NR AURV
AU Barenco,M.G.; Hammann,J.; Valori,C.; Crugnola,A.; Löwer,J.; Weissmann,C.; Montrasio,F.; Rossi,D.
TI The N-terminal domain of PrPc is not necessary for the induction of neuronal differentiation
QU TSE-Forum, 6. Kongress - Nationale TSE-Forschungsplattform, Greifswald 26.6.-28.6.2006, Poster: Struktur und zellbiologische Ansätze ZELL-01
PT Konferenz-Poster
AB The cellular prion protein is a glycosylphosphatidylinositol-anchored cell-surface protein whose biological function is largely unknown. In order to develop in vitro models for studying prion protein-dependent pathways, we have first generated a novel PrP knockout cell line called PrP0/0 ML, which does express neither the prion protein nor doppel. Here we show that the PrP0/0 ML cell line is a unipotent neuronal precursor line which can specifically differentiate into mature neurons when cultivated under specific culture conditions. The role of the prion protein in the process of neuronal differentiation was then analyzed in PrP0/0 ML cells reconstituted for the expression of either the full-length or a N-terminal deleted form of the prion protein. We show that prion protein expression induces neuronal differentiation and that the N-terminal domain containing the octapeptide repeat region of the prion protein is not necessary for the activation of the neuronal differentiation pathway.
AD M.G.Barenco, Joanna Hammann (hamjo@pei.de), J.Löwer, F.Montrasio*, Prion Research Group, Paul-Ehrlich-Institut, Langen, Germany; C.Valori, A.Crugnola, D.Rossi*, Center of Excellence on Neurodegenerative Diseases, Department of Pharmacological Sciences, University of Milan, Milan, Italy, C.Weissmann, Department of Infectology, Scripps Florida Research Institute, Schmidt Building, 777 Glades Road, Boca Raton FL 33431, USA; *These two authors contributed equally to this work. Correspondence to: daniela.rossi@unimi.it and monfa@pei.de
SP englisch
PO Deutschland
OR Tagungsband