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P1‐240: TEMPLATION AND PROPAGATION OF TAU PATHOLOGY BY ALZHEIMER TAU IN C57BL/6 MICE
Author(s) -
Zhou Yan,
Hu Wen,
Tung Yunn Chyn,
Gong Cheng-Xin,
Iqbal Khalid,
Liu Fei
Publication year - 2018
Publication title -
alzheimer's and dementia
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 6.713
H-Index - 118
eISSN - 1552-5279
pISSN - 1552-5260
DOI - 10.1016/j.jalz.2018.06.245
Subject(s) - tau pathology , tau protein , genetically modified mouse , tauopathy , entorhinal cortex , immunostaining , pathology , hippocampus , chemistry , alzheimer's disease , transgene , in vivo , microbiology and biotechnology , neurodegeneration , biology , neuroscience , immunohistochemistry , medicine , biochemistry , disease , gene
than the number of p-Tau+ neurons does (Table 1). The frequencies of PTMs, the percent overlap between PTMs, and significance of difference between early and late Braak stages are depicted in Table 2. Conclusions:Caspase-6 cleavage at Asp401 facilitates the formation of paired helical filaments (PHF). The PTMs that trigger this caspase activity are unclear. These data suggest that acetylation of tau at Lys274 correlates better with cleavage by caspase-6 than phosphorylation of tau at Ser202/Thr205 does. While there is colocalization between p-Tau and c-Tau, the majority of neurons positive for both p-Tau and c-Tau are also positive for a-Tau, suggesting that caspase-mediated cleavage of tau in these neuronsmay be primarily induced by acetylation, rather than phosphorylation. These preliminary data highlight that the acetylation of tau represents a key step in AD pathobiology and warrants further study.