NR AWBN
AU Barenco,M.G.; Valori,C.; Hammann,J.; Crugnola,A.; Loewer,J.; Weissmann,C.; Montrasio,F.; Rossi,D.
TI The N-terminal domain of the cellular prion protein is not necessary to induce neuronal differentiation and neurite outgrowth
QU International Conference - Prion 2006: Strategies, advances and trends towards protection of society - 3.10.-6.10.2006, Torino, Italy, Lingotto Conference Centre - Poster sessions CE-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 with either the full-length or an Nterminal deleted form of the prion protein. We show that prion protein expression induces neuronal differentiation and neurite outgrowth and that the N-terminal domain containing the octapeptide repeat region of the prion protein is not necessary for the activation of the signalling pathway underlying such events.
AD M.G. Barenco, J. Hammann, J. Loewer, F. Montrasio: Prion Research Group, Paul-Ehrlich-Institute, 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 Infectiology, The Scripps Research Institute, West Palm Beach, USA. E-mail: daniela.rossi@unimi.it and monfa@pei.de
SP englisch
PO Italien