NR ATID
AU Laffont-Proust,I.; Hässig,R.; Haik,S.; Sazdovitch,V.; Simon,S.; Grassi,J.; Hauw,J.J.; Fonta,C.; Faucheux,B.A.; Moya,K.L.
TI The C-terminal fragment of cellular prion protein: interspecies variation and localization within raft domains
QU International Conference - Prion 2005: Between fundamentals and society's needs - 19.10.-21.10.2005, Congress Center Düsseldorf - Poster Session: Cell Biology of PrPc and PrPsc CELL-35
PT Konferenz-Poster
AB In mammals, cellular prion protein is found in both full-length and N-terminally truncated forms. It is known that PrPc amino acid sequence differences contribute to the species barrier. However, amino-terminal cleavage of PrPc could also be involved in species barrier phenomenon by modifying the recognition of the host cleaved PrPc by the exogeneous PrPres leading to changes in the rate of transconformation. Comparison of PrPc truncation in mammals is not fully documentated. Because of a well known species-barrier, we examined, by Western blotting, the PrPc pattern and distribution at the membrane surface in primates and rodents. We used several antibodies directed against the C-terminal region of PrPc to detect full-length and truncated forms of PrPc in isocortex homogenates of rodents (rat, mouse, hamster), prosimians (microcebus), New World monkeys (marmoset) and Old World monkeys (macaque, baboon). Our results show that PrPc was not artifactually truncated in vitro. We found that there are important variations in the proportion of the C-terminal fragment between rodents and non-human primates. Because cell surface PrPc is found in detergent-resistant membrane domains called "raft" domains, we examined whether the C-terminal fragment of PrPc was present in such domains in hamster and baboon. We observed the C-terminal fragment, as well as the full-length form, in raft domains. Its presence in raft domains could subject the C-terminal fragment to the conversion process that requires cell membrane exposition. Support: GIS Prion.
IN Zwischen Nagern und Nichtmenschenaffen fanden die Autoren große Unterschiede hinsichtlich des Anteils der Prionproteine, bei denen schon in vivo der Aminoterminus abgespalten wurde.
AD Isabelle Laffont-Proust, Raymonde Hässig, Kenneth L. Moya, CEA-CNRS URA2210, F. Joliot Hospital, 4, place du Général Leclerc, F-91406 Orsay, France; Stéphane Haïk, Véronique Sazdovitch, Jean-Jacques Hauw, Baptiste A. Faucheux, INSERM Avenir team "Human prion diseases", IFR70, Neuropathology, Salpêtrière Hospital, F-75013 Paris, France; Stéphanie Simon, Jacques Grassi, Pharmacology and Immunology department, CEA/Saclay, F-91191 Gif-sur-Yvette, France; Caroline Fonta, CERCO, UMR5549 CNRS-UPS, Rangueil University Medical School, 133, route de Narbonne, F-31062, Toulouse, France
SP englisch
PO Deutschland