Klingeborn, Mikael
- Institutionen för molekylär biovetenskap, Sveriges lantbruksuniversitet
Konferensabstrakt2008Vetenskapligt granskad
Linne Tommy, Wik Lotta, Klingeborn Mikael
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
Titel: Book of abstracts
Prion2008
Veterinärmedicin
Husdjursvetenskap
https://res.slu.se/id/publ/22691