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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.
Nanotherapeutics: Enabling Vitamin D3 as a Multifaceted Nutraceutical
Published in Bhupinder Singh, Minna Hakkarainen, Kamalinder K. Singh, NanoNutraceuticals, 2019
Krantisagar S. More, Vinod S. Ipar, Amit S. Lokhande, Anisha A. D’souza, Padma V. Devarajan
Alzheimer’s disease is a neurodegenerative condition characterized clinically by progressive cognitive decline and histologically by senile plaques and neurofibrillary tangles. The major component of senile plaques is the amyloid β protein (Aβ), whose accumulation is accompanied by increased inflammatory responses in the brain. Such inflammatory responses cause increased influx of Ca2+ in neurons, which causes destruction of mitochondria by releasing reactive oxygen species (ROS). This Ca2+ then binds with calcium binding proteins (calcindin, calbindin), where calcindin binding causes memory loss whereas calbindin increases Ca2+ outflow. Increased Ca2+ concentration induces Aβ formation, which on binding with AβPP (Amyloid β precursor protein) causes Aβ oligomerization and fibrillation (Gezen-Ak et al., 2014). This Aβ fibrillation enhances Tau Kinase expression, which causes phosphorylation of Tau protein and neuronal death. However, vitamin D is known to exhibit neuroprotection, where it increases calbindin expression, reduces Tau Kinase activity, reacts with ROS, and reduces glutamate excitotoxicity, as shown in Figure 11.5 (Banerjee et al., 2015).
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
One of the major target proteins of OS in AD is tau protein [46]. For example, the sudden change in the conformations of tau protein is observed with 4-hydroxynonenal [47] (4-HNE). These change in protein conformations are preferably occurred due to amyloid β which ultimately lead to the formation of neurofibrillary tangles for the progression of AD. In addition to amyloid-β, the nitration reaction of tau protein also results in the formation of neurofibrillary tangles by inducing a conformational change [48]. The nitrated tau proteins are known to associate with neurofibrillary tangles before the maturation event of tau proteins which ultimately bring AD to early stages [49].
Neuroprotective effect of peanut against oxidative stress in streptozotocin-induced diabetic rats
Published in Egyptian Journal of Basic and Applied Sciences, 2022
Norhan H. Mohamed, Hassan Elsayad, Yasser M. Elsherbini, Mohamed E. Abdraboh
The observed findings revealed that the diabetic-related inflammation led to injured brain structure and reduced brain function which were correlated with the significant upregulation of brain tau protein, amyloid-β and α-amylase. In diabetes, amyloid-β and tau proteins have been considered as the major components of senile plaques and neurofibrillary tangles, respectively. The hyperphosphorylation of tau protein would stimulate its aggregation to form neurofibrillary tangles [61]. The hippocampus of STZ-induced diabetic rats showed a significant increase in the levels of amyloid precursor protein (APP), amyloid-β expressions and phosphorylated tau [62,63]. The upregulation of brain α-amylase enzyme level in diabetic rats indicated their high susceptibility to neuronal damage which was reversed by peanut oral supplementation. These results were supported by other studies which revealed the role of altered levels of α-amylase in brains leading to variations of glucose readiness and neuropathological changes observed in patients with Alzheimer’s disease [64].
Investigating sensitivity coefficients characterizing the response of a model of tau protein transport in an axon to model parameters
Published in Computer Methods in Biomechanics and Biomedical Engineering, 2019
Ivan A. Kuznetsov, Andrey V. Kuznetsov
One of the hallmarks of Alzheimer’s disease (AD) is the formation of insoluble neurofibrillary tangles (NFTs) composed of tau protein (Ballatore et al. 2007; Tai et al. 2012; Ittner et al. 2011; Bloom 2014). Some recent research suggests that abnormalities in axonal transport precede NFT formation and any clinical symptoms of AD (Moreno et al. 2016). The relevance to AD explains the importance of understanding and modeling tau transport in neurons. This is especially important because tau and its interaction with microtubules (MTs) have been identified as a possible therapeutic target in AD (Boutajangout et al. 2011; Pachima et al. 2016; Lippens et al. 2016). For example, DeVos et al. (2017) presented evidence that tau reduction therapy can reverse tau seeding capability in aged mice with tauopathy.
A quantitative risk assessment for chronic traumatic encephalopathy (CTE) in football: How public health science evaluates evidence
Published in Human and Ecological Risk Assessment: An International Journal, 2019
Adam M. Finkel, Kevin F. Bieniek
According to the 2017 Berlin Consensus Statement on Concussion in Sports by 36 neuroscientists, “chronic traumatic encephalopathy (CTE)… appears to represent a distinct tauopathy with an unknown incidence in athletic populations” (McCrory et al.2017). The term “tauopathy” refers to one of several neurodegenerative diseases, including frontotemporal lobar degeneration (FTLD) and progressive supranuclear palsy (PSP), in which the protein tau (found in normal human brain) becomes abnormally aggregated and forms inclusion bodies within nerve and glial cells in the brain. The abnormal tau becomes burdened by an excess of phosphate groups (hyperphosphorylation). A frequent inclusion body containing abnormal and insoluble tau is the “neurofibrillary tangle,” a lesion most often seen in the Alzheimer's disease (AD) brain.14AD also involves aggregation of hyperphosphorylated tau, but because its primary hallmark is the accumulation of fibrils of amyloid protein within plaques, it is considered a “secondary tauopathy.” CTE per se (when not co-existing with AD) does not display amyloid accumulation. In CTE, these tangles accumulate in a characteristic pattern that is different from AD and other tauopathies. A consensus conference of neuropathologists, sponsored by the National Institutes of Health, defined the pathognomonic lesion of CTE as hyperphosphorylated tau aggregates in neurons, astrocytes, and cell processes around small vessels in an irregular pattern at the depths of the cortical sulci (McKee et al.2016). There appear to be two different clinical presentations of CTE (Stern et al.2013); some cases begin relatively early in life (ages 30–50) and involve behavioral and mood disturbances with minimal cognitive impairment, while others begin later in life and display marked cognitive impairment and often motor disturbances as well.