%0 Journal Article
%T In vitro generation of tau aggregates conformationally distinct from parent tau seeds of Alzheimer¡¯s brain
%A Won-Hee Nam
%A Young Pyo Choi
%J Prion
%D 2019
%R https://doi.org/10.1080/19336896.2018.1545524
%X ABSTRACT Normal monomeric tau can be converted into pathogenic aggregates and acquire protease resistance in a prion-like manner. This acquisition of partial protease-resistance in tau aggregates has to date only been partially investigated in various studies exploring the prion-like properties of tau. In this study, we induced the aggregation of tau repeat domain (RD) in cultured cells using detergent insoluble fractions of Alzheimer¡¯s brain tissue as seeds. The seeded aggregation of tau RD in cultured cells formed a ~7 kDa protease-resistant fragment in contrast to the ~12 kDa tau fragment characteristic of the AD seeds, suggesting that the in vitro generated tau aggregates were conformationally distinct from parent seeds
%U https://www.tandfonline.com/doi/full/10.1080/19336896.2018.1545524