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Relevant bibliographies by topics / Amyloid beta deposition

Academic literature on the topic 'Amyloid beta deposition'

Author: Grafiati

Published: 10 December 2022

Last updated: 28 January 2023

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Journal articles on the topic "Amyloid beta deposition"

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Head, Elizabeth, and Ira T. Lott. "Down syndrome and beta-amyloid deposition." Current Opinion in Neurology 17, no. 2 (April 2004): 95–100. http://dx.doi.org/10.1097/00019052-200404000-00003.

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Vlassenko, Andrei, Tyler Blazey, Yi Su, Chengjie Xiong, Tammie Benzinger, and John Morris. "P2-204: Regional beta-amyloid deposition several years prior to beta-amyloid positivity." Alzheimer's & Dementia 9 (July 2013): P431—P432. http://dx.doi.org/10.1016/j.jalz.2013.05.850.

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Rodrigue, Karen M., Kristen M. Kennedy, and Denise C. Park. "Beta-Amyloid Deposition and the Aging Brain." Neuropsychology Review 19, no. 4 (November 12, 2009): 436–50. http://dx.doi.org/10.1007/s11065-009-9118-x.

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Stein, Thor D., Philip H. Montenigro, Victor E. Alvarez, Weiming Xia, John F. Crary, Yorghos Tripodis, Daniel H. Daneshvar, et al. "Beta-amyloid deposition in chronic traumatic encephalopathy." Acta Neuropathologica 130, no. 1 (May 6, 2015): 21–34. http://dx.doi.org/10.1007/s00401-015-1435-y.

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Shin, Soo Jung, Yuon Jeong, Seong Gak Jeon, Sujin Kim, Seong-kyung Lee, Hong Seok Choi, Cheong Su Im, et al. "Uncaria rhynchophylla ameliorates amyloid beta deposition and amyloid beta-mediated pathology in 5XFAD mice." Neurochemistry International 121 (December 2018): 114–24. http://dx.doi.org/10.1016/j.neuint.2018.10.003.

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Bubak, Andrew N., Christina N. Como, James E. Hassell, Teresa Mescher, Seth E. Frietze, Christy S. Niemeyer, Randall J. Cohrs, and Maria A. Nagel. "Targeted RNA Sequencing of VZV-Infected Brain Vascular Adventitial Fibroblasts Indicates That Amyloid May Be Involved in VZV Vasculopathy." Neurology - Neuroimmunology Neuroinflammation 9, no. 1 (November 10, 2021): e1103. http://dx.doi.org/10.1212/nxi.0000000000001103.

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Background and ObjectivesCompared with stroke controls, patients with varicella zoster virus (VZV) vasculopathy have increased amyloid in CSF, along with increased amylin (islet amyloid polypeptide [IAPP]) and anti-VZV antibodies. Thus, we examined the gene expression profiles of VZV-infected primary human brain vascular adventitial fibroblasts (HBVAFs), one of the initial arterial cells infected in VZV vasculopathy, to determine whether they are a potential source of amyloid that can disrupt vasculature and potentiate inflammation.MethodsMock- and VZV-infected quiescent HBVAFs were harvested at 3 days postinfection. Targeted RNA sequencing of the whole-human transcriptome (BioSpyder Technologies, TempO-Seq) was conducted followed by gene set enrichment and pathway analysis. Selected pathways unique to VZV-infected cells were confirmed by enzyme-linked immunoassays, migration assays, and immunofluorescence analysis (IFA) that included antibodies against amylin and amyloid-beta, as well as amyloid staining by Thioflavin-T.ResultsCompared with mock, VZV-infected HBVAFs had significantly enriched gene expression pathways involved in vascular remodeling and vascular diseases; confirmatory studies showed secretion of matrix metalloproteinase-3 and -10, as well increased migration of infected cells and uninfected cells when exposed to conditioned media from VZV-infected cells. In addition, significantly enriched pathways involved in amyloid-associated diseases (diabetes mellitus, amyloidosis, and Alzheimer disease), tauopathy, and progressive neurologic disorder were identified; predicted upstream regulators included amyloid precursor protein, apolipoprotein E, microtubule-associated protein tau, presenilin 1, and IAPP. Confirmatory IFA showed that VZV-infected HBVAFs contained amyloidogenic peptides (amyloid-beta and amylin) and intracellular amyloid.DiscussionGene expression profiles and pathway enrichment analysis of VZV-infected HBVAFs, as well as phenotypic studies, reveal features of pathologic vascular remodeling (e.g., increased cell migration and changes in the extracellular matrix) that can contribute to cerebrovascular disease. Furthermore, the discovery of amyloid-associated transcriptional pathways and intracellular amyloid deposition in HBVAFs raise the possibility that VZV vasculopathy is an amyloid disease. Amyloid deposition may contribute to cell death and loss of vascular wall integrity, as well as potentiate chronic inflammation in VZV vasculopathy, with disease severity and recurrence determined by the host's ability to clear virus infection and amyloid deposition and by the coexistence of other amyloid-associated diseases (i.e., Alzheimer disease and diabetes mellitus).

