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Amyloid oligomers

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https://www.readbyqxmd.com/read/29156571/studies-for-improving-a-rat-model-of-alzheimer-s-disease-icv-administration-of-well-characterized-%C3%AE-amyloid-1-42-oligomers-induce-dysfunction-in-spatial-memory
#1
Ágnes Kasza, Botond Penke, Zsuzsanna Frank, Zsolt Bozsó, Viktor Szegedi, Ákos Hunya, Klaudia Németh, Gábor Kozma, Lívia Fülöp
During the past 15 years, several genetically altered mouse models of human Alzheimer's disease (AD) have been developed. These costly models have greatly facilitated the evaluation of novel therapeutic approaches. Injecting synthetic β-amyloid (Aβ) 1-42 species into different parts of the brain of non-transgenic rodents frequently provided unreliable results, owing to a lack of a genuine characterization of the administered Aβ aggregates. Previously, we have published a new rat AD-model in which protofibrillar-fibrillar Aβ1-42 was administered into rat entorhinal cortex (Sipos 2007)...
November 18, 2017: Molecules: a Journal of Synthetic Chemistry and Natural Product Chemistry
https://www.readbyqxmd.com/read/29155887/effects-of-an-a%C3%AE-antibody-fragment-on-a%C3%AE-aggregation-and-astrocytic-uptake-are-modulated-by-apolipoprotein-e-and-j-mimetic-peptides
#2
Laia Montoliu-Gaya, Sandra D Mulder, Robert Veerhuis, Sandra Villegas
Aβ-Immunotherapy has long been studied in the treatment of Alzheimer's disease (AD), but not how other molecules involved in the disease can affect antibody performance. We previously designed an antibody fragment, scFv-h3D6, and showed that it precludes Aβ-induced cytotoxicity by withdrawing Aβ oligomers from the amyloid pathway towards a non-toxic, worm-like pathway. ScFv-h3D6 was effective at the behavioral, cellular, and molecular levels in the 3xTg-AD mouse model. Because scFv-h3D6 treatment restored apolipoprotein E (apoE) and J (apoJ) concentrations to non-pathological values, and Aβ internalization by glial cells was found to be decreased in the presence of these apolipoproteins, we now aimed to test the influence of scFv-h3D6 on Aβ aggregation and cellular uptake by primary human astrocytes in the presence of therapeutic apoE and apoJ mimetic peptides (MPs)...
2017: PloS One
https://www.readbyqxmd.com/read/29148557/structural-and-thermodynamical-properties-of-early-human-amylin-oligomers-using-replica-exchange-molecular-dynamics-mutation-effect-of-three-key-residues-f15-h18-and-f23
#3
S Bouzakraoui, N Mousseau
Human islet amyloid polypeptide (hIAPP) is a 37-residue polypeptide, considered to be the main component of the pancreatic islet amyloid associated with type 2 diabetes and is one of the most amyloidogenic polypeptides known. Although the structure of hIAPP fibrils has already been obtained, structures of early oligomers and the mechanism of β-sheet formation remain poorly understood. Herein, we characterize the atomic structure and the thermodynamics of the 14-37 residue fragment of hIAPP wild-type and mutated dimers and trimers...
November 17, 2017: Physical Chemistry Chemical Physics: PCCP
https://www.readbyqxmd.com/read/29145032/intravenous-immunoglobulin-improves-glucose-control-and-%C3%AE-cell-function-in-human-iapp-transgenic-mice-by-attenuating-islet-inflammation-and-reducing-iapp-oligomers
#4
Yue Zhang, Xiao-Lin Yu, Jie Zhu, Shu-Ying Liu, Xiang-Meng Liu, Quan-Xiu Dong, Jia-Qian Chai, Rui-Tian Liu
Type 2 diabetes mellitus (T2DM) is a metabolic disorder characterized by β-cell loss, insulin resistance, islet inflammation and amyloid deposits derived from islet amyloid polypeptide (IAPP). Reducing toxic IAPP oligomers and inhibiting islet inflammation may provide therapeutic benefit in treating T2DM. Intravenous immunoglobulin (IVIg) is an efficient anti-inflammatory and immunomodulatory agent for the treatment of several autoimmune or inflammatory neurological diseases. However, whether IVIg has therapeutic potential on T2DM remains unclear...
