Journal
MOLECULAR NEUROBIOLOGY
Volume 57, Issue 12, Pages 5011-5025Publisher
SPRINGER
DOI: 10.1007/s12035-020-02079-x
Keywords
Alzheimer's disease; AMPK; Tau acetylation; Sirt1
Categories
Funding
- National Nature Scientific Foundation of China [81671262, 81901105]
- Natural Science Foundation of Anhui province [1908085QH357]
Ask authors/readers for more resources
Alzheimer's disease (AD) is the most common neurodegenerative disease, but its underlying mechanism is still unclear and the identities of drugs for AD also lack. Tau acetylation has become potentially important post-translational modification of tau. Levels of tau acetylation are significantly enhanced in AD patients and transgenic mouse models of AD, but the underlying mechanism and roles of tau hyperacetylation in AD onset maintain elusive. In the current study, we found that tau acetylation is obviously enhanced and the activities of AMP-activated protein kinase (AMPK) and sirtuin1 (Sirt1) are significantly decreased in APP/PS1 and streptozotocin (STZ) mice and high glucose (HG)-treated cells. Moreover, we demonstrated that activation of AMPK reduces the level of tau acetylation and ameliorates memory impairment, and its mechanism is associated with activation of Sirt1. Taken together, AMPK might be a crucial upstream molecular to regulate acetylation of tau and become a new target for AD therapy in the future.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available