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Brancaccio, D., G. M. Ghiggeri, P. Braidotti, A. Garberi, M. Gallieni, V. Bellotti, U. Zoni, R. Gusmano, and G. Coggi. "Deposition of kappa and lambda light chains in amyloid filaments of dialysis-related amyloidosis." Journal of the American Society of Nephrology 6, no. 4 (October 1995): 1262–70. http://dx.doi.org/10.1681/asn.v641262.

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beta 2-Microglobulin (beta 2m) is considered to be the amyloidogenic precursor in dialysis-related amyloidosis, although the implication of other relevant cofactors in the pathogenesis of this disease has also been hypothesized. It is conceivable that substances found in amyloid deposits might represent something more than simple codeposition, possibly playing a pathogenic role in amyloidogenesis. Along these lines, a detailed analysis of the protein composition of amyloid fibrils purified from synovial material surgically obtained from nine patients on long-term dialysis was carried out. By the use of sodium dodecyl sulfate-polyacrylamide gel electrophoresis, several other protein components, in addition to beta 2m, were found. These were characterized by NH2 amino-terminal sequencing and immunoblotting. In fibrils obtained by water extraction, which fulfill the electron microscopy criteria of highly pure amyloid material, polyclonal kappa and lambda light chains were detected with a concentration of 15 micrograms/mL in the water extraction material; the beta 2m concentration was 200 micrograms/mL. Light microscopy immunohistochemistry was performed on samples from five patients. Amyloid deposits reacted with anti-beta 2m, and anti-light (kappa, lambda), chain antibodies. The immunoreaction of amyloid filaments to anti-beta 2m, anti-lambda, and anti-kappa light chain antibodies was also tested by electron microscopy by use of the immunogold staining procedure. Amyloid filaments were labeled by the three antibodies and showed a different intensity of immunostaining apparently related to their different aggregation pattern. These observations demonstrate that polyclonal immunoglobulin light chains (kappa and lambda) are not contaminants but, together with beta 2m, represent a major constituent of amyloid deposits in dialysis-related osteoarticular amyloidosis, thus indicating their possible role in amyloidogenesis.

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MOON, MARY ANN. "Alzheimer's Allele Related to Early Beta-Amyloid Deposition." Clinical Psychiatry News 34, no. 10 (October 2006): 31. http://dx.doi.org/10.1016/s0270-6644(06)71805-7.

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Costassa, E. V., G. Zanusso, F. Ingravalle, S. Peletto, M. N. Chieppa, M. Gallo, C. Palmitessa, et al. "Characterization of Beta Amyloid Deposition in Cattle Brain." Journal of Comparative Pathology 146, no. 1 (January 2012): 61. http://dx.doi.org/10.1016/j.jcpa.2011.11.063.

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Marano, Christopher, Clifford Workman, Christopher Lyman, Tova Narrow, Yun Zhou, Cynthia Munro, Robert Dannals, et al. "Cortical Beta-Amyloid Deposition in Late-Life Depression." American Journal of Geriatric Psychiatry 21, no. 3 (March 2013): S127. http://dx.doi.org/10.1016/j.jagp.2012.12.169.

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Dissertations / Theses on the topic "Amyloid beta deposition"

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Schrump, Stefanie. "Modifiers of Beta-Amyloid Metabolism and Deposition in Mouse Models of Alzheimer's Disease." Case Western Reserve University School of Graduate Studies / OhioLINK, 2011. http://rave.ohiolink.edu/etdc/view?acc_num=case1307654122.

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Elliott, Jennifer Jane. "Parkinson's disease : behavioural effects following extracellular deposition of non-beta amyloid component and pharmacological interventions." Thesis, University of Ulster, 2004. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.413864.

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Cairns, Nigel John. "Beta-amyloid protein deposition in the brain and its role in the pathogenesis of Alzheimer's disease." Thesis, King's College London (University of London), 1995. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.283135.

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Clayton, Kevin A. "Amyloid plaque deposition accelerates tau propagation via activation of microglia in a humanized app mouse model." Thesis, 2021. https://hdl.handle.net/2144/42695.

