NR AWQK
AU Wik,L.; Klingeborn,M.; Johansson,H.; Linne,T.
TI Analysis of the distribution of cell-released bovine PrP in an exosomal and a soluble fraction
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-53
PT Konferenz-Poster
AB Proteolytic, phospholipase-mediated and exosome-mediated release of the prion protein have been reported. Recently, exosomes containing PrPsc released from prion-infected cells were shown infectious, suggesting exosome release as a means of spreading prions between cells (Fevrier et al, 2004). It is therefore of large interest to investigate the targeting of prion proteins to proteolytic, phospholipase-mediated or exosome-mediated release. We found the PrP released from transfected cells in a soluble fraction and an exosome bound fraction. The soluble fraction contained proteolytical shed PrP cleaved at the extreme C-terminal end. The exosomal fraction contained the GPI-anchored PrP. A deletion mutant in the C-1 cleavage site affected the C-1 cleavage and a full length PrP was found in the exosomal fraction. Further analysis of the distribution of the PrP in the exosomal fraction and the interaction of the released PrP with various cells are currently being studied.
AD Department of Molecular Biosciences, Section of Veterinary Immunology and Virology, Swedish University of Agricultural Sciences, Biomedical Centre, Box 588, SE-75 123 Uppsala, Sweden. E-mail: lotta.wik@mbv.slu.se
SP englisch
PO Italien