Truncated PrP(c) in mammalian brain: interspecies variation and location in membrane rafts.

Isabelle Laffont-Proust (1) , Raymonde Hässig , Stéphane Haïk , Stéphanie Simon , Jacques Grassi , Caroline Fonta (2) , Baptiste A Faucheux , Kenneth L Moya

1 IFR des Neurosciences
2 CERCO - Centre de recherche cerveau et cognition

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).

Domaines: Neurosciences [q-bio.NC]

Isabelle Laffont-Proust, Raymonde Hässig, Stéphane Haïk, Stéphanie Simon, Jacques Grassi, et al.. Truncated PrP(c) in mammalian brain: interspecies variation and location in membrane rafts.. Biol Chem, 2006, 387 (3), pp.297-300. ⟨10.1515/BC.2006.039⟩. ⟨hal-00111080⟩