November 13, 2017: International Immunopharmacology
https://www.readbyqxmd.com/read/29143447/investigation-of-the-interactions-between-aptamer-and-misfolded-proteins-from-monomer-and-oligomer-to-fibril-by-single-molecule-force-spectroscopy
#5
Yan Zheng, Qing Wang, Xiaohai Yang, Zhiping Li, Lei Gao, Hua Zhang, Wenyan Nie, Xiuhua Geng, Kemin Wang
Increasing knowledge on the understanding interactions of aptamer with misfolded proteins (including monomer, oligomer, and amyloid fibril) is crucial for development of aggregation inhibitors and diagnosis of amyloid diseases. Herein, the interactions of lysozyme monomer-, oligomer-, and amyloid fibril-aptamer were investigated using single-molecule force spectroscopy. The results revealed that the aptamer screened against lysozyme monomer could also bind to oligomer and amyloid fibril, in spite of the recognition at a lower binding probability...
November 16, 2017: Journal of Molecular Recognition: JMR
https://www.readbyqxmd.com/read/29142509/using-an-nmr-metabolomics-approach-to-investigate-the-pathogenicity-of-amyloid-beta-and-alpha-synuclein
#6
M M Phelan, E Caamaño-Gutiérrez, M S Gant, R X Grosman, J Madine
Introduction: The pathogenicity at differing points along the aggregation pathway of many fibril-forming proteins associated with neurodegenerative diseases is unclear. Understanding the effect of different aggregation states of these proteins on cellular processes is essential to enhance understanding of diseases and provide future options for diagnosis and therapeutic intervention. Objectives: To establish a robust method to probe the metabolic changes of neuronal cells and use it to monitor cellular response to challenge with three amyloidogenic proteins associated with neurodegenerative diseases in different aggregation states...
2017: Metabolomics: Official Journal of the Metabolomic Society
https://www.readbyqxmd.com/read/29138762/identifying-cu-ii-amyloid-peptide-binding-intermediates-in-the-early-stages-of-aggregation-by-resonance-raman-spectroscopy-a-simulation-study
#7
Hao Ren, Yu Zhang, Sibei Guo, Na Lin, Li Deng, Tongtao Yue, Fang Huang
The aggregation of amyloid beta (Aβ) peptides plays a crucial role in the pathology and etiology of Alzheimer's disease. Experimental evidence shows that copper ion is an aggregation-prone species with the ability to coordinately bind to Aβ and further induce the formation of neurotoxic Aβ oligomers. However, the detailed structures of Cu(ii)-Aβ complexes have not been illustrated, and the kinetics and dynamics of the Cu(ii) binding are not well understood. Two Cu(ii)-Aβ complexes have been proposed to exist under physiological conditions, and another two might exist at higher pH values...
November 15, 2017: Physical Chemistry Chemical Physics: PCCP
https://www.readbyqxmd.com/read/29137651/abnormal-dendritic-calcium-activity-and-synaptic-depotentiation-occur-early-in-a-mouse-model-of-alzheimer-s-disease
#8
Yang Bai, Miao Li, Yanmei Zhou, Lei Ma, Qian Qiao, Wanling Hu, Wei Li, Zachary Patrick Wills, Wen-Biao Gan
BACKGROUND: Alzheimer's disease (AD) is characterized by amyloid deposition, tangle formation as well as synapse loss. Synaptic abnormalities occur early in the pathogenesis of AD. Identifying early synaptic abnormalities and their underlying mechanisms is likely important for the prevention and treatment of AD. METHODS: We performed in vivo two-photon calcium imaging to examine the activities of somas, dendrites and dendritic spines of layer 2/3 pyramidal neurons in the primary motor cortex in the APPswe/PS1dE9 mouse model of AD and age-matched wild type control mice...
