Journal article

Gene Knockout of tau Expression Does Not Contribute to the Pathogenesis of Prion Disease

Victoria A Lawson, Helen M Klemm, Jeremy M Welton, Colin L Masters, Peter Crouch, Roberto Cappai, Giuseppe D Ciccotosto

JOURNAL OF NEUROPATHOLOGY AND EXPERIMENTAL NEUROLOGY | OXFORD UNIV PRESS INC | Published : 2011

Abstract

Prion diseases or transmissible spongiform encephalopathies are a group of fatal and transmissible disorders affecting the central nervous system of humans and animals. The principal agent of prion disease transmission and pathogenesis is proposed to be an abnormal protease-resistant isoform of the normal cellular prion protein. The microtubule-associated protein tau is elevated in patients with Creutzfeldt-Jakob disease. To determine whether tau expression contributes to prion disease pathogenesis, tau knockout and control wild-type mice were infected with the M1000 strain of mouse-adapted human prions. Immunohistochemical analysis for total tau expression in prion-infected wild-type mice i..

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