The cellular prion protein: biochemistry, topology, and physiologic functions.
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 prion. 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.
Griffoni
Cristiana
C
Department of Experimental Biology, University of Bologna, Bologna, Italy.
Toni
Mattia
M
Spisni
Enzo
E
Bianco
Maria
M
Santi
Spartaco
S
Riccio
Massimo
M
Tomasi
Vittorio
V
D000818:Animals; D017209:Apoptosis / Q000502:physiology; D003300:Copper / Q000737:chemistry; D007562:Creutzfeldt-Jakob Syndrome / Q000378:metabolism; D006801:Humans; D051379:Mice; D008954:Models, Biological; D018621:PrPC Proteins / Q000737:chemistry / Q000378:metabolism* / Q000502:physiology; D018620:PrPSc Proteins / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D011487:Protein Conformation; D011956:Receptors, Cell Surface / Q000378:metabolism
D018621:PrPC Proteins; D018620:PrPSc Proteins; D011956:Receptors, Cell Surface; D003300:Copper