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Journal articles on the topic 'Amyloidopathie'

Author: Grafiati
Published: 14 February 2023

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1

Regland, Björn, and Andrew McCaddon. "Alzheimer’s Amyloidopathy: An Alternative Aspect." Journal of Alzheimer's Disease 68, no. 2 (March 29, 2019): 483–88. http://dx.doi.org/10.3233/jad-181007.

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2

Philippens, Ingrid H. C. H. M., and Jan A. M. Langermans. "Preclinical Marmoset Model for Targeting Chronic Inflammation as a Strategy to Prevent Alzheimer’s Disease." Vaccines 9, no. 4 (April 15, 2021): 388. http://dx.doi.org/10.3390/vaccines9040388.

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Due to the aging population, modern society is facing an increasing prevalence of neurological diseases such as Alzheimer’s disease (AD). AD is an age-related chronic neurodegenerative disorder for which no satisfying therapy exists. Understanding the mechanisms underlying the onset of AD is necessary to find targets for protective treatment. There is growing awareness of the essential role of the immune system in the early AD pathology. Amyloidopathy, the main feature of early-stage AD, has a deregulating effect on the immune function. This is reciprocal as the immune system also affects amyloidopathy. It seems that the inflammatory reaction shows a heterogeneous pattern depending on the stage of the disease and the variation between individuals, making not only the target but also the timing of treatment important. The lack of relevant translational animal models that faithfully reproduce clinical and pathogenic features of AD is a major cause of the delay in developing new disease-modifying therapies and their optimal timing of administration. This review describes the communication between amyloidopathy and inflammation and the possibility of using nonhuman primates as a relevant animal model for preclinical AD research.
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3

Opel, Ryan A., Alison Christy, Erin L. Boespflug, Kristianna B. Weymann, Brendan Case, Jeffery M. Pollock, Lisa C. Silbert, and Miranda M. Lim. "Effects of traumatic brain injury on sleep and enlarged perivascular spaces." Journal of Cerebral Blood Flow & Metabolism 39, no. 11 (August 10, 2018): 2258–67. http://dx.doi.org/10.1177/0271678x18791632.

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Clearance of perivascular wastes in the brain may be critical to the pathogenesis of amyloidopathies. Enlarged perivascular spaces (ePVS) on MRI have also been associated with amyloidopathies, suggesting that there may be a mechanistic link between ePVS and impaired clearance. Sleep and traumatic brain injury (TBI) both modulate clearance of amyloid-beta through glymphatic function. Therefore, we sought to evaluate the relationship between sleep, TBI, and ePVS on brain MRI. A retrospective study was performed in individuals with overnight polysomnography and 3T brain MRI consented from a single site ( n = 38). Thirteen of these individuals had a medically confirmed history of TBI. ePVS were visually assessed by blinded experimenters and analyzed in conjunction with sleep metrics and TBI status. Overall, individuals with shorter total sleep time had significantly higher ePVS burden. Furthermore, individuals with TBI showed a stronger relationship between sleep and ePVS compared to the non-TBI group. These results support the hypothesis that ePVS may be modulated by sleep and TBI, and may have implications for the role of the glymphatic system in ePVS.
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4

Maloney, Michael T., and James R. Bamburg. "Cofilin-mediated neurodegeneration in alzheimer’s disease and other amyloidopathies." Molecular Neurobiology 35, no. 1 (January 2007): 21–43. http://dx.doi.org/10.1007/bf02700622.

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5

Maloney, Michael T., and James R. Bamburg. "Cofilin-mediated neurodegeneration in alzheimer’s disease and other amyloidopathies." Molecular Neurobiology 35, no. 1 (January 2007): 21–43. http://dx.doi.org/10.1007/s12035-007-0009-y.

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Maloney, Michael T., and James R. Bamburg. "Cofilin-Mediated Neurodegeneration in Alzheimer’s Disease and Other Amyloidopathies." Molecular Neurobiology 36, no. 2 (October 2, 2007): 201–4. http://dx.doi.org/10.1007/s12035-007-8011-y.

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7

Iohan, Lukas da Cruz Carvalho, Jean-Charles Lambert, and Marcos R. Costa. "Analysis of modular gene co-expression networks reveals molecular pathways underlying Alzheimer’s disease and progressive supranuclear palsy." PLOS ONE 17, no. 4 (April 14, 2022): e0266405. http://dx.doi.org/10.1371/journal.pone.0266405.

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A comprehensive understanding of the pathological mechanisms involved at different stages of neurodegenerative diseases is key for the advance of preventive and disease-modifying treatments. Gene expression alterations in the diseased brain is a potential source of information about biological processes affected by pathology. In this work, we performed a systematic comparison of gene expression alterations in the brains of human patients diagnosed with Alzheimer’s disease (AD) or Progressive Supranuclear Palsy (PSP) and animal models of amyloidopathy and tauopathy. Using a systems biology approach to uncover biological processes associated with gene expression alterations, we could pinpoint processes more strongly associated with tauopathy/PSP and amyloidopathy/AD. We show that gene expression alterations related to immune-inflammatory responses preponderate in younger, whereas those associated to synaptic transmission are mainly observed in older AD patients. In PSP, however, changes associated with immune-inflammatory responses and synaptic transmission overlap. These two different patterns observed in AD and PSP brains are fairly recapitulated in animal models of amyloidopathy and tauopathy, respectively. Moreover, in AD, but not PSP or animal models, gene expression alterations related to RNA splicing are highly prevalent, whereas those associated with myelination are enriched both in AD and PSP, but not in animal models. Finally, we identify 12 AD and 4 PSP genetic risk factors in cell-type specific co-expression modules, thus contributing to unveil the possible role of these genes to pathogenesis. Altogether, this work contributes to unravel the potential biological processes affected by amyloid versus tau pathology and how they could contribute to the pathogenesis of AD and PSP.
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8

Zhou, Zhi, Martijn L. T. M. Müller, Prabesh Kanel, Jason Chua, Vikas Kotagal, Daniel I. Kaufer, Roger L. Albin, Kirk A. Frey, and Nicolaas I. Bohnen. "Apathy rating scores and β-amyloidopathy in patients with Parkinson disease at risk for cognitive decline." Neurology 94, no. 4 (November 15, 2019): e376-e383. http://dx.doi.org/10.1212/wnl.0000000000008683.

