Truncated PrPc in mammalian brain: interspecies variation and location in membrane rafts

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 trunc...

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Veröffentlicht in:Biological chemistry 2006-03, Vol.387 (3), p.297-300
Hauptverfasser: Laffont-Proust, Isabelle, Hässig, Raymonde, Haïk, Stéphane, Simon, Stéphanie, Grassi, Jacques, Fonta, Caroline, Faucheux, Baptiste A., Moya, Kenneth L.
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Sprache:eng
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Zusammenfassung: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.
ISSN:1431-6730
1437-4315
DOI:10.1515/BC.2006.039