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The Neurodegenerative Characteristics of Alzheimer’s Disease and Related Multi-Target Drug Design Studies
Published in Peter Grunwald, Pharmaceutical Biocatalysis, 2019
Hayrettin Ozan Gülcan, Ilkay Erdogan Orhan
Aβ deposits are not the only aggregated peptides observed in the development of AD, since tau protein hyper-phosphorylation and related tangle formation are another outcome. Tau is a brain-specific, axon-enriched microtubule-associated protein (De Felice et al., 2008). Hyper-phosphorylation of tau generates insoluble neurofibrillary tangles, also referred to as one of the biomarkers of AD. Neurofibrillary tangle formations are also toxic and lead to neuronal cell loss (Jack et al., 2011). However, the relation of Aβ plaque formation and neurofibrillary tangles is still a topic of debate, since the study results are controversial to depict whether the mechanisms to generate the formations of Aβ plaque formation and neurofibrillary tangles are independent or affecting each other.
An Outbreak of Oxidative Stress in Pathogenesis of Alzheimer's Disease
Published in Suvardhan Kanchi, Rajasekhar Chokkareddy, Mashallah Rezakazemi, Smart Nanodevices for Point-of-Care Applications, 2022
Sourbh Suren Garg, Poojith Nuthalapati, Sruchi Devi, Atulika Sharma, Debasis Sahu, Jeena Gupta
The existence of intracellular neurofibrillary tangles in the brain is possibly a hallmark of AD [27]. The event of hyperphosphorylation of tau protein contributes to the pathogenesis of Alzheimer's [28]. The interaction of tubulin with proteins attached to microtubules results in the stabilization of microtubules [29]. It has been noted that the cascade of p38 MAPK gets activated due to the presence of amyloid-β. This activation results in the aberrant phosphorylation of tau proteins in AD [30]. This aberrant phosphorylation event causes the aggregation of neurons in neurofibrillary tangles. However, aggregation of neurons makes the microtubule unstable and causes the loss of neuron functioning [31], as depicted in Figure 16.3.
The cushioning function of woodpecker’s jaw apparatus during the pecking process
Published in Computer Methods in Biomechanics and Biomedical Engineering, 2021
Peng Xu, Yikun Ni, Shan Lu, Sijian Liu, Xue Zhou, Yubo Fan
Woodpeckers have long attracted interest for their remarkable impact resistant abilities. Woodpeckers, which drummed and drilled with approximately 6–7 m/s and withstood the deceleration exceeding 1200 g, seem without any damage to its brain and eyes (May et al. 1976, 1979; Lu et al. 2020). Tau is a microtubule-associated protein in the central nervous system, and the hyperphosphorylation of tau will cause its accumulations and the loss of its physiological function. Tau accumulations usually are observed in association with chronic traumatic encephalopathy (CTE) and Alzheimer’s disease (AD) in humans. But Tau accumulations were found in the brain of woodpeckers recently (Farah et al. 2018). The impact-resistant performance of woodpecker’s head was questioned (Smoliga 2018), because CTE is a form of neurodegeneration disorder triggered by repetitive mild traumatic brain injury (mTBI). However, due to the differences in nervous systems between human and avian, it’s still unknown that these tau deposits are pathological or not (Farah et al. 2018; Smoliga 2018). What’s more, the impact-resistant mechanism of woodpeckers could be applied not only to prevent human’s traumatic brain injury (TBI) but also to develop bio-inspired structure and material for energy-absorbing (Bian and Jing 2014; Lee et al. 2016; Ni et al. 2017; Sabah et al. 2017; San Ha et al. 2019). Therefore, it is still meaningful to continue the study of woodpecker’s impact-resistant mechanism.
The protective mechanism underlying phenylethanoid glycosides (PHG) actions on synaptic plasticity in rat Alzheimer’s disease model induced by beta amyloid 1-42
Published in Journal of Toxicology and Environmental Health, Part A, 2018
Jian-xin Jia, Xu-sheng Yan, Wei Song, Xin Fang, Zhi-ping Cai, Dong-sheng Huo, He Wang, Zhan-jun Yang
Crimins et al. (2013) reported that hyper-phosphorylation of Tau protein, which accumulate in neurofibrilliary tangles (NFT) and are detected in AD brain, also produce synaptic dysfunction and loss. In our study, Aβ1-42 significantly increased expression levels of p-Tau protein, while PHG significantly inhibited phosphorylation of Tau. It is possible that PHG improved synaptic plasticity by reducing hyperphosphorylation of Tau and NFT formation in the brain, and thus prevented cell death. In conclusion, our data indicate that the protective effects of PHG on synaptic plasticity in AD model rats may be mediated through antioxidant mechanisms. It is conceivable that PHG may thus serve as a potential candidate for cognitive improvement in neurodegenerative disorders by counteracting oxidant stress.
The protective underlying mechanisms of Schisandrin on SH-SY5Y cell model of Alzheimer’s disease
Published in Journal of Toxicology and Environmental Health, Part A, 2019
Zhi-Ying Zhao, Yuan-Qing Zhang, Yong-Hui Zhang, Xie-Ze Wei, He Wang, Ming Zhang, Zhan-Jun Yang, Chun-Hong Zhang
Hyperphosphorylation of tau protein is a manifestation of AD. Treatment with Aβ1-42 was found to enhance tau protein expression, which was prevented by Schisandrin in SH-SY5Y cells. It is conceivable that Schisandrin-mediated decreased protein p-GSK-3β expression levels and reduced tau protein phosphorylation may occur subsequent to upregulation of upstream Akt phosphorylation which is consistent with the protective effect of Schisandrin in AD (Yao et al. 2019). Data suggest that Schisandrin was found to be protective against nerve damage induced by Aβ1-42 and that the underlying mechanisms involve PI3K/Akt/GSK-3β signaling pathways and tau protein phosphorylation.