The cellular prion protein: Biochemistry, topology, and physiologic functions

Cristiana Griffoni, Mattia Toni, Enzo Spisni, Maria Cristina Bianco, Spartaco Santi, Massimo Riccio, Vittorio Tomasi

Research output: Contribution to journalArticlepeer-review

Abstract

Studies on the transmission from man to animals of Creutzfeld-Jacob disease (CJD) led Prusiner to identify a proteinaceous infectious particle lacking nucleic acid, which was called priori. The identification of the infectious prion (PrPsc) then led to the discovery of the normal cellular counterpart (PrPc). One of the still enigmatic aspects regarding prion diseases is actually how, where, and when the transformation PrPc/PrPsc is occurring, this being due to the result of a large extent to the fact that so far most studies have been dedicated to the formation and transmission of PrPsc, whereas the understanding of physiologic roles of PrPc are in their infancy. In this review, we hope to identify the most reliable hypotheses for future experiments on PrPc. This is relevant not only for the understanding of PrPc functions but also to unravel the enigmatic nature of PrPc/PrPsc conversion.

Original languageEnglish
Pages (from-to)287-304
Number of pages18
JournalCell Biochemistry and Biophysics
Volume38
Issue number3
DOIs
Publication statusPublished - Jun 2003

Keywords

  • Caveolae
  • Copper binding
  • Prion protein
  • Rafts
  • Signal transduction

ASJC Scopus subject areas

  • Cell Biology
  • Clinical Biochemistry
  • Biophysics

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