein neuroprotective function: implications in prion diseases

J Mol Med (Berl). 2005 Jan;83(1):3-11. doi: 10.1007/s00109-004-0605-5. Epub 2004 Nov 10.


Prion protein can display two conformations: a normal cellular conformation (PrP) and a pathological conformation associated with prion diseases (PrP(Sc)). Three complementary strategies are used by researchers investigating how PrP is involved in the pathogenesis of prion diseases: elucidation of the normal function of PrP, determination of how PrP(Sc) is toxic to neurons, and unraveling the mechanism for the conversion of PrP to PrP(Sc). We review the normal function of PrP as an antioxidant and an antiapoptotic protein in vivo and in vitro. This review also addresses contrasting evidence that PrP is cytotoxic. Finally, we discuss the implication of the neuroprotective role of PrP in prion diseases.

Publication types

  • Review

MeSH terms

  • Animals
  • Apoptosis / genetics
  • Apoptosis / physiology
  • Brain / metabolism
  • Breast Neoplasms / metabolism
  • Cell Survival / physiology
  • GPI-Linked Proteins
  • Humans
  • Mice
  • Neurons / metabolism*
  • Oxidative Stress / physiology
  • Prion Diseases / metabolism*
  • Prions / metabolism*
  • Proto-Oncogene Proteins c-bcl-2 / physiology
  • Tumor Necrosis Factor-alpha / metabolism
  • bcl-2-Associated X Protein


  • GPI-Linked Proteins
  • PRND protein, human
  • Prions
  • Prnd protein, mouse
  • Proto-Oncogene Proteins c-bcl-2
  • Tumor Necrosis Factor-alpha
  • bcl-2-Associated X Protein