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ObjectiveTo determine whether β-amyloidopathy correlates with apathy rating scores independently of mood changes and other neurodegenerative processes in Parkinson disease (PD).MethodsIn this cross-sectional study, patients with PD (n = 64, 48 male and 16 female, mean age 69.2 ± 6.7 years, Hoehn & Yahr stage 2.7 ± 0.5, Montreal Cognitive Assessment score 25.3 ± 3.0) underwent [11C]Pittsburgh compound B β-amyloid, [11C]dihydrotetrabenazine vesicular monoamine transporter type 2 (VMAT2), and [11C]methyl 4 piperidinyl propionate acetylcholinesterase brain PET imaging and clinical assessments, including the Marin Apathy Evaluation Scale, Clinician Version. Patients were recruited on the basis of having at least 1 risk factor for PD dementia, but they were excluded if they had dementia.ResultsMean apathy rating score was 25.4 ± 6.4, reflecting predominantly subclinical apathy. Apathy rating scale scores correlated with amyloid binding, cognitive, depressive, and anxiety scores but not significantly with age, duration of disease, striatal VMAT2, or cholinergic binding. Multiple regression analysis model (p < 0.0001) showed significant regressor effects for global β-amyloid burden (p = 0.0038) with significant covariate effects for global cognitive z scores (p = 0.028) and for anxiety (p = 0.038) but not with depressive scores. Voxel-based analysis showed robust correlation between apathy rating scale scores and β-amyloid binding in bilateral nuclei accumbens, inferior frontal, and cingulate cortices (family-wise error rate–corrected p < 0.005).ConclusionApathy is independently associated with β-amyloidopathy in patients with PD at risk of dementia. Regional brain findings are most robust for β-amyloidopathy in the nuclei accumbens, inferior frontal, and cingulate regions. Findings may provide an explanation for the often treatment-refractory nature of apathy in advancing PD despite optimized dopaminergic and antidepressant pharmacotherapy.ClinicalTrials.gov identifier:NCT01565473.
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9

Frey, Kirk A., and Myria Petrou. "Imaging amyloidopathy in Parkinson disease and parkinsonian dementia syndromes." Clinical and Translational Imaging 3, no. 1 (February 2015): 57–64. http://dx.doi.org/10.1007/s40336-015-0104-4.

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10

Mattana, Sara, Silvia Caponi, Francesco Tamagnini, Daniele Fioretto, and Francesca Palombo. "Viscoelasticity of amyloid plaques in transgenic mouse brain studied by Brillouin microspectroscopy and correlative Raman analysis." Journal of Innovative Optical Health Sciences 10, no. 06 (November 2017): 1742001. http://dx.doi.org/10.1142/s1793545817420019.

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Amyloidopathy is one of the most prominent hallmarks of Alzheimer’s disease (AD), the leading cause of dementia worldwide, and is characterized by the accumulation of amyloid plaques in the brain parenchyma. The plaques consist of abnormal deposits mainly composed of an aggregation-prone protein fragment, [Formula: see text]-amyloid 1-40/1-42, into the extracellular matrix. Brillouin microspectroscopy is an all-optical contactless technique that is based on the interaction between visible light and longitudinal acoustic waves or phonons, giving access to the viscoelasticity of a sample on a subcellular scale. Here, we describe the first application of micromechanical mapping based on Brillouin scattering spectroscopy to probe the stiffness of individual amyloid plaques in the hippocampal part of the brain of a [Formula: see text]-amyloid overexpressing transgenic mouse. Correlative analysis based on Brillouin and Raman microspectroscopy showed that amyloid plaques have a complex structure with a rigid core of [Formula: see text]-pleated sheet conformation ([Formula: see text]-amyloid) protein surrounded by a softer ring-shaped region richer in lipids and other protein conformations. These preliminary results give a new insight into the plaque biophysics and biomechanics, and a valuable contrast mechanism for the study and diagnosis of amyloidopathy.
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11

More, Swati S., James M. Beach, and Robert Vince. "Early Detection of Amyloidopathy in Alzheimer's Mice by Hyperspectral Endoscopy." Investigative Opthalmology & Visual Science 57, no. 7 (June 22, 2016): 3231. http://dx.doi.org/10.1167/iovs.15-17406.

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12

Shah, Neha, Kirk A. Frey, Martijn L.T.M Müller, Myria Petrou, Vikas Kotagal, Robert A. Koeppe, Peter J. H. Scott, Roger L. Albin, and Nicolaas I. Bohnen. "Striatal and Cortical β-Amyloidopathy and Cognition in Parkinson's Disease." Movement Disorders 31, no. 1 (September 18, 2015): 111–17. http://dx.doi.org/10.1002/mds.26369.

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13

Bourdenx, Mathieu, Nikolaos Stavros Koulakiotis, Despina Sanoudou, Erwan Bezard, Benjamin Dehay, and Anthony Tsarbopoulos. "Protein aggregation and neurodegeneration in prototypical neurodegenerative diseases: Examples of amyloidopathies, tauopathies and synucleinopathies." Progress in Neurobiology 155 (August 2017): 171–93. http://dx.doi.org/10.1016/j.pneurobio.2015.07.003.

