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Experimental Genetics Group
J Neurosci. 2002 Sep 1;22(17):7471-7. Künzi V1,4, Glatzel M1,4, Nakano MY2, Greber UF2, Van Leuven F3, Aguzzi A1. 1Institute of Neuropathology, University Hospital Zürich, Zürich, Switzerland. 2Institute of Zoology, University of Zürich, Zürich, Switzerland. 3Experimental Genetics Gorup, Department of Human Genetics, Catholic University of Leuven, Leuven, Belgium. 4Contributed equally to this work. Transmissible spongiform encephalopathies often are caused by peripheral uptake of infectious prions, and the peripheral nervous system is involved in prion spread to the brain. Although the cellular prion protein is subjected to fast axonal transport, the mechanism of intranerval transport of infectious prions is unclear. Here we administered prions intranervally to transgenic mice overexpressing the four-repeat human tau protein, which exhibit defective fast axonal transport. These mice showed unaltered neuroinvasion, suggesting that transport mechanisms distinct from fast axonal transport effect prion neuroinvasion along peripheral nerves. Surprisingly, scrapie-sick tau transgenic mice accumulated intraneuronal deposits of hyperphosphorylated tau protein. The coincidence of tau and prion pathology resembled Gerstmann-Sträussler-Scheinker syndrome. These findings identify tau pathology as a possible end stretch of prion-induced neurodegeneration.  FULL TEXT |
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