Critical role of acetylation in tau-mediated neurodegeneration and cognitive deficits.

Author: ChenXu, CongXin, DefensorErwin, EllerbyLisa, GanLi, GestwickiJason, GibsonBradford W, JohnsonJeffrey, KroganNevan, LiYaqiao, MasliahEliezer, MinSang-Won, MinamiS Sakura, MokSue Ann, SchillingBirgit, ShamlooMehrdad, ShirakawaKotaro, SohnPeter Dongmin, TracyTara E, VerdinEric, WangChao, ZhouYungui

Paper Details 
Original Abstract of the Article :
Tauopathies, including frontotemporal dementia (FTD) and Alzheimer's disease (AD), are neurodegenerative diseases in which tau fibrils accumulate. Recent evidence supports soluble tau species as the major toxic species. How soluble tau accumulates and causes neurodegeneration remains unclear. Here w...See full text at original site
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引用元:
https://pubmed.ncbi.nlm.nih.gov/26390242

データ提供:米国国立医学図書館(NLM)

Unraveling the Mystery of Tau Acetylation in Neurodegenerative Diseases

The study dives deep into the intricate world of neurodegenerative diseases, specifically tauopathies, like Alzheimer's disease and frontotemporal dementia. These conditions involve the accumulation of tau protein, which forms toxic fibrils in the brain. While the role of soluble tau species in neurodegeneration is gaining recognition, the exact mechanisms behind their accumulation and toxicity are still under investigation. This research sheds light on a critical aspect of this complex process by examining the role of tau acetylation, specifically at Lys174 (K174).

Tau Acetylation: A Key Player in Neurodegeneration

Researchers discovered that tau acetylation at K174 is an early event in Alzheimer's disease and plays a crucial role in the stability and toxicity of tau protein. The study demonstrates that altering tau acetylation affects its turnover rate and consequently influences cognitive function. The results show that mimicking acetylation at K174 slows down tau turnover and leads to cognitive deficits in mice. Conversely, inhibiting tau acetylation by using drugs like salsalate and salicylate enhances tau turnover and reduces tau levels, potentially mitigating cognitive decline. Furthermore, the study found that salsalate can effectively reduce tau-induced memory deficits and prevent hippocampal atrophy in a mouse model of frontotemporal dementia. This suggests that targeting tau acetylation could be a promising therapeutic strategy for treating neurodegenerative diseases.

A Glimpse into the Future of Tauopathy Treatment

These findings hold significant implications for treating neurodegenerative diseases. By understanding the crucial role of tau acetylation, researchers can develop new therapeutic strategies aimed at modulating tau acetylation to prevent or delay disease progression. Imagine a vast desert landscape, where tau acetylation is a hidden oasis, providing a potential source of relief for those suffering from these debilitating conditions.

Dr.Camel's Conclusion

This research offers valuable insight into the complex mechanisms underlying neurodegeneration and presents a promising avenue for therapeutic intervention. By exploring the role of tau acetylation, researchers are paving the way for innovative approaches to combat these devastating diseases.
Date :
  1. Date Completed 2016-01-19
  2. Date Revised 2022-03-31
Further Info :

Pubmed ID

26390242

DOI: Digital Object Identifier

NIHMS717753

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English

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