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14

Allali, Gilles, Ilse Kern, Magali Laidet, Stéphane Armand, and Frédéric Assal. "Parkinsonism is a Phenotypical Signature of Amyloidopathy in Patients with Gait Disorders." Journal of Alzheimer's Disease 63, no. 4 (May 30, 2018): 1373–81. http://dx.doi.org/10.3233/jad-171055.

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15

Yu, Ji Sun, Gwang Je Kim, Byoung-sub Lee, Aerim Choe, Sungmin Kang, Yechan Joh, Shinwon Kim, et al. "P1-257: A BLOOD TEST OF AMYLOIDOPATHY FOR DIAGNOSIS OF ALZHEIMER'S DISEASE." Alzheimer's & Dementia 14, no. 7S_Part_7 (July 1, 2006): P379. http://dx.doi.org/10.1016/j.jalz.2018.06.263.

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16

Ermilov, V. V., and A. A. Nesterova. "Beta-amyloidopathy as a manifestation of proteinopathy in age-related macular degeneration." Vestnik oftal'mologii 131, no. 2 (2015): 26. http://dx.doi.org/10.17116/oftalma2015131226-31.

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17

Zhang, Hongyu, Changlong Hao, Aihua Qu, Maozhong Sun, Liguang Xu, Chuanlai Xu, and Hua Kuang. "Light‐Induced Chiral Iron Copper Selenide Nanoparticles Prevent β‐Amyloidopathy In Vivo." Angewandte Chemie 132, no. 18 (March 10, 2020): 7197–204. http://dx.doi.org/10.1002/ange.202002028.

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18

Zhang, Hongyu, Changlong Hao, Aihua Qu, Maozhong Sun, Liguang Xu, Chuanlai Xu, and Hua Kuang. "Light‐Induced Chiral Iron Copper Selenide Nanoparticles Prevent β‐Amyloidopathy In Vivo." Angewandte Chemie International Edition 59, no. 18 (March 10, 2020): 7131–38. http://dx.doi.org/10.1002/anie.202002028.

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19

Pichla, Monika, Grzegorz Bartosz, and Izabela Sadowska-Bartosz. "The Antiaggregative and Antiamyloidogenic Properties of Nanoparticles: A Promising Tool for the Treatment and Diagnostics of Neurodegenerative Diseases." Oxidative Medicine and Cellular Longevity 2020 (October 13, 2020): 1–11. http://dx.doi.org/10.1155/2020/3534570.

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Due to the progressive aging of the society, the prevalence and socioeconomic burden of neurodegenerative diseases are predicted to rise. The most common neurodegenerative disorders nowadays, such as Parkinson’s disease, Alzheimer’s disease, and amyotrophic lateral sclerosis, can be classified as proteinopathies. They can be either synucleinopathies, amyloidopathies, tauopathies, or TDP-43-related proteinopathies; thus, nanoparticles with a potential ability to inhibit pathological protein aggregation and/or degrade already existing aggregates can be a promising approach in the treatment of neurodegenerative diseases. As it turns out, nanoparticles can be a double-edged sword; they can either promote or inhibit protein aggregation, depending on coating, shape, size, surface charge, and concentration. In this review, we aim to emphasize the need of a breakthrough in the treatment of neurodegenerative disorders and draw attention to nanomaterials, as they can also serve as a diagnostic tool for protein aggregates or can be used in a high-throughput screening for novel antiaggregative compounds.
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20

Wieczorek, Elżbieta, and Andrzej Ożyhar. "Transthyretin: From Structural Stability to Osteoarticular and Cardiovascular Diseases." Cells 10, no. 7 (July 13, 2021): 1768. http://dx.doi.org/10.3390/cells10071768.

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Transthyretin (TTR) is a tetrameric protein transporting hormones in the plasma and brain, which has many other activities that have not been fully acknowledged. TTR is a positive indicator of nutrition status and is negatively correlated with inflammation. TTR is a neuroprotective and oxidative-stress-suppressing factor. The TTR structure is destabilized by mutations, oxidative modifications, aging, proteolysis, and metal cations, including Ca2+. Destabilized TTR molecules form amyloid deposits, resulting in senile and familial amyloidopathies. This review links structural stability of TTR with the environmental factors, particularly oxidative stress and Ca2+, and the processes involved in the pathogenesis of TTR-related diseases. The roles of TTR in biomineralization, calcification, and osteoarticular and cardiovascular diseases are broadly discussed. The association of TTR-related diseases and vascular and ligament tissue calcification with TTR levels and TTR structure is presented. It is indicated that unaggregated TTR and TTR amyloid are bound by vicious cycles, and that TTR may have an as yet undetermined role(s) at the crossroads of calcification, blood coagulation, and immune response.
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21

Lee, Hyun-ju, Ha-Ram Jeong, Jin-Hee Park, and Hyang-Sook Hoe. "Idebenone Decreases Aβ Pathology by Modulating RAGE/Caspase-3 Signaling and the Aβ Degradation Enzyme NEP in a Mouse Model of AD." Biology 10, no. 9 (September 19, 2021): 938. http://dx.doi.org/10.3390/biology10090938.

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The coenzyme Q10 analogue idebenone is an FDA-approved antioxidant that can cross the blood–brain barrier (BBB). The effects of idebenone on the pathology of Alzheimer’s disease (AD) and the underlying molecular mechanisms have not been comprehensively investigated. Here, we examined the impact of idebenone treatment on AD pathology in 5xFAD mice, a model of AD. Idebenone significantly downregulated Aβ plaque number via multi-directional pathways in this model. Specifically, idebenone reduced the RAGE/caspase-3 signaling pathway and increased levels of the Aβ degradation enzyme NEP and α-secretase ADAM17 in 5xFAD mice. Importantly, idebenone significantly suppressed tau kinase p-GSK3βY216 levels, thereby inhibiting tau hyperphosphorylation at Thr231 and total tau levels in 5xFAD mice. Taken together, the present study indicates that idebenone modulates amyloidopathy and tauopathy in 5xFAD mice, suggesting therapeutic potential for AD.
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22

Liguori, Claudio, Matteo Spanetta, Michele Romoli, Fabio Placidi, Elena Nardi Cesarini, Nicola Biagio Mercuri, and Cinzia Costa. "Sleep disorders and late-onset epilepsy of unknown origin: Understanding new trajectories to brain amyloidopathy." Mechanisms of Ageing and Development 194 (March 2021): 111434. http://dx.doi.org/10.1016/j.mad.2021.111434.

