scholarly journals Root-Securing and Brain-Fortifying Liquid Upregulates Caveolin-1 in Cell Model with Alzheimer’s Disease through Inhibiting Tau Phosphorylation

2017 ◽  
Vol 2017 ◽  
pp. 1-12 ◽  
Author(s):  
Depei Yuan ◽  
Chuhua Zeng ◽  
Qianfeng Chen ◽  
Fengjie Wang ◽  
Lin Yuan ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Tau Protein ◽  
Hippocampal Neurons ◽  
Cell Model ◽  
Tau Phosphorylation ◽  
Caveolin 1 ◽  
Sd Rats ◽  
A Cell ◽  
Underlying Mechanisms

In order to explore the effect of root-securing and brain-fortifying Liquid- (RSBFL-) mediated caveolin-1 (CAV-1) on phosphorylation of Tau protein and to uncover underlying mechanisms of RSBFL for the prevention and treatment of Alzheimer’s disease (AD), hippocampal neurons isolated from neonatal SD rats and cultured in DMEM-F12 medium were induced by exogenous Aβ1–42 to establish a cell model with AD. Meanwhile, pEGFP-C1-CAV1 and CAV1-shRNA plasmids were transfected into hippocampal neurons for CAV-1 overexpression and silence, respectively. The serum containing RSBFL was prepared for the intervention of AD model cells. The expression of CAV-1, GSK-3β, and p-Tau in normal hippocampal neurons and AD model cells in the presence of serum containing RSBFL was evaluated. The model hippocampal neurons with AD induced by Aβ1–42 revealed an obvious CAV-1 inhibition, enhanced GSK-3βactivity, and abnormal Tau phosphorylation. In contrast, the treatment with serum containing RSBFL could upregulate CAV-1 in AD hippocampal neurons (P<0.05) with improved p-GSK-3βSer9and reduced p-GSK-3βTyr216(P<0.01), as well as suppressed abnormal phosphorylation of Tau protein. Therefore, RSBFL has an excellent protective effect on hippocampal neurons through increasing CAV-1 expression, inhibiting GSK-3βactivity, and reducing excessive abnormal phosphorylation of Tau protein.

Overexpression of miR-26a-5p Suppresses Tau Phosphorylation and Aβ Accumulation in the Alzheimer’s Disease Mice by Targeting DYRK1A

2020 ◽  
Vol 17 (3) ◽  
pp. 241-248 ◽  
Author(s):  
Yanni Liu ◽  
Lin Wang ◽  
Fuheng Xie ◽  
Xiao Wang ◽  
Yuanyuan Hou ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Neuronal Development ◽  
Tau Phosphorylation ◽  
Luciferase Reporter ◽  
Morris Water Maze Test ◽  
Spatial Learning And Memory ◽  
Latency Time ◽  
Underlying Mechanisms

Objective: It is reported that miR-26a-5p could regulate neuronal development, but its underlying mechanisms in Alzheimer’s disease (AD) progression is unclear. Methods: APP (swe)/PS1 (ΔE9) transgenic mice served as AD mice. Morris water maze test was used to measure the spatial learning and memory ability of mice. The expressions of miR-26a-5p, DYRK1A, phosphorylated-Tau, Aβ40, and Aβ42 were detected. The relationship between miR- 26a-5p and DYRK1A was explored using dual luciferase reporter assay. The effects of miR-26a- 5p on AD mice was determined. Results: AD mice walked a lot of wrong ways to find the platform area and the latency time to reach the platform was longer. There was low expression of MiR-26a-5p in AD mice. Overexpression of miR-26a-5p inhibited Tau phosphorylation and Aβ accumulation. MiR-26a-5p negatively regulated DYRK1A via targeting its 3’UTR. In vivo, increased miR-26a-5p down-regulated Aβ40, Aβ42, p-APP and p-Tau levels in AD mice through decreasing DYRK1A. Meanwhile, the swimming path and the latency time, to reach the platform, was shorten after enhancing miR-26a-5p expression. Conclusion: Overexpression of miR-26a-5p could repress Tau phosphorylation and Aβ accumulation via down-regulating DYRK1A level in AD mice.

Pharmacological Modulations of the Serotonergic System in a Cell-Model of Familial Alzheimer’s Disease

2016 ◽  
Vol 53 (1) ◽  
pp. 349-361 ◽  
Author(s):  
Walid Tajeddinn ◽  
Torbjörn Persson ◽  
Javier Calvo-Garrido ◽  
Mohammed Seed Ahmed ◽  
Silvia Maioli ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Cell Model ◽  
Serotonergic System ◽  
Familial Alzheimer’S Disease ◽  
A Cell ◽  
Familial Alzheimer's Disease

