NR AJRG
AU Prusiner,S.B.
TI Transgenetic investigations of prion diseases of humans and animals
QU Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences 1993 Feb 27; 339(1288): 239-54
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 the PrP gene are genetically linked to development of neurodegeneration. Transgenic mice expressing mutant PrP spontaneously develop neurological dysfunction and spongiform neuropathology. Investigations of prion diseases using transgenesis promise to yield much new information about these once enigmatic disorders.
ZR 136
MH Animal; Cattle; Cattle Diseases/genetics; Gene Expression; Human; Mice; Mice, Transgenic; Mutation; PrPsc Proteins; Prion Diseases/*genetics/metabolism/veterinary; Prions/*genetics/metabolism; Protein Processing, Post-Translational; Sheep; Sheep Diseases/genetics; Support, Non-U.S. Gov't; Support, U.S. Gov't, P.H.S.; Variation (Genetics)
AD Department of Neurology, University of California, San Francisco 94143.
SP englisch
PO England