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23

Kang, Jiseung, Mincheol Park, Eunkyung Lee, Jieun Jung, and Tae Kim. "The Role of Vitamin D in Alzheimer’s Disease: A Transcriptional Regulator of Amyloidopathy and Gliopathy." Biomedicines 10, no. 8 (July 28, 2022): 1824. http://dx.doi.org/10.3390/biomedicines10081824.

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Alzheimer’s disease (AD) is characterized by amyloid-beta (Aβ) accumulation and cognitive mental decline. Epidemiological studies have suggested an association between low serum vitamin D levels and an increased risk of AD. Vitamin D regulates gene expression via the vitamin D receptor, a nuclear ligand-dependent transcription factor. However, the molecular mechanism underlying the pathogenic and therapeutic effects of vitamin D on AD is not fully understood yet. To better understand how vitamin D regulates the expression of genes related to AD pathology, first, we induced vitamin D deficiency in 5xFAD mice by providing a vitamin-D-deficient diet and observed the changes in the mRNA level of genes related to Aβ processing, which resulted in an increase in the Aβ load in the brain. The vitamin D-deficient diet also suppressed the expression of genes for microglial Aβ phagocytosis. Interestingly, vitamin D deficiency in the early stage of AD resulted in earlier memory impairment. In addition, we administered vitamin D intraperitoneally to 5xFAD mice with a normal diet and found lower Aβ levels with the suppressed expression of genes for Aβ generation and observed improved memory function, which may be potentially associated with reduced MAO-B expression. These findings strongly suggest the role of vitamin D as a crucial disease-modifying factor that may modulate the amyloid pathology with regard to reducing AD symptoms.
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24

More, Swati S., and Robert Vince. "Hyperspectral Imaging Signatures Detect Amyloidopathy in Alzheimer’s Mouse Retina Well before Onset of Cognitive Decline." ACS Chemical Neuroscience 6, no. 2 (November 26, 2014): 306–15. http://dx.doi.org/10.1021/cn500242z.

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25

Garrido, Maria Garcia, Thomas Ridler, John Terry, and Jonathan T. Brown. "P2-243: IMPAIRMENTS IN NEURAL CORRELATES OF CONTEXTUAL MEMORY IN A MOUSE MODEL OF AMYLOIDOPATHY." Alzheimer's & Dementia 15 (July 2019): P676. http://dx.doi.org/10.1016/j.jalz.2019.06.2650.

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26

Haghi, Mehrnaz, Raheleh Masoudi, and Seyed Morteza Najibi. "Distinctive alteration in the expression of autophagy genes in Drosophila models of amyloidopathy and tauopathy." Upsala Journal of Medical Sciences 125, no. 4 (July 11, 2020): 265–73. http://dx.doi.org/10.1080/03009734.2020.1785063.

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27

Gholami Pourbadie, Hamid, Nima Naderi, Mahyar Janahmadi, Nasrin Mehranfard, and Fereshteh Motamedi. "Calcium channel blockade attenuates abnormal synaptic transmission in the dentate gyrus elicited by entorhinal amyloidopathy." Synapse 70, no. 10 (July 7, 2016): 408–17. http://dx.doi.org/10.1002/syn.21915.

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28

Jackson, Johanna, Francesco Tamagnini, James Johnson, Terri-Leigh Stephen, Zeshan Ahmed, Alice Oliver-Evans, Soraya Meftah, et al. "[P3-178]: IN VIVO TWO-PHOTON IMAGING OF THE EFFECTS OF TAUOPATHY AND AMYLOIDOPATHY ON SYNAPSES." Alzheimer's & Dementia 13, no. 7S_Part_21 (July 2017): P1002. http://dx.doi.org/10.1016/j.jalz.2017.06.1390.

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29

Sharma, Chanchal, and Sang Ryong Kim. "Linking Oxidative Stress and Proteinopathy in Alzheimer’s Disease." Antioxidants 10, no. 8 (July 30, 2021): 1231. http://dx.doi.org/10.3390/antiox10081231.

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Proteinopathy and excessive production of reactive oxygen species (ROS), which are the principal features observed in the Alzheimer’s disease (AD) brain, contribute to neuronal toxicity. β-amyloid and tau are the primary proteins responsible for the proteinopathy (amyloidopathy and tauopathy, respectively) in AD, which depends on ROS production; these aggregates can also generate ROS. These mechanisms work in concert and reinforce each other to drive the pathology observed in the aging brain, which primarily involves oxidative stress (OS). This, in turn, triggers neurodegeneration due to the subsequent loss of synapses and neurons. Understanding these interactions may thus aid in the identification of potential neuroprotective therapies that could be clinically useful. Here, we review the role of β-amyloid and tau in the activation of ROS production. We then further discuss how free radicals can influence structural changes in key toxic intermediates and describe the putative mechanisms by which OS and oligomers cause neuronal death.
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Candelise, Niccolò, Matthias Schmitz, Susana Margarida Da Silva Correia, Amandeep Singh Arora, Anna Villar-Piqué, Saima Zafar, Franc Llorens, Maria Cramm, and Inga Zerr. "Applications of the real-time quaking-induced conversion assay in diagnosis, prion strain-typing, drug pre-screening and other amyloidopathies." Expert Review of Molecular Diagnostics 17, no. 10 (September 8, 2017): 897–904. http://dx.doi.org/10.1080/14737159.2017.1368389.

