Abstract

Determining the intra- and intercellular trafficking and processing of PrPC, is important in discerning its normal physiological function and the mechanism of conversion to disease-associated isoforms. PrPC is bound to the cell membrane via a glycosylphosphatidylinositol (GPI) anchor but secreted forms of PrPC have been identified. In the cell medium two distinct PrP populations could be found. The major fraction was released by proteolytic cleavage near the GPI anchor. A minor fraction released in association with exosomes was characterized by western immunoblotting with exosome-specific markers, phospholipase assays, and electron microscopic analysis. Less than 1% of the released PrP was exosome-associated. The role of cell-to-cell transport of PrPC by exosomes is studied further

Published in

Title: Book of abstracts

Conference

Prion2008

SLU Authors

• Klingeborn, Mikael

  • Department of Molecular Biosciences, Swedish University of Agricultural Sciences
    

• Linne, Tommy

  • Department of Molecular Biosciences, Swedish University of Agricultural Sciences
    

• Wik, Lotta

  • 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/22691