Truncated PrP(c) in mammalian brain: interspecies variation and location in membrane rafts |
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Authors: | Laffont-Proust Isabelle Hässig Raymonde Haïk Stéphane Simon Stéphanie Grassi Jacques Fonta Caroline Faucheux Baptiste A Moya Kenneth L |
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Affiliation: | INSERM Avenir Team-Human prion diseases, IFR70, Neuropathology, Salpêtrière Hospital, F-75013 Paris, France. |
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Abstract: | A key molecular event in prion diseases is the conversion of cellular prion protein (PrP(c)) into an abnormal misfolded conformer (PrP(sc)). The PrP(c) N-terminal domain plays a central role in PrP(c) functions and in prion propagation. Because mammalian PrP(c) is found as a full-length and N-terminally truncated form, we examined the presence and amount of PrP(c) C-terminal fragment in the brain of different species. We found important variations between primates and rodents. In addition, our data show that the PrP(c) fragment is present in detergent-resistant raft domains, a membrane domain of critical importance for PrP(c) functions and its conversion into PrP(sc). |
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