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31

Sil, Susmita, Seema Singh, Divya T. Chemparathy, Ernest T. Chivero, Lila Gordon, and Shilpa Buch. "Astrocytes & Astrocyte derived Extracellular Vesicles in Morphine Induced Amyloidopathy: Implications for Cognitive Deficits in Opiate Abusers." Aging and disease 12, no. 6 (2021): 1389. http://dx.doi.org/10.14336/ad.2021.0406.

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32

Tamagnini, Francesco, Jon T. Brown, and Andrew D. Randall. "P3-040: ALTERED INTRINSIC PROPERTIES OF HIPPOCAMPAL PUTATIVE O-LM INTERNEURONES IN TRANSGENIC MOUSE MODELS OF AMYLOIDOPATHY." Alzheimer's & Dementia 10 (July 2014): P643. http://dx.doi.org/10.1016/j.jalz.2014.05.1127.

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33

Rojo, Ana I., Marta Pajares, Angel J. García-Yagüe, Izaskun Buendia, Fred Van Leuven, Masayuki Yamamoto, Manuela G. López, and Antonio Cuadrado. "Deficiency in the transcription factor NRF2 worsens inflammatory parameters in a mouse model with combined tauopathy and amyloidopathy." Redox Biology 18 (September 2018): 173–80. http://dx.doi.org/10.1016/j.redox.2018.07.006.

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Lee, Suji, Hyun-Ghang Jeong, and Hyun Chul Youn. "[P4-216]: COMPARISON OF GRAY MATTER VOLUME AND FRACTIONAL ANISOTROPY IN MILD COGNITIVE IMPAIRMENT PATIENTS WITH AND WITHOUT AMYLOIDOPATHY." Alzheimer's & Dementia 13, no. 7S_Part_28 (July 2017): P1350. http://dx.doi.org/10.1016/j.jalz.2017.06.2084.

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Youn, HyunChul, Eun Seong Lee, Suji Lee, Sangil Suh, Hyun-Ghang Jeong, and Jae Seon Eo. "Regional glucose metabolism due to the presence of cerebral amyloidopathy in older adults with depression and mild cognitive impairment." Journal of Affective Disorders 239 (October 2018): 30–36. http://dx.doi.org/10.1016/j.jad.2018.06.029.

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36

Wu, Aston J., Benjamin C. K. Tong, Alexis S. Huang, Min Li, and King-Ho Cheung. "Mitochondrial Calcium Signaling as a Therapeutic Target for Alzheimer’s Disease." Current Alzheimer Research 17, no. 4 (June 29, 2020): 329–43. http://dx.doi.org/10.2174/1567205016666191210091302.

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Mitochondria absorb calcium (Ca2+) at the expense of the electrochemical gradient generated during respiration. The influx of Ca2+ into the mitochondrial matrix helps maintain metabolic function and results in increased cytosolic Ca2+ during intracellular Ca2+ signaling. Mitochondrial Ca2+ homeostasis is tightly regulated by proteins located in the inner and outer mitochondrial membranes and by the cross-talk with endoplasmic reticulum Ca2+ signals. Increasing evidence indicates that mitochondrial Ca2+ overload is a pathological phenotype associated with Alzheimer’s Disease (AD). As intracellular Ca2+ dysregulation can be observed before the appearance of typical pathological hallmarks of AD, it is believed that mitochondrial Ca2+ overload may also play an important role in AD etiology. The high mitochondrial Ca2+ uptake can easily compromise neuronal functions and exacerbate AD progression by impairing mitochondrial respiration, increasing reactive oxygen species formation and inducing apoptosis. Additionally, mitochondrial Ca2+ overload can damage mitochondrial recycling via mitophagy. This review will discuss the molecular players involved in mitochondrial Ca2+ dysregulation and the pharmacotherapies that target this dysregulation. As most of the current AD therapeutics are based on amyloidopathy, tauopathy, and the cholinergic hypothesis, they achieve only symptomatic relief. Thus, determining how to reestablish mitochondrial Ca2+ homeostasis may aid in the development of novel AD therapeutic interventions.
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Ermilov, Victor Vladimirovich. "P4-100: The Role of B-Amyloidopathy in The Pathogenesis of Age-Related Macular Degeneration in Correlation with Alzheimer’s Disease." Alzheimer's & Dementia 12 (July 2016): P1050. http://dx.doi.org/10.1016/j.jalz.2016.06.2174.

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38

Lukiw, Walter J. "Recent Advances in Our Molecular and Mechanistic Understanding of Misfolded Cellular Proteins in Alzheimer’s Disease (AD) and Prion Disease (PrD)." Biomolecules 12, no. 2 (January 20, 2022): 166. http://dx.doi.org/10.3390/biom12020166.

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Naturally occurring neuron-abundant proteins including amyloid Aβ42 peptide and the microtubule-associated protein tau (MAPT) can, over time and under pathological situations, assume atypical conformations, altering their normal biological structure and function, and causing them to aggregate into insoluble and neurotoxic intracellular inclusions. These misfolded proteins ultimately contribute to the pathogenesis of several progressive, age-related and ultimately lethal human neurodegenerative disorders. The molecular mechanism of this pathological phenomenon of neuronal protein misfolding lends support to the ‘prion hypothesis’, which predicts that the aberrant folding of endogenous natural protein structures into unusual pathogenic isoforms can induce the atypical folding of other similar brain-abundant proteins, underscoring the age-related, progressive nature and potential transmissible and spreading capabilities of the aberrant protein isoforms that drive these invariably fatal neurological syndromes. The abnormal folding and aggregation of host proteins is a consistent feature of both amyloidopathies and tauopathies that encompass a continuous spectrum of brain diseases that include Alzheimer’s disease (AD), prion disorders (PrD) such as scrapie in sheep and goats (Bovidae), experimental prion infection of rodents (Muridae), Creutzfeldt–Jakob disease (CJD) and Gerstmann–Sträussler–Scheinker syndrome (GSS) in humans (Hominidae), and other fatal prion-driven neurological disorders. Because AD patients accumulate both misfolded tau and Aβ peptides, AD may be somewhat unique as the first example of a ‘double prion disorder’. This commentary will examine current research trends in this fascinating research area, with a special emphasis on AD and PrD, and the novel pathological misfolded protein processes common to both intractable neurological disorders.
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39

