Normal prion protein trafficking in cultured human erythroblasts

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...

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...

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...

Cellular Trafficking of the Pathogenic Prion Protein PrPSc and Phenotypic Characterisation of Deletion Mutants in the Hydrophobic Domain of the Normal Prion Protein PrPC

LRP1 controls biosynthetic and endocytic trafficking of neuronal prion protein.

The trafficking of normal cellular prion protein (PrPC) is believed to control its conversion to the altered conformation (designated PrPSc) associated with prion disease. Although anchored to the membrane by means of glycosylphosphatidylinositol (GPI), PrPC on neurons is rapidly and constitutively endocytosed by means of coated pits, a property dependent upon basic amino acids at its N-terminu...