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P3‐327: Hsp90 inhibition rescues behavioral deficits and reduces tau phosphorylation in ps19 mice model for Alzheimer's disease (AD)
Author(s) -
Inda Carmen,
Koren John,
Boalander Alexander,
Panchal Palak,
Gandu Srinivasa,
Chiosis Gabriela
Publication year - 2015
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.2015.06.1701
Subject(s) - genetically modified mouse , pharmacology , toxicity , in vivo , immunostaining , drug , transgene , medicine , biology , immunohistochemistry , neuroscience , pathology , biochemistry , microbiology and biotechnology , gene
with neurotoxicity & ameliorates strain-specific tau-related phenotypes. Mice treated display no signs of toxicity; confirmed through pathology analysis following chronic administration. The inhibition of Hsp90 induced the expression of the pro-survival chaperone Hsp70, a chaperone also associated with tau degradation. Additionally, inhibiting the Hsp90-dependent protection of tau abrogated a terminal tau-driven phenotype thereby extending the lives of treated animals as compared to transgenic animals receiving vehicle or no treatment. Conclusions: Together, these findings demonstrate the potential for Hsp90 inhibition in the treatment of neurodegenerative diseases involving tau accumulation; namely, Alzheimer’s disease. Data accompanying this presentation which presents experimental behavioral changes and immunohistochemical analysis of neural tau burden can be seen on the poster presented by Inda, C. et al.