NR AUNW
AU Laffont-Proust,I.; Hässig,R.; Haik,S.; Simon,S.; Grassi,J.; Fonta,C.; Faucheux,B.A.; Moya,K.L.
TI Truncated PrPc in mammalian brain: interspecies variation and location in membrane rafts.
QU Biological Chemistry 2006 Mar; 387(3): 297-300
PT journal article
AB A key molecular event in prion diseases is the conversion of cellular prion protein (PrPc) into an abnormal misfolded conformer (PrPsc). The PrPc N-terminal domain plays a central role in PrPc functions and in prion propagation. Because mammalian PrPc is found as a full-length and N-terminally truncated form, we examined the presence and amount of PrPc C-terminal fragment in the brain of different species. We found important variations between primates and rodents. In addition, our data show that the PrPc fragment is present in detergent-resistant raft domains, a membrane domain of critical importance for PrPc functions and its conversion into PrPsc.
MH Animals; Brain/*metabolism; Cell Membrane/*metabolism; Cricetinae; Detergents/pharmacology; Electrophoresis, Polyacrylamide Gel; Membrane Microdomains/*metabolism; Papio; PrPc Proteins/chemistry/genetics/*metabolism; PrPsc Proteins/chemistry/genetics/*metabolism; Primates; Prion Diseases/etiology/*metabolism; Rodentia; Species Specificity
AD INSERM Avenir Team-Human prion diseases, IFR70, Neuropathology, Salpetriere Hospital, F-75013 Paris, France.
SP englisch
PO Deutschland