November 14, 2017: Molecular Neurodegeneration
https://www.readbyqxmd.com/read/29137322/the-c-jun-n-terminal-kinase-plays-a-key-role-in-ocular-degenerative-changes-in-a-mouse-model-of-alzheimer-disease-suggesting-a-correlation-between-ocular-and-brain-pathologies
#9
Lucia Buccarello, Alessandra Sclip, Matteo Sacchi, Anna Maria Castaldo, Ilaria Bertani, Andrea ReCecconi, Silvia Maestroni, Gianpaolo Zerbini, Paolo Nucci, Tiziana Borsello
Recently a range of ocular manifestations such as retinal and lens amyloid-beta accumulation and retinal nerve fiber layer loss have been proposed as potential biomarkers in Alzheimer disease (AD). The TgCRND8 mouse model of AD exhibits age-dependent amyloid β (Aβ) oligomers accumulation and cognitive defects, amyloid plaques and hyperphosphorylated Tau deposition and inflammation. We proved the correlation between ocular pathologies and AD, observing increased levels of p-APP and p-Tau, accumulation of Aβ oligomers in the retina, eye, and optic nerve...
October 10, 2017: Oncotarget
https://www.readbyqxmd.com/read/29129774/crosstalk-between-endoplasmic-reticulum-stress-and-brain-inflammation-in-alzheimer-s-disease
#10
REVIEW
Luis E Santos, Sergio T Ferreira
While most often noted for its cognitive symptoms, Alzheimer's disease (AD) is, at its core, a disease of protein misfolding/aggregation, with an intriguing inflammatory component. Defective clearance and/or abnormal production of the amyloid-β peptide (Aβ), and its ensuing accumulation and aggregation, underlie two hallmark features of AD: brain accumulation of insoluble protein deposits known as amyloid or senile plaques, and buildup of soluble Aβ oligomers (AβOs), diffusible toxins linked to synapse dysfunction and memory impairment...
November 9, 2017: Neuropharmacology
https://www.readbyqxmd.com/read/29128369/inhibition-of-poly-adp-ribose-polymerase-1-alters-expression-of-mitochondria-related-genes-in-pc12-cells-relevance-to-mitochondrial-homeostasis-in-neurodegenerative-disorders
#11
Grzegorz A Czapski, Magdalena Cieślik, Przemysław L Wencel, Sylwia Wójtowicz, Robert P Strosznajder, Joanna B Strosznajder
Alzheimer's disease (AD) is characterized by the release of amyloid beta peptides (Aβ) in the form of monomers/oligomers which may lead to oxidative stress, mitochondria dysfunction, synaptic loss, neuroinflammation and, in consequence, to overactivation of poly(ADP-ribose) polymerase-1 (PARP-1). However, Aβ peptides are also released in the brain ischemia, traumatic injury and in inflammatory response. PARP-1 is suggested to be a promising target in therapy of neurodegenerative disorders. We investigated the impact of PARP-1 inhibition on transcription of mitochondria-related genes in PC12 cells...
November 8, 2017: Biochimica et Biophysica Acta
https://www.readbyqxmd.com/read/29120943/native-prion-protein-homodimers-are-destabilized-by-oligomeric-amyloid-%C3%AE-1-42-species-as-shown-by-single-molecule-imaging
#12
Sachin S Tiwari, Yuki M Shirai, Yuri L Nemoto, Kumiko Kojima, Kenichi G N Suzuki
Prion proteins (PrPc) are receptors for amyloid β 1-42 (Aβ1-42) oligomers, but we do not know the impact of Aβ1-42 binding to PrPc on the interaction of membrane-bound PrPc with molecules that regulate downstream biological pathways. Stability of the PrPc dimeric complex and subsequent intermolecular interactions with membranous or cytoplasmic molecules are important for physiological functions of PrPc including neuroprotection. The principal aim of this study was to determine whether homodimer lifetime of PrPc is affected by the presence of Aβ1-42 oligomers...
