scholarly journals Aluminum alters cell viability and axonal transport system in Alzheimer's disease pathogenic mutation-bearing cells

2004 ◽  
Vol 4 (2) ◽  
pp. 20-23
Author(s):  
Hisashi TANII ◽  
Naohiko MATSUMOTO ◽  
Yujiro KASHIWAGI ◽  
Masayasu OKOCHI ◽  
Toshihisa TANAKA ◽  
...  
2013 ◽  
Vol 246 ◽  
pp. 44-53 ◽  
Author(s):  
Nicholas M. Kanaan ◽  
Gustavo F. Pigino ◽  
Scott T. Brady ◽  
Orly Lazarov ◽  
Lester I. Binder ◽  
...  

2021 ◽  
Vol 17 (6) ◽  
pp. 1123-1130
Author(s):  
Qichen Pan ◽  
Yunchao Ban ◽  
Lijun Xu

Alzheimer’s disease (AD) is strongly associated with oxidative stress which can damage neural cells. Silibinin has shown potential antioxidative effects. However, due to its low solubility in water, silibinin provides low biological activity and bioavailability. Therefore, to increase its pharmacological effects, silibilin was encapsulated into human serum albumin (HSA) nanoparticles and well-characterized by DLS and TEM techniques. The antioxidant activity of silibinin-HSA nanoparticles was evaluated on LPS-induced oxidative stress in neuron-like cells (SH-SY5Y) through MTT, antioxidant activity and apoptotic assay. It was shown that the mean diameter of HSA and silibinin-HSA nanoparticles were 88 and 105 nm, respectively with a drug loading of 24.08%, drug encapsulation rate of 94.72%, and the yield of silibinin-HSA nanoparticles of around 83.41% and the HSA nano-formulation released silibinin for 15 h. The results displayed that cell viability was reduced by LPS (10 μg/mL), who’s also determined to stimulate oxidative stress and apoptosis. However, co-incubation of cells with silibinin (50 μg/mL) or silibinin-HSA nanoparticles led to the recovery of cell viability, activation of SOD and CAT, increase of GSH content, and reduction of ROS level, Caspase-3 activity and fragmentation of DNA. It was also indicated that the neuroprotective and antioxidant activities of silibinin-HAS nanoparticles was greater than free silibinin, indicating that using albumin can be a potential formulation approach for improving the antioxidant efficacy of silibinin.


2002 ◽  
Vol 2 (2) ◽  
pp. 151-166 ◽  
Author(s):  
Dick Terwel ◽  
Ilse Dewachter ◽  
Fred Van Leuven

2017 ◽  
Vol 216 (10) ◽  
pp. 3161-3178 ◽  
Author(s):  
Xiaoyi Qu ◽  
Feng Ning Yuan ◽  
Carlo Corona ◽  
Silvia Pasini ◽  
Maria Elena Pero ◽  
...  

Oligomeric Amyloid β1–42 (Aβ) plays a crucial synaptotoxic role in Alzheimer’s disease, and hyperphosphorylated tau facilitates Aβ toxicity. The link between Aβ and tau, however, remains controversial. In this study, we find that in hippocampal neurons, Aβ acutely induces tubulin posttranslational modifications (PTMs) and stabilizes dynamic microtubules (MTs) by reducing their catastrophe frequency. Silencing or acute inhibition of the formin mDia1 suppresses these activities and corrects the synaptotoxicity and deficits of axonal transport induced by Aβ. We explored the mechanism of rescue and found that stabilization of dynamic MTs promotes tau-dependent loss of dendritic spines and tau hyperphosphorylation. Collectively, these results uncover a novel role for mDia1 in Aβ-mediated synaptotoxicity and demonstrate that inhibition of MT dynamics and accumulation of PTMs are driving factors for the induction of tau-mediated neuronal damage.


Talanta ◽  
2021 ◽  
Vol 223 ◽  
pp. 121738
Author(s):  
Meng-Meng Liu ◽  
Hui Liu ◽  
Shan-Hong Li ◽  
Yu Zhong ◽  
Yao Chen ◽  
...  

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