Abstract
Epigenetic remodeling via histone acetylation has become a popular therapeutic strategy to treat Alzheimer’s disease (AD). In particular, histone deacetylase (HDAC) inhibitors including M344 and SAHA have been elucidated to be new drug candidates for AD, improving cognitive abilities impaired in AD mouse models. Although emerged as a promising target for AD, most of the HDAC inhibitors are poorly selective and could cause unwanted side effects. Here we show that tau is one of the cytosolic substrates of HDAC and the treatment of HDAC inhibitors such as Scriptaid, M344, BML281, and SAHA could increase the level of acetylated tau, resulting in the activation of tau pathology.
Original language | English |
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Article number | 4283 |
Journal | International journal of molecular sciences |
Volume | 20 |
Issue number | 17 |
DOIs | |
Publication status | Published - 2019 Sept 1 |
Bibliographical note
Publisher Copyright:© 2019 by the authors. Licensee MDPI, Basel, Switzerland.
Keywords
- Alzheimer’s disease
- Histone deacetylase inhibitor
- Tau acetylation
- Tau aggregation
ASJC Scopus subject areas
- Catalysis
- Molecular Biology
- Spectroscopy
- Computer Science Applications
- Physical and Theoretical Chemistry
- Organic Chemistry
- Inorganic Chemistry