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Alzheimer’s disease is characterized by the formation of two major pathological hallmarks: amyloid plaques and neurofibrillary tangles. Although there have been many studies to understand the role of microglia in Alzheimer’s disease, it is not yet known how microglia can promote disease progression while actively phagocytosing amyloid plaques or phosphorylated tau (p-tau). Through stereotaxic injection of adeno-associated virus expressing mutant P301L tau (AAV-P301L-tau) into the medial entorhinal cortex (MEC) of both wild-type (WT) and APPNL-G-F mice, we demonstrate how amyloid plaques exacerbate p-tau propagation to the granule cell layer (GCL) of the hippocampus. However, in mice receiving the colony-stimulating factor 1 receptor inhibitor (PLX5622), ~95% of microglia were depleted, which dramatically reduced p-tau propagation to the GCL. Although microglia depletion curtailed p-tau propagation, it also led to reduced plaque compaction and an increase in overall amyloid-beta (Aβ) plaque presence. Additionally, we found microglia depletion resulted in greater p-tau aggregation in dystrophic neurites surrounding amyloid plaques. We investigated neurodegenerative microglia (MGnD), which are activated in response to amyloid plaques, for their propensity to release extracellular vesicles in comparison to homeostatic microglia. We discovered that MGnD, identified by Clec7a or Mac2 staining, strongly express Tumor susceptibility gene 101 (Tsg101), which is an ESCRT-1 protein and a marker for extracellular vesicles (EVs). To further investigate EV release and MGnD, a novel lentivirus expressing fluorescent mEmerald conjugated to CD9 (mE-CD9) was constructed and injected into the MEC of both WT and APPNL-G-F mice which allowed for visualization of mE-CD9+ puncta around individual microglia. CD9 is a tetraspanin and also a marker for EVs. We observed that the number of mEmerald+ particles surrounding MGnD was three-fold higher compared to non-diseased, homeostatic microglia. Sequential injection of mE-CD9 and AAV-P301L-tau into the MEC revealed that microglia-derived EVs encapsulate pathologic p-tau, which is augmented by the MGnD phenotype. Taken together, these data provide strong evidence that MGnD exhibit increased secretion of tau-containing EVs, providing a possible mechanism for how amyloid deposition indirectly exacerbates tau propagation.

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"Physicochemical studies on those neurochemical factors that promote beta-amyloid deposition in APP trangenic mouse and human Alzheimer-diseased brain." Tulane University, 1999.

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The present thesis focuses on deciphering the biochemical sequelae responsible for the precipitation of Alzheimer's disease (AD). The hallmark occurrence in AD is the assembly of Abeta (a normally soluble component of cerebrospinal fluid) into insoluble, extracellular plaques. The genetics of AD and recent observations of partial AD phenotype (i.e. Abeta plaque deposits) in transgenic mice overproducing Abeta indicate that Abeta amyloid deposition in the neocortex is intimately involved in the pathophysiology of the disorder. Hence, neurochemical candidates, which may impact the solubility of Abeta, were investigated. Recent studies conducted by our laboratory show that Abeta is a physiological metalloprotein, saturably binding zinc and copper. In fact, the interaction of Abeta with physiological concentrations of zinc, copper, and iron generate amyloid plaques in vitro, which can be resolubilized by the extraction of metal ions via chelation. Extending these findings, a vertically innovative approach was used to determine whether our in vitro findings are germane to AD pathology First, we investigated whether plaque deposited preferentially within cerebral regions enriched in zinc and copper. It was observed that brain regions targeted by AD (e.g. the hippocampal formation) experience drastic fluxes in metal ion concentrations, which may rise as much as 300muM in the case of zinc. In particular, it was noted that subdivisions of the inferior pulvinar that receive putative zinc-enriched projections from the primary visual cortex contain Abeta amyloid plaques. Interestingly, the region most affected in the thalamus is known to mediate visual attention which is compromised in AD Based on our above in vitro findings, the ability of metal chelators to resolubilize Abeta aggregates from the brains of transgenic mice overexpressing the human amyloid precursor protein (APP) and bearing cerebral amyloid was assessed. We noted that homogenization of APP transgenic mouse brains in the presence of metal chelators highly specific for zinc and copper significantly increased extractable Abeta (p < 0.01) as compared to homogenization in the presence of phosphate buffered saline alone. These findings suggest that the assembly of plaques in APP transgenic mouse brains appeared to parallel that in human, providing an exploitable model of AD amyloidosis Finally, United States Pharmacopeia (USP) drugs (i.e. clioquinol and triene), having zinc and copper chelating abilities, were administered daily to APP transgenic mice at 12 months of age. After 3 months of drug therapy, it was observed that animals receiving clioquinol, a chelator highly specific for zinc, were healthy and had more than a 50% reduction in Abeta load (p < 0.05) and a 60% decrease in sedimentable Abeta (p < 0.01). There was also a corresponding decrease (p < 0.05) in the progenitor pool of Abeta species, namely the APP beta-carboxyl terminal fragment concentration as measured by Western blot analysis. These findings suggest that chelation therapy may alter APP processing, thereby arresting Abeta production. Thus, metal chelators are one class of compounds that may be highly effective for the treatment of AD
acase@tulane.edu

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Book chapters on the topic "Amyloid beta deposition"

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Tashiro, M., N. Okamura, S. Watanuki, S. Furumoto, K. Furukawa, Y. Funaki, K. Shibuya, et al. "Quantitative Analysis of Amyloid Beta Deposition in the Brain of Alzheimer’s Disease Patients Using PET and [11C]BF-227 and [18F]FACT." In IFMBE Proceedings, 1648–51. Berlin, Heidelberg: Springer Berlin Heidelberg, 2010. http://dx.doi.org/10.1007/978-3-642-14515-5_419.

