Prion protein lacks robust cytoprotective activity in cultured cells

Evaluation of Infective Property of Recombinant Prion Protein Amyloids in Cultured Cells Overexpressing Cellular Prion Protein

Misfolded isoform of prion protein (PrP), termed scrapie PrP (PrP(Sc)), tends to aggregate into various fibril forms. Previously, we reported various conditions that affect aggregation of recombinant PrP into amyloids. Because amyloidogenesis of PrP is closely associated with transmissible spongiform encephalopathies such as Creutzfeldt-Jakob disease in humans, we investigated infectivity of re...

RED CELLS Normal prion protein trafficking in cultured human erythroblasts

Normal prion protein (PrPc), an essential substrate for development of prion disease, is widely distributed in hematopoietic cells. Recent evidence that variant Creutzfeldt-Jakob disease can be transmitted by transfusion of red cell preparations has highlighted the need for a greater understanding of the biology of PrPc in blood and blood-forming tissues. Here, we show that in contrast to anoth...

GPI-anchorless human prion protein is secreted and glycosylated but lacks superoxide dismutase activity.

Prion protein (PrP) is a glycosylphosphatidylinositol (GPI)-anchored membrane protein that is thought to play a role in anti-oxidative stress. It remains controversial whether PrP elicits superoxide dismutase (SOD) activity itself or indirectly by activating cellular SOD. Our previous studies showed that soluble PrP produced by a baculovirus expression system did not exhibit any SOD activity in...

Cytoprotective and toxic functions of the prion protein family

Normal prion protein trafficking in cultured human erythroblasts.

Normal prion protein (PrP(c)), an essential substrate for development of prion disease, is widely distributed in hematopoietic cells. Recent evidence that variant Creutzfeldt-Jakob disease can be transmitted by transfusion of red cell preparations has highlighted the need for a greater understanding of the biology of PrP(c) in blood and blood-forming tissues. Here, we show that in contrast to a...