Pourbadie, Hamid Gholami, Nima Naderi, Hadi Mirzapour Delavar, Mahshid Hosseinzadeh, Nasrin Mehranfard, Fariba Khodagholi, Mahyar Janahmadi, and Fereshteh Motamedi. "Decrease of high voltage Ca2+ currents in the dentate gyrus granule cells by entorhinal amyloidopathy is reversed by calcium channel blockade." European Journal of Pharmacology 794 (January 2017): 154–61. http://dx.doi.org/10.1016/j.ejphar.2016.11.032.

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40

Pan, Allen L., Mickael Audrain, Emmy Sakakibara, Rajeev Joshi, Xiaodong Zhu, Qian Wang, Minghui Wang, et al. "Dual-Specificity Protein Phosphatase 4 (DUSP4) Overexpression Improves Learning Behavior Selectively in Female 5xFAD Mice, and Reduces β-Amyloid Load in Males and Females." Cells 11, no. 23 (December 1, 2022): 3880. http://dx.doi.org/10.3390/cells11233880.

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Recent multiscale network analyses of banked brains from subjects who died of late-onset sporadic Alzheimer’s disease converged on VGF (non-acronymic) as a key hub or driver. Within this computational VGF network, we identified the dual-specificity protein phosphatase 4 (DUSP4) [also known as mitogen-activated protein kinase (MAPK) phosphatase 2] as an important node. Importantly, DUSP4 gene expression, like that of VGF, is downregulated in postmortem Alzheimer’s disease (AD) brains. We investigated the roles that this VGF/DUSP4 network plays in the development of learning behavior impairment and neuropathology in the 5xFAD amyloidopathy mouse model. We found reductions in DUSP4 expression in the hippocampi of male AD subjects, correlating with increased CDR scores, and in 4-month-old female and 12–18-month-old male 5xFAD hippocampi. Adeno-associated virus (AAV5)-mediated overexpression of DUSP4 in 5xFAD mouse dorsal hippocampi (dHc) rescued impaired Barnes maze performance in females but not in males, while amyloid loads were reduced in both females and males. Bulk RNA sequencing of the dHc from 5-month-old mice overexpressing DUSP4, and Ingenuity Pathway and Enrichr analyses of differentially expressed genes (DEGs), revealed that DUSP4 reduced gene expression in female 5xFAD mice in neuroinflammatory, interferon-gamma (IFNγ), programmed cell death protein-ligand 1/programmed cell death protein 1 (PD-L1/PD-1), and extracellular signal-regulated kinase (ERK)/MAPK pathways, via which DUSP4 may modulate AD phenotype with gender-specificity.
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41

Riordan, Ruben. "Brain Cellular Senescence in Mouse Models of Alzheimer's Disease." Innovation in Aging 5, Supplement_1 (December 1, 2021): 929. http://dx.doi.org/10.1093/geroni/igab046.3363.

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Abstract Abstract The accumulation of senescent cells contributes to aging pathologies, including neurodegenerative diseases, and its selective removal improves physiological and cognitive function in wild type mice as well as in Alzheimer’s disease (AD) models. AD models recapitulate some, but not all components of disease and do so at different rates. Whether brain cellular senescence is recapitulated in some or all AD models, and whether the emergence of cellular senescence in AD mouse models occurs before or after the expected onset of AD-like cognitive deficits in these models is not yet known. The goal of this study was to identify mouse models of AD and AD-related dementias that develop measurable markers of cellular senescence in brain and thus may be useful to study the role of cellular senescence in these conditions. We measured levels of cellular senescence markers in brains of P301S(PS19), P301L, hTau, and 3xTg-AD mice that model amyloidopathy and/or tauopathy in AD and related dementias, and in wild type, age-matched control mice for each strain. Expression of cellular senescence markers in brains of transgenic P301L and 3xTg-AD mice was largely indistinguishable from that in WT control age-matched mice. In contrast, markers of cellular senescence were significantly increased in brains of transgenic P301S and hTau mice as compared to WT control mice at the expected time of onset of AD-like cognitive deficits. Taken together, our data suggest that P301S(PS19) and hTau mice may be useful for the study of brain cellular senescence in tauopathies including, but not limited to, AD.
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42

Majdi, Alireza, Saeed Sadigh-Eteghad, Sepideh Rahigh Aghsan, Fereshteh Farajdokht, Seyed Mehdi Vatandoust, Ali Namvaran, and Javad Mahmoudi. "Amyloid-β, tau, and the cholinergic system in Alzheimer’s disease: seeking direction in a tangle of clues." Reviews in the Neurosciences 31, no. 4 (May 26, 2020): 391–413. http://dx.doi.org/10.1515/revneuro-2019-0089.

