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O5‐06‐06: TAU Tubulin Kinase Activation Coincides with Neuropathology in Dementia
Author(s) -
Taylor Laura,
McMillan Pamela,
Liachko Nicole,
Strovas Timothy C.,
Kraemer Brian C.
Publication year - 2016
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.2016.06.740
Subject(s) - neurodegeneration , tauopathy , kinase , neuropathology , frontotemporal dementia , hyperphosphorylation , biology , microbiology and biotechnology , neuroscience , neurotoxicity , frontotemporal lobar degeneration , phosphorylation , gsk 3 , amyotrophic lateral sclerosis , dementia , medicine , pathology , disease , toxicity
synaptic proteins were measured by ELISA, Western blot, and immunohistochemistry. Results: We found that TOMA-treated A53T mice performed at the same level as wildtype mice on cognitive and motor tasks, when compared to control IgGtreated mice that were impaired in all tasks. Treating with an antibody for all forms of tau, Tau-13, was not similarly protective and actually appeared to exacerbate the phenotype on certain tasks. We found A53T mice treated with TOMA had lower levels of tau oligomers, while levels of dopamine and synaptic proteins were elevated in TOMA-treated mice. The alphasynuclein aggregation pathway also appeared to be altered by TOMA treatment. Conclusions:An antibody specific to tau oligomers, as opposed to non-selective targeting of tau protein, effectively protects against toxicity in a synucleinopathy mouse model. This strategy represents a new route for the treatment of diseases with a synergistic relationship between tau and alphasynuclein.