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Anand, Abhinav, Neha Sharma, Monica Gulati, and Navneet Khurana. "Amyloid Beta." In Research Anthology on Diagnosing and Treating Neurocognitive Disorders, 1–17. IGI Global, 2021. http://dx.doi.org/10.4018/978-1-7998-3441-0.ch001.

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Alzheimer's disease (AD), exhibiting accumulation of amyloid beta (Aβ) peptide as a foremost protagonist, is one of the top five causes of deaths. It is a neurodegenerative disorder (ND) that causes a progressive decline in memory and cognitive abilities. It is characterized by deposition of Aβ plaques and neurofibrillary tangles (NFTs) in the neurons, which in turn causes a decline in the brain acetylcholine levels. Aβ hypothesis is the most accepted hypothesis pertaining to the pathogenesis of AD. Amyloid Precursor Protein (APP) is constitutively present in brain and it is cleaved by three proteolytic enzymes (i.e., alpha, beta, and gamma secretases). Beta and gamma secretases cleave APP to form Aβ. Ubiquitin Proteasome System (UPS) is involved in the clearing of Aβ plaques. AD also involves impairment in UPS. The novel disease-modifying approaches involve inhibition of beta and gamma secretases. A number of clinical trials are going on worldwide with moieties targeting beta and gamma secretases. This chapter deals with an overview of APP and its enzymatic cleavage leading to AD.

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Anand, Abhinav, Neha Sharma, Monica Gulati, and Navneet Khurana. "Amyloid Beta." In Advances in Medical Diagnosis, Treatment, and Care, 235–51. IGI Global, 2019. http://dx.doi.org/10.4018/978-1-5225-5282-6.ch011.

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Alzheimer's disease (AD), exhibiting accumulation of amyloid beta (Aβ) peptide as a foremost protagonist, is one of the top five causes of deaths. It is a neurodegenerative disorder (ND) that causes a progressive decline in memory and cognitive abilities. It is characterized by deposition of Aβ plaques and neurofibrillary tangles (NFTs) in the neurons, which in turn causes a decline in the brain acetylcholine levels. Aβ hypothesis is the most accepted hypothesis pertaining to the pathogenesis of AD. Amyloid Precursor Protein (APP) is constitutively present in brain and it is cleaved by three proteolytic enzymes (i.e., alpha, beta, and gamma secretases). Beta and gamma secretases cleave APP to form Aβ. Ubiquitin Proteasome System (UPS) is involved in the clearing of Aβ plaques. AD also involves impairment in UPS. The novel disease-modifying approaches involve inhibition of beta and gamma secretases. A number of clinical trials are going on worldwide with moieties targeting beta and gamma secretases. This chapter deals with an overview of APP and its enzymatic cleavage leading to AD.

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Manley, Geoffrey T., John K. Yue, Hansen Deng, Ethan A. Winkler, John F. Burke, and Catherine Suen. "Pathophysiology of traumatic brain injury." In Oxford Textbook of Neurological Surgery, edited by Ramez W. Kirollos, Adel Helmy, Simon Thomson, and Peter J. A. Hutchinson, 483–96. Oxford University Press, 2019. http://dx.doi.org/10.1093/med/9780198746706.003.0041.

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This chapter provides summative information on the biomechanics, classification, and metabolism of traumatic brain injury (TBI). Impact, impulse, static/quasistatic loading, and related biomechanical sequelae following rotational shear and strain are discussed. Morphological classifications across extradural, acute/chronic subdural, subarachnoid, and intraventricular haemorrhages, as well as cerebral contusions and axonal injuries, are characterized and correlated with injury severity. Management options and implications for penetrating TBI and mild TBI/concussion are described. Cerebral metabolism including pressure/viscosity, CO₂ reactivity, and autoregulation are explained in detail to provide for in-depth exploration of a spectrum of secondary injury cascades, encompassing glutamatergic excitotoxicity, autoregulatory loss, and the pressure reactivity index, flow disturbances, elevated intracranial pressure, cortical spreading depression and seizures/epilepsy. Beta-amyloid deposition in response to TBI, and genetic susceptibilities to poor recovery are covered. Current developments to standardize TBI classification systems, establish evidentiary benchmarks for quality of care, and accelerate advances in diagnosis and prognosis are highlighted.

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