Tau protein phosphorylation in Alzheimer's disease and in experimental models

2000 ◽  
Vol 28 (1) ◽  
pp. A15-A15
Author(s):  
I.P. Brion
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Protein Phosphorylation ◽  
Tau Protein ◽  
Experimental Models

scholarly journals A current view on Tau protein phosphorylation in Alzheimer's disease

2021 ◽  
Vol 69 ◽  
pp. 131-138
Author(s):  
Susanne Wegmann ◽  
Jacek Biernat ◽  
Eckhard Mandelkow
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Protein Phosphorylation ◽  
Tau Protein ◽  
Current View ◽  
A Current

scholarly journals Lithium inhibits Alzheimer's disease-like tau protein phosphorylation in neurons

FEBS Letters ◽  
1997 ◽  
Vol 411 (2-3) ◽  
pp. 183-188 ◽  
Author(s):  
Juan Ramón Muñoz-Montaño ◽  
Francisco J. Moreno ◽  
Jesús Avila ◽  
Javier Dı́az-Nido
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Protein Phosphorylation ◽  
Tau Protein

Quantitative analysis of tau protein in paired helical filament preparations: Implications for the role of tau protein phosphorylation in PHF assembly in Alzheimer's disease

1995 ◽  
Vol 16 (3) ◽  
pp. 409-417 ◽  
Author(s):  
Claude M. Wischik ◽  
Patricia C. Edwards ◽  
Robert Y.K. Lai ◽  
Herman N.-J. Gertz ◽  
John H. Xuereb ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Quantitative Analysis ◽  
Protein Phosphorylation ◽  
Tau Protein ◽  
Paired Helical Filament

Interleukin-1 promotion of MAPK-p38 overexpression in experimental animals and in Alzheimer's disease: potential significance for tau protein phosphorylation

2001 ◽  
Vol 39 (5-6) ◽  
pp. 341-348 ◽  
Author(s):  
Jin G. Sheng ◽  
Richard A. Jones ◽  
Xue Q. Zhou ◽  
John M. McGinness ◽  
Linda J. Van Eldik ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Protein Phosphorylation ◽  
Tau Protein ◽  
Interleukin 1 ◽  
Potential Significance ◽  
Experimental Animals

Osthole decreases tau protein phosphorylation via PI3K/AKT/GSK-3β signaling pathway in Alzheimer's disease

Life Sciences ◽  
2019 ◽  
Vol 217 ◽  
pp. 16-24 ◽  
Author(s):  
Yingjia Yao ◽  
Yameng Wang ◽  
Liang Kong ◽  
Yuqing Chen ◽  
Jingxian Yang
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Protein Phosphorylation ◽  
Signaling Pathway ◽  
Tau Protein ◽  
Gsk 3Β

scholarly journals Accelerating action of Alzheimer’s disease gut microbiota on Tau protein hyperphosphorylation: crosstalk of inflammation and autophagy

2020 ◽  
Author(s):  
Guo Yinrui ◽  
Tang Xiaocui ◽  
Qi Longkai ◽  
Yang Xin ◽  
Li Ran ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Gut Microbiota ◽  
Protein Phosphorylation ◽  
Tau Protein ◽  
Hippocampal Slices ◽  
Long Term Potentiation ◽  
Early Exposure ◽  
Newborn Mice ◽  
Metabolism Disorder

Abstract Background: The gut-brain axis has been implicated in the complex pathogenesis of Alzheimer’s disease (AD), but the action is unclear, this study was performed to clarify the effect of ad-related gut microbiota on the pathogenesis of AD during pregnancy and early exposure. Methods: A pilot study of gut microbiota in AD patients was performed.Gut microbiota structure, long-term potentiation (LTP), inflammation levels, AD biomarkers, and metabolomics of serum and fecal were monitored after cohousing by cohousing in early life (from pregnancy 14 days to birth 14 days with 8-month old APP/PS1 mice).The regulatory action of bacterial metabolites on Tau protein phosphorylation was evaluated. Results: Gut microbiota from APP/SP1 mice altered structure of gut microbiota in newborn mice, LTP in hippocampal slices was significantly shortened, and inflammatory markers levels were increased, AD biomarkers were upregulated, with significantly higher Tau protein phosphorylation at multiple sites (p < 0.05). Conclusions: These results imply ad-related gut microbiota can change the structure of gut microbiota during pregnancy and early exposure. Changing the structure of gut microbiota in the newborn mice can induce leucine metabolism disorder, induce mTOR mediated autophagy dysfunction and increase the level of inflammation, thus leading to accelerate Tau protein phosphorylation and reduce LTP occurs in AD-cohousing mouse hippocampus.

