Abstract

Proteolytic, phospholipase-mediated and exosome-mediated release of the prion protein has 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 proteolytically shed PrP cleaved at the extreme C-terminal end. The exosomal fraction contained the GPI-anchored PrP. A deletion mutant in the C1 cleavage site affected the C1 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

Published in

Title: Prion 2006, "Strategies, advances and trends towards protection of society",

Conference

"Strategies, advances and trends towards protection of society", Prion 2006,

SLU Authors

• Klingeborn, Mikael

  • Department of Molecular Biosciences, Swedish University of Agricultural Sciences
    

• Wik, Lotta

  • Department of Molecular Biosciences, Swedish University of Agricultural Sciences
    

• Willander, Hanna

  • Department of Animal Biosciences, Swedish University of Agricultural Sciences
    

• Linne, Tommy

  • Department of Molecular Biosciences, Swedish University of Agricultural Sciences
    

UKÄ Subject classification

Veterinary Science
Animal and Dairy Science


Permanent link to this page (URI)

https://res.slu.se/id/publ/22700