NR AJRJ
AU Prusiner,S.B.
TI Natural and experimental prion diseases of humans and animals
QU Current Opinion in Neurobiology 1992 Oct; 2(5): 638-47
PT journal article; review; review, academic
AB Prions cause transmissible and genetic neurodegenerative diseases. Infectious prion particles are composed largely, if not entirely, of an abnormal isoform of the prion protein (PrPsc), which is encoded by a chromosomal gene. Although the PrP gene is single copy, transgenic mice with both alleles of the PrP gene ablated develop normally. A post-translational process, as yet unidentified, converts the cellular prion protein (PrPc) into PrPsc. Scrapie incubation times, neuropathology and prion synthesis in transgenic mice are controlled by the PrP gene. Mutations in this gene are genetically linked to the development of neurodegeneration. Transgenic mice expressing mutant PrP spontaneously develop neurological dysfunction and spongiform neuropathology. Future investigations of prion diseases using molecular biological and genetic approaches promise to yield much new information about these once enigmatic disorders.
ZR 115
MH Animal; Creutzfeldt-Jakob Syndrome/genetics/*physiopathology; Human; Prions/*pathogenicity; Scrapie/genetics/*physiopathology; Support, Non-U.S. Gov't; Support, U.S. Gov't, P.H.S.; Virus Replication
AD Department of Neurology, University of California, San Francisco 94143.
SP englisch
PO England