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 |
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Hauptverfasser: | , , , , , , , |
Format: | Artikel |
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. |
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ISSN: | 1431-6730 1437-4315 |
DOI: | 10.1515/BC.2006.039 |