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AbstractThe link between histopathological hallmarks of Alzheimer’s disease (AD), i.e. amyloid plaques, and neurofibrillary tangles, and AD-associated cognitive impairment, has long been established. However, the introduction of interactions between amyloid-beta (Aβ) as well as hyperphosphorylated tau, and the cholinergic system to the territory of descriptive neuropathology has drastically changed this field by adding the theory of synaptic neurotransmission to the toxic pas de deux in AD. Accumulating data show that a multitarget approach involving all amyloid, tau, and cholinergic hypotheses could better explain the evolution of events happening in AD. Various species of both Aβ and tau could be traced in cholinergic neurons of the basal forebrain system early in the course of the disease. These molecules induce degeneration in the neurons of this system. Reciprocally, aberrant cholinergic system modulation promotes changes in amyloid precursor protein (APP) metabolism and tau phosphorylation, resulting in neurotoxicity, neuroinflammation, and neuronal death. Altogether, these changes may better correlate with the clinical findings and cognitive impairment detected in AD patients. Failure of several of Aβ- and tau-related therapies further highlights the need for special attention to molecules that target all of these mentioned pathologic changes. Another noteworthy fact here is that none of the popular hypotheses of AD such as amyloidopathy or tauopathy seem to be responsible for the changes observed in AD alone. Thus, the main culprit should be sought higher in the stream somewhere in APP metabolism or Wnt signaling in the cholinergic system of the basal forebrain. Future studies should target these pathological events.
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43

Sánchez‐Rodríguez, Irene, Souhail Djebari, Sara Temprano‐Carazo, David Vega‐Avelaira, Raquel Jiménez‐Herrera, Guillermo Iborra‐Lázaro, Javier Yajeya, Lydia Jiménez‐Díaz, and Juan D. Navarro‐López. "Hippocampal long‐term synaptic depression and memory deficits induced in early amyloidopathy are prevented by enhancing G‐protein‐gated inwardly rectifying potassium channel activity." Journal of Neurochemistry 153, no. 3 (January 30, 2020): 362–76. http://dx.doi.org/10.1111/jnc.14946.

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44

Jackson, Johanna, Francesco Tamagnini, James Johnson, Zeshan Ahmed, Alice Oliver-Evans, Soraya Meftah, Michael Hutton, et al. "P4-079: In Vivo Two-Photon Imaging of the Effects of Tauopathy and Amyloidopathy on Synapse Dynamics in the RTG4510 and J20 Transgenic Models, Respectively." Alzheimer's & Dementia 12 (July 2016): P1043. http://dx.doi.org/10.1016/j.jalz.2016.06.2168.

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45

Jackson, Johanna. "IC-P-032: In Vivo Two-Photon Imaging of The Effects of Tauopathy And Amyloidopathy on Synapse Dynamics in The Rtg4510 and J20 Transgenic Models Respectively." Alzheimer's & Dementia 12 (July 2016): P31. http://dx.doi.org/10.1016/j.jalz.2016.06.042.

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46

Chang, Ta Yuan, Catherine C. Y. Chang, Taylor C. Harned, Adrianna L. De La Torre, Junghoon Lee, Thao N. Huynh, and James G. Gow. "Blocking cholesterol storage to treat Alzheimer’s disease." Exploration of Neuroprotective Therapy 1, no. 3 (December 30, 2021): 173–84. http://dx.doi.org/10.37349/ent.2021.00014.

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Cholesterol serves as an essential lipid molecule in various membrane organelles of mammalian cells. The metabolites of cholesterol also play important functions. Acyl-coenzyme A: cholesterol acyltransferase 1 (ACAT1), also named as sterol O-acyltransferase 1, is a membrane-bound enzyme residing at the endoplasmic reticulum (ER). It converts cholesterol to cholesteryl esters (CEs) for storage, and is expressed in all cells. CEs cannot partition in membranes; they can only coalesce as cytosolic lipid droplets. Excess CEs are found in the vulnerable region of the brains of patients with late-onset Alzheimer’s disease (AD), and in cell and mouse models for AD. Reducing CE contents by genetic inactivation of ACAT1, or by pharmacological inhibition of ACAT is shown to reduce amyloidopathy and other hallmarks for AD. To account for the various beneficial actions of the ACAT1 blockade (A1B), a working hypothesis is proposed here: the increase in CE contents observed in the AD brain is caused by damages of cholesterol-rich lipid rafts that are known to occur in neurons affected by AD. These damages cause cholesterol to release from lipid rafts and move to the ER where it will be converted to CEs by ACAT1. In addition, the increase in CE contents may also be caused by overloading with cholesterol-rich substances, or through activation of ACAT1 gene expression by various pro-inflammatory agents. Both scenarios may occur in microglia of the chronically inflamed brain. A1B ameliorates AD by diverting the cholesterol pool destined for CE biosynthesis such that it can be utilized more efficiently to repair membrane damage in various organelles, and to exert regulatory actions more effectively to defend against AD. To test the validity of the A1B hypothesis in cell culture and in vivo, the current status of various anti-ACAT1 agents that could be further developed is briefly discussed.
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47

Gauthier, Kim, Alexandrine Morand, Frederic Dutheil, Béatrice Alescio-Lautier, José Boucraut, David Clarys, Francis Eustache, et al. "Ageing stereotypes and prodromal Alzheimer’s disease (AGING): study protocol for an ongoing randomised clinical study." BMJ Open 9, no. 10 (October 2019): e032265. http://dx.doi.org/10.1136/bmjopen-2019-032265.

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IntroductionThe number of older people diagnosed with amnestic mild cognitive impairment (aMCI), the prodromal state of Alzheimer's disease (AD), is increasing worldwide. However, some patients with aMCI never convert to the AD type of dementia, with some remaining stable and others reverting to normal. This overdiagnosis bias has been largely overlooked and gone unexplained. There is ample evidence in the laboratory that negative ageing stereotypes (eg, the culturally shared belief that ageing inescapably causes severe cognitive decline) contribute to the deteriorating cognitive performances of healthy older adults, leading them to perform below their true abilities. The study described here is intended to test for the first time whether such stereotypes also impair patients’ cognitive performances during neuropsychological examinations in memory clinics, resulting in overdiagnosis of aMCI.Methods and analysisThe ongoing study is a 4-year randomised clinical trial comparing patients’ physiological stress and cognitive performances during neuropsychological testing in memory clinics. A total of 260 patients attending their first cognitive evaluation will be randomised to either a standard condition of test administration, assumed here to implicitly activate negative ageing stereotypes or a reduced-threat instruction condition designed to alleviate the anxiety arising from these stereotypes. Both groups will be tested with the same test battery and stress biomarkers. For 30 patients diagnosed with aMCI in each group (n=60), biomarkers of neurodegeneration and amyloidopathy will be used to distinguish between aMCI with normal versus abnormal AD biomarkers. A 9-month follow-up will be performed on all patients to identify those whose cognitive performances remain stable, deteriorate or improve.Ethics and disseminationThis protocol has been approved by the French National Agency for Medicines and Health Products Safety and the Sud-Est I French Ethics Committee (2017-A00946-47). Results will be published in peer-reviewed journals.Trial registration numberNCT03138018.
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48

