Guo JL, Covell DJ, Daniels JP, Iba M, Stieber A, Zhang B, Riddle DM, Kwong LK, Xu Y, Trojanowski JQ, Lee VM.
Distinct α-synuclein strains differentially promote tau inclusions in neurons.
Cell. 2013 Jul 3;154(1):103-17.
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This work demonstrates the existence of assembled α-synuclein strains, based on the cross-seeding (or not) of tau aggregation. This is important for understanding some human neurodegenerative diseases, where α-synuclein inclusions are present in different cell types and different parts of the nervous system, sometimes in conjunction with tau inclusions. Aggregates of tau give rise to distinct human tauopathies and recent experiments have shown that strains of assembled four-repeat tau appear to exist (Clavaguera et al., 2013). Strains of assembled α-synuclein and tau provide a further link with prion diseases, where different aggregate conformations of the prion protein give rise to distinct disease phenotypes and neuropathologies.
Clavaguera F, Akatsu H, Fraser G, Crowther RA, Frank S, Hench J, Probst A, Winkler DT, Reichwald J, Staufenbiel M, Ghetti B, Goedert M, Tolnay M.
Brain homogenates from human tauopathies induce tau inclusions in mouse brain.
Proc Natl Acad Sci U S A. 2013 Jun 4;110(23):9535-40.