A Cell Model for the Initial Phase of Sporadic Alzheimer's Disease

2014 ◽  
Vol 42 (2) ◽  
pp. 395-411 ◽  
Author(s):  
Carola Stockburger ◽  
Vicki A.M. Gold ◽  
Thea Pallas ◽  
Natalie Kolesova ◽  
Davide Miano ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Initial Phase ◽  
Cell Model ◽  
Sporadic Alzheimer’S Disease ◽  
A Cell

scholarly journals Dihydrolipoamide dehydrogenase suppression induce human tau phosphorylation by increasing whole body glucose levels in a C. elegans model of Alzheimer’s Disease

2017 ◽  
Author(s):  
Waqar Ahmad
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Energy Metabolism ◽  
Tau Protein ◽  
Tau Phosphorylation ◽  
Whole Body ◽  
Ionophore A23187 ◽  
Dihydrolipoamide Dehydrogenase ◽  
C Elegans ◽  
Glucose Levels

AbstractThe microtubule associated tau protein becomes hyperphosphorylated in Alzheimer’s disease (AD). While hyperphosphorylation promotes neurodegeneration, the cause and consequences of this abnormal modification are poorly understood. As impaired energy metabolism is an important hallmark of AD progression, we tested whether it could trigger phosphorylation of human tau protein in a transgenic C. elegans model of AD. We found that inhibition of a mitochondrial enzyme of energy metabolism, dihydrolipoamide dehydrogenase (DLD) resulted in elevated whole-body glucose levels as well as increased phosphorylation of tau. Hyperglycemia and tau phosphorylation were induced by either epigenetic suppression of the dld-1 gene or by inhibition of the DLD enzyme by the inhibitor, 2-methoxyindole-2-carboxylic acid (MICA). Although the calcium ionophore A23187 could reduce tau phosphorylation induced by either chemical or genetic suppression of DLD, it was unable to reduce tau phosphorylation induced by hyperglycemia. While inhibition of the dld-1 gene or treatment with MICA partially reversed the inhibition of acetylcholine neurotransmission by tau, neither treatment affected tau inhibited mobility. Conclusively, any abnormalities in energy metabolism were found to significantly affect the AD disease pathology.

Synthesis and approbation of new neuroprotective chemicals of pyrrolyl- and indolylazine classes in a cell model of Alzheimer's disease

2021 ◽  
pp. 113577
Author(s):  
Elizaveta A. Dutysheva ◽  
Irina A. Utepova ◽  
Maria A. Trestsova ◽  
Alexander S. Anisimov ◽  
Valery N. Charushin ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Cell Model ◽  
Model Of Alzheimer’S Disease ◽  
A Cell

scholarly journals PIAS3 suppresses damage in an Alzheimer’s disease cell model by inducing the STAT3-associated STAT3/Nestin/Nrf2/HO-1 pathway

2021 ◽  
Vol 27 (1) ◽  
Author(s):  
Chen Li ◽  
Ruili Wang ◽  
Youyou Zhang ◽  
Chunting Hu ◽  
Qiaoya Ma
Keyword(s):  
Oxidative Stress ◽  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Cell Model ◽  
Control Group ◽  
Heme Oxygenase 1 ◽  
Related Factor ◽  
A Cell ◽  
The Central Nervous System ◽  
And Oxidative Stress

Abstract Background Alzheimer’s disease (AD), the most common form of dementia, is caused by the degeneration of the central nervous system (CNS). A previous study reported that signal transducer and activator of transcription 3 (STAT3) is activated during AD development; nonetheless, the related mechanism remains unknown. Thus, this study used a cell model to explore whether and how the protein inhibitor of activated STAT3 (PIAS3) is involved in AD development. Methods Cerebrospinal fluid (CSF) specimens of 30 patients with AD and 10 normal participants were included in this study. SH-SY5Y cells were used to constructed AD model. Relevant indices were then detected and analyzed. Results The results showed that compared with the control group, PIAS3 expression was substantially decreased in patients with AD and amyloid beta (Aβ)-treated SH-SY5Y cells. PIAS3 overexpression was able to reverse the detrimental effects of Aβ treatment on cell survival and growth. Further, it could also ameliorate apoptosis and oxidative stress in Aβ-treated SH-SY5Y cells. Additionally, PIAS3 was shown to reduce the activated form of STAT3 and increase the activity of the downstream Nestin/nuclear factor erythroid 2-related factor/heme oxygenase-1 pathway. Conclusions STAT3 reactivation by colivelin treatment negated the influence of PIAS3 on the survival, growth, apoptosis, and oxidative stress of Aβ-treated SH-SY5Y cells.

Accelerated Aβ Generation in a Cell Model of Alzheimer's Disease-related Endosomal–Lysosomal System Upregulation

2003 ◽  
pp. 461-467
Author(s):  
Paul M. Mathews ◽  
Carolyn B. Guerra ◽  
Ying Jiang ◽  
Benjamin H. Kao ◽  
Ravi Dinakar ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Cell Model ◽  
Model Of Alzheimer’S Disease ◽  
A Cell ◽  
Lysosomal System ◽  
Aβ Generation
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