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- W2016110327 abstract "Understanding the formation and propagation of aggregates of the Alzheimer disease-associated Tau protein in vivo is vital for the development of therapeutics for this devastating disorder. The progression of tau pathology throughout the brain has long been observed in patients and resulted in the definition of Braak stages with respect to the location of neurofibrillary tangles. Recent evidence from cellular, biochemical and biophysical experiments now supports the idea that extracellular tau aggregates may transmit their misfolded state to the inside of a neighbouring cell. Our group specialises in the development and application of advanced microscopy techniques for the functional study of protein self-assembly reactions in neurodegenerative disease. We have used a large set of techniques to support our research: Fluorescence lifetime imaging (FLIM), direct stochastic optical reconstruction microscopy (d STORM), AFM, western blotting and confocal imaging. Using our recently developed live-cell aggregation sensor in neuron-like cells, we demonstrate that different variants of exogenous monomeric Tau, namely full-length Tau (hTau40) and the Tau-derived construct K18 comprising the repeat domain, initially accumulate in endosomal compartments, where they form fibrillar seeds which subsequently induce the aggregation of endogenous Tau. Using super-resolution imaging, we confirm that fibrils consisting of endogenous and exogenous Tau are released from cells and demonstrate their potential to spread Tau pathology. We show here, in a live cell culture model, that advanced optical techniques give new insight on the kinetics of aggregation and propagation of tauopathies. Our data importantly indicate a greater pathological risk and potential toxicity than hitherto suspected for extracellular soluble Tau." @default.
- W2016110327 created "2016-06-24" @default.
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- W2016110327 date "2014-07-01" @default.
- W2016110327 modified "2023-10-14" @default.
- W2016110327 title "P3-050: EXTRACELLULAR MONOMERIC TAU IS SUFFICIENT TO INITIATE THE SPREAD OF TAU PATHOLOGY" @default.
- W2016110327 doi "https://doi.org/10.1016/j.jalz.2014.05.1137" @default.
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