November 8, 2017: Neuroreport
https://www.readbyqxmd.com/read/29118388/near-infrared-light-decreases-synaptic-vulnerability-to-amyloid-beta-oligomers
#13
Michele M Comerota, Balaji Krishnan, Giulio Taglialatela
Synaptic dysfunction due to the disrupting binding of amyloid beta (Aβ) and tau oligomers is one of the earliest impairments in Alzheimer's Disease (AD), driving initial cognitive deficits and clinical manifestation. Consequently, there is ample consensus that preventing early synaptic dysfunction would be an effective therapeutic strategy for AD. With this goal in mind, we investigated the effect of a treatment of mice with near infrared (NIR) light on synaptic vulnerability to Aβ oligomers. We found that Aβ oligomer binding to CNS synaptosomes isolated from wild type (wt) mice treated with NIR light was significantly reduced and the resulting suppression of long term potentiation (LTP) by Aβ oligomers was prevented...
November 8, 2017: Scientific Reports
https://www.readbyqxmd.com/read/29114064/sorla-attenuates-epha4-signaling-and-amyloid-%C3%AE-induced-neurodegeneration
#14
Timothy Y Huang, Yingjun Zhao, Lu-Lin Jiang, Xiaoguang Li, Yan Liu, Yu Sun, Juan C Piña-Crespo, Bing Zhu, Eliezer Masliah, Thomas E Willnow, Elena B Pasquale, Huaxi Xu
Sortilin-related receptor with LDLR class A repeats (SORLA, SORL1, or LR11) is a genetic risk factor associated with Alzheimer's disease (AD). Although SORLA is known to regulate trafficking of the amyloid β (Aβ) precursor protein to decrease levels of proteotoxic Aβ oligomers, whether SORLA can counteract synaptic dysfunction induced by Aβ oligomers remains unclear. Here, we show that SORLA interacts with the EphA4 receptor tyrosine kinase and attenuates ephrinA1 ligand-induced EphA4 clustering and activation to limit downstream effects of EphA4 signaling in neurons...
November 7, 2017: Journal of Experimental Medicine
https://www.readbyqxmd.com/read/29113468/hippocampal-cholinergic-neurostimulating-peptide-as-a-possible-modulating-factor-against-glutamatergic-neuronal-disability-by-amyloid-oligomers
#15
Toyohiro Sato, Yoshiaki Ohi, Daisuke Kato, Masayuki Mizuno, Hiroshi Takase, Tetsuko Kanamori, Cesar V Borlongan, Akira Haji, Noriyuki Matsukawa
Despite having pathological changes in the brain associated with Alzheimer's disease (AD), some patients have preserved cognitive function. A recent epidemiological study has shown that diet, exercise, cognitive training, and vascular risk monitoring interventions may reduce cognitive decline in at-risk elderly people in the general population. However, the details of molecular mechanisms underlying this cognitive function preservation are still unknown. Previous reports have demonstrated that enriched environments prevent the impairment of hippocampal long-term potentiation (LTP) through β2-adrenergic signals, when LTP is incompletely suppressed by synthetic amyloid-β (Aβ) oligomers...
September 2017: Cell Transplantation
https://www.readbyqxmd.com/read/29104140/low-dose-%C3%AE-secretase-inhibition-increases-secretion-of-a%C3%AE-peptides-and-intracellular-oligomeric-a%C3%AE
#16
Lotta Agholme, Marcus Clarin, Eleni Gkanatsiou, Petronella Kettunen, Jasmine Chebli, Gunnar Brinkmalm, Kaj Blennow, Petra Bergström, Erik Portelius, Henrik Zetterberg
γ-Secretase inhibitors have been considered promising drug candidates against Alzheimer's disease (AD) due to their ability to reduce amyloid-β (Aβ) production. However, clinical trials have been halted due to lack of clinical efficacy and/or side effects. Recent in vitro studies suggest that low doses of γ-secretase inhibitors may instead increase Aβ production. Using a stem cell-derived human model of cortical neurons and low doses of the γ-secretase inhibitor DAPT, the effects on a variety of Aβ peptides were studied using mass spectrometry...
