Quantitative propagation of assembled human Tau from Alzheimer's disease brain in microfluidic neuronal cultures

• Published in: The Journal of biological chemistry Vol. 295; no. 37; pp. 13079 - 13093
• Main Authors: Katsikoudi, Antigoni, Ficulle, Elena, Cavallini, Annalisa, Sharman, Gary, Guyot, Amelie, Zagnoni, Michele, Eastwood, Brian J., Hutton, Michael, Bose, Suchira
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 11.09.2020; American Society for Biochemistry and Molecular Biology
• Subjects: Alzheimer disease; Alzheimer Disease - metabolism; Alzheimer Disease - pathology; Amyloid beta-Peptides - metabolism; Animals; drug screening; Entorhinal Cortex - metabolism; Entorhinal Cortex - pathology; human; Humans; Locus Coeruleus - metabolism; Locus Coeruleus - pathology; Microfluidic Analytical Techniques; microfluidics; microtubule; Models, Neurological; Neurobiology; neurodegeneration; neurodegenerative disease; neuron; Neurons - metabolism; Neurons - pathology; propagation; protein aggregation; Rats; Rats, Sprague-Dawley; Tau protein (Tau); tau Proteins - metabolism; tauopathy; Tissue Culture Techniques; microtubule; tauopathy; neurodegenerative disease; propagation; Tau protein (Tau); drug screening; Alzheimer disease; protein aggregation; neurodegeneration; neuron; human; microfluidics

Tau aggregation and hyperphosphorylation is a key neuropathological hallmark of Alzheimer's disease (AD), and the temporospatial spread of Tau observed during clinical manifestation suggests that Tau pathology may spread along the axonal network and propagate between synaptically connected neur...