NR AWER
AU Farinazzo,A.; Zanusso,G.; Piccardo,P.; Ferrari,S.; Fasoli,E.; Gelati,M.; Fiorini,M.; Rizzuto,N.; Monaco,S.; Ghetti,B.
TI Two-dimensional analysis of proteinase K-resistant prion protein in GSS P102L mutation
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 PR-12
PT Konferenz-Poster
AB The most common Gerstmann-Sträussler-Scheinker (GSS) disease phenotype is associated with a point mutation at codon 102, which results in the proline-to-leucine substitution. In P102L mutation, immunoblot analysis of protease-resistant PrP, or PrPres, shows the presence of a C-terminal 21kDa fragment, in addition to an internal 8kDa peptide, spanning positions 80-150. Protease-resistant PrP species encountered in P102L mutation are not limited to the above molecules but also include truncated fragments migrating at 17 and 14 kDa. With the exception of the internal 8 kDa fragment, the migration of the 21kDa core fragment and of truncated PrP species is indistinguishable from that observed in sCJD cases with type 1 PrPPres. However, when PrPres species of GSS associated with P102L mutation were analyzed by 2D analysis novel C-terminal PrPres variants were found. The present findings suggest that the composition of C-terminal variants observed in GSS is different from those found in sCJD, and this may accounts for differences in disease phenotypes. This work was supported by Neuroprion (FOOD-CT-2004-506579)
AD A. Farinazzo, G. Zanusso, S. Ferrari, E. Fasoli, M. Gelati, M. Fiorini, N. Rizzuto, S. Monaco: Department of Neurological and Visual Sciences, University of Verona, Verona, Italy; P. Piccardo, B. Ghetti: Department of Pathology and Laboratory Medicine, Indiana University, Indianapolis, IN, USA. E-mail: gianluigi.zanusso@univr.it
SP englisch
PO Italien