dc.contributor.author | Uddin M.S. | |
dc.contributor.author | Tewari D. | |
dc.contributor.author | Sharma G. | |
dc.contributor.author | Kabir M.T. | |
dc.contributor.author | Barreto G.E. | |
dc.contributor.author | Bin-Jumah M.N. | |
dc.contributor.author | Perveen A. | |
dc.contributor.author | Abdel-Daim M.M. | |
dc.contributor.author | Ashraf G.M. | |
dc.date.accessioned | 2020-09-02T22:29:30Z | |
dc.date.available | 2020-09-02T22:29:30Z | |
dc.date.issued | 2020 | |
dc.identifier | 10.1007/s12035-020-01929-y | |
dc.identifier.citation | 57, 7, 2902-2919 | |
dc.identifier.issn | 08937648 | |
dc.identifier.uri | https://hdl.handle.net/20.500.12728/6469 | |
dc.description | Alzheimer’s disease (AD) is a progressive neurodegenerative disease involving aggregation of misfolded proteins inside the neuron causing prolonged cellular stress. The neuropathological hallmarks of AD include the formation of senile plaques and neurofibrillary tangles in specific brain regions that lead to synaptic loss and neuronal death. The exact mechanism of neuron dysfunction in AD remains obscure. In recent years, endoplasmic reticulum (ER) dysfunction has been implicated in neuronal degeneration seen in AD. Apart from AD, many other diseases also involve misfolded proteins aggregations in the ER, a condition referred to as ER stress. The response of the cell to ER stress is to activate a group of signaling pathways called unfolded protein response (UPR) that stimulates a particular transcriptional program to restore ER function and ensure cell survival. ER stress also involves the generation of reactive oxygen species (ROS) that, together with mitochondrial ROS and decreased effectiveness of antioxidant mechanisms, producing a condition of chronic oxidative stress. The unfolded proteins may not always produce a response that leads to the restoration of cellular functions, but they may also lead to inflammation by a set of different pathways with deleterious consequences. In this review, we extensively discuss the role of ER stress and how to target it using different pharmacological approaches in AD development and onset. © 2020, Springer Science+Business Media, LLC, part of Springer Nature. | |
dc.language.iso | en | |
dc.publisher | Springer | |
dc.subject | Alzheimer’s disease | |
dc.subject | Amyloid β | |
dc.subject | Endoplasmic reticulum | |
dc.subject | Tau | |
dc.subject | Unfolded protein response | |
dc.subject | activating transcription factor 4 | |
dc.subject | activating transcription factor 6 | |
dc.subject | ADAM10 endopeptidase | |
dc.subject | adenosine triphosphatase (calcium) | |
dc.subject | amyloid beta protein | |
dc.subject | amyloid precursor protein | |
dc.subject | anthra[1,9 cd]pyrazol 6(2h) one | |
dc.subject | beta secretase 1 | |
dc.subject | calcium calmodulin dependent protein kinase II | |
dc.subject | dibenzoylmethane derivative | |
dc.subject | glucose regulated protein 78 | |
dc.subject | glutathione | |
dc.subject | glycogen synthase kinase 3 inhibitor | |
dc.subject | growth arrest and DNA damage inducible protein 153 | |
dc.subject | gsk 2606414 | |
dc.subject | initiation factor 2 | |
dc.subject | initiation factor 2alpha | |
dc.subject | inositol 1,4,5 trisphosphate receptor | |
dc.subject | pancreatic ER kinase | |
dc.subject | protein disulfide isomerase | |
dc.subject | protein IRE1 | |
dc.subject | protein kinase | |
dc.subject | protein tyrosine kinase inhibitor | |
dc.subject | reactive oxygen metabolite | |
dc.subject | resveratrol | |
dc.subject | tau protein | |
dc.subject | transcription factor Nrf2 | |
dc.subject | trazodone | |
dc.subject | unclassified drug | |
dc.subject | unindexed drug | |
dc.subject | X box binding protein 1 | |
dc.subject | Alzheimer disease | |
dc.subject | apoptosis | |
dc.subject | autophagy (cellular) | |
dc.subject | brain mitochondrion | |
dc.subject | calcium signaling | |
dc.subject | endoplasmic reticulum | |
dc.subject | endoplasmic reticulum stress | |
dc.subject | gene expression | |
dc.subject | gene overexpression | |
dc.subject | hippocampus | |
dc.subject | human | |
dc.subject | hyperphosphorylation | |
dc.subject | immunohistochemistry | |
dc.subject | nerve cell necrosis | |
dc.subject | nonhuman | |
dc.subject | oxidative stress | |
dc.subject | pathogenesis | |
dc.subject | phosphorylation | |
dc.subject | protein aggregation | |
dc.subject | protein degradation | |
dc.subject | protein expression | |
dc.subject | protein folding | |
dc.subject | protein phosphorylation | |
dc.subject | protein protein interaction | |
dc.subject | Review | |
dc.subject | temporal cortex | |
dc.subject | unfolded protein response | |
dc.subject | upregulation | |
dc.subject | Western blotting | |
dc.title | Molecular Mechanisms of ER Stress and UPR in the Pathogenesis of Alzheimer’s Disease | |
dc.type | Review | |