The physiological functions of prion protein

Christian Wechselberger, Susanne Wurm, Werner Pfarr, Otmar Höglinger

Research output: Contribution to journalArticlepeer-review

25 Citations (Scopus)


Prion proteins are mentioned predominantly as unprecedented infectious pathogens in the context of transmissible spongiform encephalopathies. Since prions are devoid of nucleic acids, disease transmission must be mediated by an entirely novel mechanism. The general accepted theory proposes the conversion of cellular prion protein (PrPC) into the pathological isoform solely through conformational changes. This process favors the development of insoluble protein aggregates in the central nervous system typical for prion diseases. However, progress to elucidate the physiological functions of PrPC is still slow besides recent indications of a multifaceted network, in which PrPC seems to play a fundamental role. Possible contributions of interrupted or disturbed physiological signaling events due to the pathological prion protein isoform are presented in terms of recent findings.

Original languageEnglish
Pages (from-to)1-8
Number of pages8
JournalExperimental Cell Research
Issue number1
Publication statusPublished - 2002
Externally publishedYes


  • Cellular prion protein
  • Interacting proteins
  • Pathological isoform
  • Physiological functions
  • Signal transduction cascades
  • Prions/physiology
  • Humans
  • Mice, Knockout
  • Signal Transduction/physiology
  • Animals
  • Protein Isoforms
  • Mice
  • Prion Diseases/metabolism


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