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Prion-Like Activity of Pathological Tau Species Derived from Alzheimer's Brain

神经药理学报 2019年第Z1期 34-35页

作者： LIU Fei LI Long-fei ZHOU Yan GU Jian-lan MIAO Jin SHI Rui-rui JIN Na-na CHU Dan-dan tung yunn chyn HU Wen GONG Cheng-Xin Khalid Iqbal Department of Neurochemistry Inge Grundke-Iqbal Research FloorNew York State Institute for Basic Research in Developmental Disabilities Key Laboratory of Neuroregeneration of Jiangsu and Ministry of Education of China Co-innovation Center of Neuroregeneration

Background:Neurofibrillary tangles(NFTs),the insoluble and fibrillar intraneuronal accumulations of hyperphosphorylated tau protein,are a defining histopathological hallmark of the Alzheimer’s disease(AD) brain. NFTs initiate in subcortical regions,transentorhinal area,and entorhinal cortex,then appear in the hippocampal formation and some parts of the neocortex,followed by most of the neocortex. The distribution of tau pathology correlates with the progression of AD. Injection of misfolded tau aggregates derived from AD and transgenic mouse brains or generated in vitro induces tau pathology not only at the injection sites,but also in the anatomically connected brain regions in a time-dependent manner,introducing the concept of "prion-like propagation of tau pathology". The prion-like activity of the pathological tau species and the role of tau hyperphosphorylation in seeding and propagation of tau pathology are currently under debate. Methods:To determine the prion-like activity of pathological tau species in AD brain,we isolated different pathological tau species,soluble tau(S-tau),heat-stable soluble tau(HS-tau),oligomeric tau(O-tau),sarkosyl insoluble tau 1(SI1-tau),and sarkosyl insoluble tau 2(SI2-tau),from AD brains,analyzed their truncation and phosphorylation by Western blots and determined their prion-like activity by capturing normal tau in vitro and seeding tau aggregation in cultured cells,and inducing tau pathology in vivo. Results:We found that these tau species isolated from AD brain showed differences in truncation,site-specific phosphorylation,and SDSand reducing agent-resistant high molecular weight aggregation. S-tau,AD O-tau and SI1-tau,but not HS-tau and SI2-tau,captured tau151-391 from cell lysates and induced tau aggregation in cultured cells. AD O-tau showed the highest prion-like activity. Dephosphorylation of AD O-tau ameliorated its prion-like activity to capture tau in vitro,to seed tau aggregation in cultured cells and to induce tau path

关键词： tau Alzheimer Prion-Like Activity of Pathological Tau Species Derived from Alzheimer’s Brain Tau Activity

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