scholarly journals Assessing the therapeutic potential of Graptopetalum paraguayense on Alzheimer’s disease using patient iPSC-derived neurons

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Pei-Chun Wu ◽  
Ming-Ji Fann ◽  
Tu Thanh Tran ◽  
Shu-Cian Chen ◽  
Tania Devina ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Protein Phosphorylation ◽  
Tau Protein ◽  
Therapeutic Potential ◽  
Herbal Medicines ◽  
Induced Pluripotent Stem Cell ◽  
Enrichment Analysis ◽  
Gene Set Enrichment Analysis ◽  
Human Ipscs

AbstractAlzheimer’s disease (AD) is the most common type of dementia and also one of the leading causes of death worldwide. However, the underlying mechanisms remain unclear, and currently there is no drug treatment that can prevent or cure AD. Here, we have applied the advantages of using induced pluripotent stem cell (iPSC)-derived neurons (iNs) from AD patients, which are able to offer human-specific drug responsiveness, in order to evaluate therapeutic candidates for AD. Using approach involving an inducible neurogenin-2 transgene, we have established a robust and reproducible protocol for differentiating human iPSCs into glutamatergic neurons. The AD-iN cultures that result have mature phenotypic and physiological properties, together with AD-like biochemical features that include extracellular β-amyloid (Aβ) accumulation and Tau protein phosphorylation. By screening using a gene set enrichment analysis (GSEA) approach, Graptopetalum paraguayense (GP) has been identified as a potential therapeutic agent for AD from among a range of Chinese herbal medicines. We found that administration of a GP extract caused a significantly reduction in the AD-associated phenotypes of the iNs, including decreased levels of extracellular Aβ40 and Aβ42, as well as reduced Tau protein phosphorylation at positions Ser214 and Ser396. Additionally, the effect of GP was more prominent in AD-iNs compared to non-diseased controls. These findings provide valuable information that suggests moving extracts of GP toward drug development, either for treating AD or as a health supplement to prevent AD. Furthermore, our human iN-based platform promises to be a useful strategy when it is used for AD drug discovery.

Targeting Tau Hyperphosphorylation via Kinase Inhibition: Strategy to Address Alzheimer's Disease

2020 ◽  
Vol 20 (12) ◽  
pp. 1059-1073 ◽  
Author(s):  
Ahmad Abu Turab Naqvi ◽  
Gulam Mustafa Hasan ◽  
Md. Imtaiyaz Hassan
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Tau Protein ◽  
Glycogen Synthase ◽  
Paired Helical Filaments ◽  
Tau Hyperphosphorylation ◽  
Microtubule Stabilization ◽  
Extracellular Signal

Microtubule-associated protein tau is involved in the tubulin binding leading to microtubule stabilization in neuronal cells which is essential for stabilization of neuron cytoskeleton. The regulation of tau activity is accommodated by several kinases which phosphorylate tau protein on specific sites. In pathological conditions, abnormal activity of tau kinases such as glycogen synthase kinase-3 &#946; (GSK3&#946;), cyclin-dependent kinase 5 (CDK5), c-Jun N-terminal kinases (JNKs), extracellular signal-regulated kinase 1 and 2 (ERK1/2) and microtubule affinity regulating kinase (MARK) lead to tau hyperphosphorylation. Hyperphosphorylation of tau protein leads to aggregation of tau into paired helical filaments like structures which are major constituents of neurofibrillary tangles, a hallmark of Alzheimer’s disease. In this review, we discuss various tau protein kinases and their association with tau hyperphosphorylation. We also discuss various strategies and the advancements made in the area of Alzheimer&#039;s disease drug development by designing effective and specific inhibitors for such kinases using traditional in vitro/in vivo methods and state of the art in silico techniques.

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