Rosu, Gabriela-Camelia, Bogdan Catalin, Tudor Adrian Balseanu, Mogoanta Laurentiu, Margaritescu Claudiu, Samir Kumar-Singh, and Pirici Daniel. "Inhibition of Aquaporin 4 Decreases Amyloid Aβ40 Drainage Around Cerebral Vessels." Molecular Neurobiology 57, no. 11 (August 11, 2020): 4720–34. http://dx.doi.org/10.1007/s12035-020-02044-8.

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Abstract Aquaporin-4 (AQP4) is located mainly in the astrocytic end-feet around cerebral blood vessels and regulates ion and water homeostasis in the brain. While deletion of AQP4 is shown to reduce amyloid-β (Aβ) clearance and exacerbate Aβ peptide accumulation in plaques and vessels of Alzheimer’s disease mouse models, the mechanism and clearing pathways involved are debated. Here, we investigated how inhibiting the function of AQP4 in healthy male C57BL/6 J mice impacts clearance of Aβ40, the more soluble Aβ isoform. Using two-photon in vivo imaging and visualizing vessels with Sulfurodamine 101 (SR101), we first showed that Aβ40 injected as a ≤ 0.5-μl volume in the cerebral cortex diffused rapidly in parenchyma and accumulated around blood vessels. In animals treated with the AQP4 inhibitor TGN-020, the perivascular Aβ40 accumulation was significantly (P < 0.001) intensified by involving four times more vessels, thus suggesting a generalized clearance defect associated with vessels. Increasing the injecting volume to ≥ 0.5 ≤ 1 μl decreased the difference of Aβ40-positive vessels observed in non-treated and AQP4 inhibitor-treated animals, although the difference was still significant (P = 0.001), suggesting that larger injection volumes could overwhelm intramural vascular clearance mechanisms. While both small and large vessels accumulated Aβ40, for the ≤ 0.5-μl volume group, the average diameter of the Aβ40-positive vessels tended to be larger in control animals compared with TGN-020-treated animals, although the difference was non-significant (P = 0.066). Using histopathology and ultrastructural microscopy, no vascular structural change was observed after a single massive dose of TGN-020. These data suggest that AQP4 deficiency is directly involved in impaired Aβ brain clearance via the peri-/para-vascular routes, and AQP4-mediated vascular clearance might counteract blood-brain barrier abnormalities and age-related vascular amyloidopathy.
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49

Abd El-Fatah, Israa M., Heba M. A. Abdelrazek, Sherehan M. Ibrahim, Dalaal M. Abdallah, and Hanan S. El-Abhar. "Dimethyl fumarate abridged tauo-/amyloidopathy in a D-Galactose/ovariectomy-induced Alzheimer's-like disease: Modulation of AMPK/SIRT-1, AKT/CREB/BDNF, AKT/GSK-3β, adiponectin/Adipo1R, and NF-κB/IL-1β/ROS trajectories." Neurochemistry International 148 (September 2021): 105082. http://dx.doi.org/10.1016/j.neuint.2021.105082.

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50

Vitale, Paola, Ana Rita Salgueiro-Pereira, Carmen Alina Lupascu, Michael Willem, Rosanna Migliore, Michele Migliore, and Hélène Marie. "Analysis of Age-Dependent Alterations in Excitability Properties of CA1 Pyramidal Neurons in an APPPS1 Model of Alzheimer’s Disease." Frontiers in Aging Neuroscience 13 (June 11, 2021). http://dx.doi.org/10.3389/fnagi.2021.668948.

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Age-dependent accumulation of amyloid-β, provoking increasing brain amyloidopathy, triggers abnormal patterns of neuron activity and circuit synchronization in Alzheimer’s disease (AD) as observed in human AD patients and AD mouse models. Recent studies on AD mouse models, mimicking this age-dependent amyloidopathy, identified alterations in CA1 neuron excitability. However, these models generally also overexpress mutated amyloid precursor protein (APP) and presenilin 1 (PS1) and there is a lack of a clear correlation of neuronal excitability alterations with progressive amyloidopathy. The active development of computational models of AD points out the need of collecting such experimental data to build a reliable disease model exhibiting AD-like disease progression. We therefore used the feature extraction tool of the Human Brain Project (HBP) Brain Simulation Platform to systematically analyze the excitability profile of CA1 pyramidal neuron in the APPPS1 mouse model. We identified specific features of neuron excitability that best correlate either with over-expression of mutated APP and PS1 or increasing Aβ amyloidopathy. Notably, we report strong alterations in membrane time constant and action potential width and weak alterations in firing behavior. Also, using a CA1 pyramidal neuron model, we evidence amyloidopathy-dependent alterations in Ih. Finally, cluster analysis of these recordings showed that we could reliably assign a trace to its correct group, opening the door to a more refined, less variable analysis of AD-affected neurons. This inter-disciplinary analysis, bringing together experimentalists and modelers, helps to further unravel the neuronal mechanisms most affected by AD and to build a biologically plausible computational model of the AD brain.
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