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The cellular prion protein (PrP C ) is a glycosylphosphatidylinositol (GPI)-anchored protein. We investigated whether PrP C can move from one cell to another cell in a cell model. Little PrP C transfer was detected when a PrP C expressing human neuroblastoma cell line was cultured with the human erythroleukemia cells IA lacking PrP C . Efficient transfer of PrP C was detected with the presence of phorbol 12-myristate 13-acetate, an activator of protein kinase C. Maximum PrP C transfer was observed when both donor and recipient cells were activated. Furthermore, PrP C transfer required the GPI anchor and direct cell to cell contact. However, intercellular protein transfer is not limited
to PrP C , another GPI-anchored protein, CD90, also transfers from the donor cells to acceptor cells after cellular activation. Therefore,
this transfer process is GPI-anchor and cellular activation dependent. These findings suggest that the intercellular transfer
of GPI-anchored proteins is a regulated process, and may have implications for the pathogenesis of prion disease.