Neuropathology of animal Prion diseases: relationships with strain, morphological change and clinical disease.

摘要

Summary: When light microscopic patterns of PrPd accumulations are correlated with sub-cellular structure, intracellular PrPd co-localises with lysosomes while other PrPd types co-localise with cell membranes and the extracellular space. Different ly-sosomal PrPd cleavage sites are found for different cells infected with the same agent indicating that not all PrPd conformers code for different prion strains. Membrane PrPd is poorly excised and recycled, probably due to increased stabilization on the membrane of PrPd complexed with other membrane ligands. PrPd on plasma-lemmas may also be transferred to other cells or released to the extracellular space. When different animal prion diseases are considered, neurological deficits do not correlate well with any morphological type of PrPd. An extended version of this review is at [1].