NR AWIR
AU Latawiec,D.; Nguyen,H.O.B.; Sussman,J.; Suzuki,E.; Prusiner,S.B.; Legname,G.
TI Antagonistic cellular functions for prion protein and its paralog doppel
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-22
PT Konferenz-Poster
AB
The physiological function of the cellular form of the prion protein (PrPc) has remained elusive. We recently described a function for PrP, by observing the effect of recombinant PrP to cultured primary neurons from the hippocampus of embryonic rats (E18/E19) (Kanaani, Prusiner et al. 2005). The assay showed that PrP plays a role in promoting both neuronal polarity and development. We have now established this assay in primary neurons cultured from the cerebellum of postnatal (P6) mice. In addition to confirming the findings of the rat model for PrP, we have elucidated a possible role for its paralog protein, doppel (Dpl). Our findings suggest that the two proteins may have an antagonistic relationship: PrP promotes cell survival and neuritogenesis, whereas Dpl induces apoptosis. Establishing the assay in postnatal mouse neurons has an important advantage over the rat model. Most importantly, the availability of a wide range of knockout and transgenic mouse models should provide a diverse source to dissect further the functions of PrP and its interaction with other cellular proteins and structures.
Reference Kanaani, J., S. B. Prusiner, et al. (2005). "Recombinant prion protein induces rapid polarization and development of synapses in embryonic rat hippocampal neurons in vitro." J. Neurochem. 95: 1373-1386.
AD D. Latwiec, H.-O. Nguyen, J. Sussman, E. Suzuki: Institute for Neurodegenerative Diseases, University of California, San Francisco, CA, USA; S.B. Prusiner: Institute for Neurogenerative Diseases, Departments of Neurology, Biochemistry and Biophysics, University of California, San Francisco, CA, USA; G. Legname: Institute for Neurodegenerative Diseases, Department of Neurology, University of California, San Francisco, CA, USA. E-mail: glegname@ind.ucsf.edu
SP englisch
PO Italien