Prion proteins: Physiological functions and role in neurological disorders

Wei Hu, Bernd Kieseier, Elliot Frohman, Todd N. Eagar, Roger N. Rosenberg, Hans Peter Hartung, Olaf Stüve

Research output: Contribution to journalReview articlepeer-review

30 Scopus citations


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 (PrPSc) 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 (PrPC) is much less clear. It is intriguing that PrPc 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 PrPC in the nervous system, as well as in lymphoid organs.

Original languageEnglish (US)
Pages (from-to)1-8
Number of pages8
JournalJournal of the Neurological Sciences
Issue number1-2
StatePublished - Jan 15 2008


  • Adaptive immunity
  • Aging
  • Alzheimer disease
  • Cognition
  • Down syndrome
  • Innate immunity
  • Lymphocytes
  • Neuroprotection
  • PrP
  • Primary progressive aphasia
  • Prion protein
  • Prnp
  • Wilson disease

ASJC Scopus subject areas

  • Neurology
  • Clinical Neurology


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