November 8, 2017: Molecular and Cellular Neurosciences
https://www.readbyqxmd.com/read/29103036/the-unexpected-role-of-a%C3%AE-1-42-monomers-in-the-pathogenesis-of-alzheimer-s-disease
#17
Elena Tamagno, Michela Guglielmotto, Debora Monteleone, Giusi Manassero, Valeria Vasciaveo, Massimo Tabaton
Amyloid-β (Aβ) has been proposed as a biomarker and a drug target for the therapy of Alzheimer's disease (AD). The neurotoxic entity and relevance of each conformational form of Aβ to AD pathology is still under debate; Aβ oligomers are considered the major killer form of the peptide whereas monomers have been proposed to be involved in physiological process. Here we reviewed some different effects mediated by monomers and oligomers on mechanisms involved in AD pathogenesis such as autophagy and tau aggregation...
October 30, 2017: Journal of Alzheimer's Disease: JAD
https://www.readbyqxmd.com/read/29101243/human-brain-derived-a%C3%AE-oligomers-bind-to-synapses-and-disrupt-synaptic-activity-in-a-manner-that-requires-app
#18
Zemin Wang, Rosemary J Jackson, Wei Hong, Walter M Taylor, Grant T Corbett, Arturo Moreno, Wen Liu, Shaomin Li, Matthew P Frosch, Inna Slutsky, Tracy Young-Pearse, Tara L Spires-Jones, Dominic M Walsh
Compelling genetic evidence links the amyloid precursor protein (APP) to Alzheimer's disease (AD), and several theories have been advanced to explain the involvement of APP in AD. A leading hypothesis proposes that a small amphipathic fragment of APP, the amyloid β-protein (Aβ), self-associates to form soluble aggregates which impair synaptic and network activity. Here, we employed the most disease-relevant form of Aβ, protein isolated from AD brain. Using this material, we show that the synaptotoxic effects of Aβ depend on expression of APP and that the Aβ-mediated impairment of synaptic plasticity is accompanied by pre-synaptic effects which disrupt the excitatory/inhibitory (E/I) balance...
November 3, 2017: Journal of Neuroscience: the Official Journal of the Society for Neuroscience
https://www.readbyqxmd.com/read/29094448/amyloid-beta-monomers-regulate-cyclic-adenosine-monophosphate-response-element-binding-protein-functions-by-activating-type-1-insulin-like-growth-factor-receptors-in-neuronal-cells
#19
Stefania Zimbone, Irene Monaco, Fiorenza Gianì, Giuseppe Pandini, Agata G Copani, Maria Laura Giuffrida, Enrico Rizzarelli
Alzheimer's disease (AD) is a progressive neurodegenerative disorder associated with synaptic dysfunction, pathological accumulation of β-amyloid (Aβ), and neuronal loss. The self-association of Aβ monomers into soluble oligomers seems to be crucial for the development of neurotoxicity (J. Neurochem., 00, 2007 and 1172). Aβ oligomers have been suggested to compromise neuronal functions in AD by reducing the expression levels of the CREB target gene and brain-derived neurotrophic factor (BDNF) (J. Neurosci...
November 1, 2017: Aging Cell
https://www.readbyqxmd.com/read/29084238/doliroside-a-from-dolichos-falcata-klein-suppressing-amyloid-%C3%AE-protein-42-fibrillogenesis-an-insight-at-molecular-level
#20
Dongpu Li, Hongfei Yu, Qinxiong Lin, Yun Liu
A bioactive chemical constituent, doliroside A, from Chinese traditional herbal medicine Dolichos falcata Klein was isolated, purified and identified by 60% ethanol extraction, thin layer chromatography (TLC), high performance liquid chromatography (HPLC) and nuclear magnetic resonance (NMR) spectroscopy. Molecular interaction mechanism between doliroside and amyloid β42 protein was evaluated by thioflavin T fluorescence (ThT), circular dichroism (CD), atomic force microscope (AFM), and differential scanning calorimeter (DSC) from the aspects of kinetics, secondary structure, morphology, and thermodynamics, respectively...
2017: PloS One
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