Prion proteins: Physiological functions and role in neurological disorders Review uri icon


MeSH Major

  • Central Nervous System
  • Neurodegenerative Diseases
  • Prion Diseases
  • Prions


  • Stanley Prusiner was the first to promote the concept of misfolded proteins as a cause for neurological disease. It has since been shown by him and other investigators that the scrapie isoform of prion protein (PrP(Sc)) functions as an infectious agent in numerous human and non-human disorders of the central nervous system (CNS). Interestingly, other organ systems appear to be less affected, and do not appear to lead to major co-morbidities. The physiological function of the endogenous cellular form of the prion protein (PrP(C)) is much less clear. It is intriguing that PrP(c) is expressed on most tissues in mammals, suggesting not only biological functions outside the CNS, but also a role other than the propagation of its misfolded isotype. In this review, we summarize accumulating in vitro and in vivo evidence regarding the physiological functions of PrP(C) in the nervous system, as well as in lymphoid organs.

publication date

  • January 15, 2008



  • Review



  • eng

Digital Object Identifier (DOI)

  • 10.1016/j.jns.2007.06.019

PubMed ID

  • 17707411

Additional Document Info

start page

  • 1

end page

  • 8


  • 264


  • 1-2