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https://www.readbyqxmd.com/read/29775624/characterization-and-comparative-analysis-of-a-new-mouse-microglial-cell-model-for-studying-neuroinflammatory-mechanisms-during-neurotoxic-insults
#1
Souvarish Sarkar, Emir Malovic, Deeksha Sarda, Vivek Lawana, Dharmin Rokad, Huajun Jin, Vellareddy Anantharam, Arthi Kanthasamy, Anumantha G Kanthasamy
Microglia are the first responders of the central nervous system, acting as the key modulators of neuroinflammation observed during neurotoxic insults as well as in the pathophysiology of several neurodegenerative disorders including Alzheimer's (AD), Parkinson's (PD), and Huntington's diseases (HD). The number of publications on microglia has increased steadily throughout the past decade because of immense interests in the neuroinflammation that precedes the neurodegenerative process. To study microglial biology and its role in modulating neuroinflammation, immortalized microglial cell lines derived from mice, rats, and humans have been developed...
May 15, 2018: Neurotoxicology
https://www.readbyqxmd.com/read/29762014/selective-and-sensitive-pull-down-of-amyloid-fibrils-produced-in-vitro-and-in-vivo-by-the-use-of-pentameric-thiophene-coupled-resins
#2
Anna Beatriz Wreden, Luiza Fernandes, Mirian Kelley, Antônio Pereira-Neves, Caroline S Moreira, David R da Rocha, Fernando L Palhano
Protein aggregation is a hallmark of several degenerative diseases, including Alzheimer's disease, Parkinson's disease and familial amyloidosis (Finnish type) (FAF). A method to isolate and detect amyloids is desired for the diagnosis of amyloid diseases. Here, we report the synthesis of pentameric thiophene amyloid ligand (p-FTAA) linked to agarose resin for selective purification of amyloid aggregates produced in vitro and in vivo. Using amyloid fibrils produced in vitro from alpha-synuclein, gelsolin and Aβ1-40 and gelsolin amyloid aggregates extracted from tissue homogenates of a mouse model of FAF, we observed that p-FTAA resin was able to pull down amyloid aggregates...
May 15, 2018: ACS Chemical Neuroscience
https://www.readbyqxmd.com/read/29755356/anti-parkinson-potential-of-silymarin-mechanistic-insight-and-therapeutic-standing
#3
REVIEW
Hammad Ullah, Haroon Khan
Parkinson's disease (PD) involves aggregation of α-synuclein and progressive loss of dopaminergic neurons. Pathogenesis of PD may also be related to one's genetic background. PD is most common among geriatric population and approximately 1-2% of population suffers over age 65 years. Currently no successful therapies are in practice for the management of PD and available therapies tend to decrease the symptoms of PD only. Furthermore, these are associated with diverse range of adverse effects profile. The neuroprotective effects of polyphenols are widely studied and documented...
2018: Frontiers in Pharmacology
https://www.readbyqxmd.com/read/29750859/different-structural-conformers-of-monomeric-alpha-synuclein-identified-after-lyophilising-and-freezing
#4
Amberley Stephens, Nadezhda Nespovitaya, Maria Zacharopoulou, Clemens F Kaminski, Jonathan James Phillips, Gabriele S Kaminski Schierle
Understanding the mechanisms behind amyloid protein aggregation in diseases such as Parkinson's and Alzheimer's disease is often hampered by the reproducibility of in vitro assays. Yet, understanding the basic mechanisms of protein misfolding is essential for the development of novel therapeutic strategies. We show here, that for the amyloid protein alpha-synuclein (aSyn), a protein involved in Parkinson's disease (PD), chromatographic buffers and storage conditions can significantly interfere with the overall structure of the protein and thus affect protein aggregation kinetics...
May 11, 2018: Analytical Chemistry
https://www.readbyqxmd.com/read/29748975/lysosomes-autophagosomes-and-alzheimer-pathology-in-dementia-with-lewy-body-disease
#5
Rowan Gurney, Yvonne S Davidson, Andrew C Robinson, Anna Richardson, Matthew Jones, Julie S Snowden, David M A Mann
A failure of protein degradation may underpin Lewy body disease (LBD) where α-synuclein is assimilated into the pathognomic Lewy bodies and Lewy neurites. We investigated histological alterations in lysosomes and autophagosomes in the substantia nigra (SN) and cingulate gyrus (CG) in 34 patients with LBD employing antibodies against phosphorylated α-synuclein and lysosomal (lysosomal associated membrane proteins 1 and 2 (LAMP-1 and LAMP-2), cathepsin D (CTSD)) and autophagosomal (microtubule-associated protein light chain 3α (LC3A)) proteins...
May 10, 2018: Neuropathology: Official Journal of the Japanese Society of Neuropathology
https://www.readbyqxmd.com/read/29744847/discriminating-strains-of-self-propagating-protein-aggregates-using-a-conformational-stability-assay
#6
Heather H C Lau, Angus Lau, Joel C Watts
Prions and other self-propagating protein aggregates can exist as distinct strains, which are thought to represent different conformations of aggregates. There is growing evidence that protein aggregate strains may be important for understanding the biology of common neurodegenerative disorders, such as Alzheimer's disease and Parkinson's disease. While methodology for discriminating prion strains is in widespread use, there is a paucity of tools for comparing the conformational properties of aggregates composed of β-amyloid (Aβ) peptide or α-synuclein protein, particularly when present in complex samples such as brain extracts...
2018: Methods in Molecular Biology
https://www.readbyqxmd.com/read/29743672/cellular-milieu-imparts-distinct-pathological-%C3%AE-synuclein-strains-in-%C3%AE-synucleinopathies
#7
Chao Peng, Ronald J Gathagan, Dustin J Covell, Coraima Medellin, Anna Stieber, John L Robinson, Bin Zhang, Rose M Pitkin, Modupe F Olufemi, Kelvin C Luk, John Q Trojanowski, Virginia M-Y Lee
In Lewy body diseases-including Parkinson's disease, without or with dementia, dementia with Lewy bodies, and Alzheimer's disease with Lewy body co-pathology 1 -α-synuclein (α-Syn) aggregates in neurons as Lewy bodies and Lewy neurites 2 . By contrast, in multiple system atrophy α-Syn accumulates mainly in oligodendrocytes as glial cytoplasmic inclusions (GCIs) 3 . Here we report that pathological α-Syn in GCIs and Lewy bodies (GCI-α-Syn and LB-α-Syn, respectively) is conformationally and biologically distinct...
May 9, 2018: Nature
https://www.readbyqxmd.com/read/29738882/a-sticky-situation-aberrant-protein-protein-interactions-in-parkinson-s-disease
#8
REVIEW
James Brown, Mathew H Horrocks
The aberrant aggregation of normally soluble proteins into amyloid fibrils is the pathological hallmark of several neurodegenerative disorders, including Alzheimer's and Parkinson's diseases. Understanding this process will be key to developing both diagnostic and therapeutic approaches for neurodegenerative diseases. Recent advances in biophysical techniques, coupled with kinetic analyses have enabled a thorough description of the key molecular steps involved in protein aggregation. In this review, we discuss these advances and how they have been applied to study the ability of one such protein, α-Synuclein, to form neurotoxic oligomers...
May 5, 2018: Seminars in Cell & Developmental Biology
https://www.readbyqxmd.com/read/29738880/the-interaction-of-%C3%AE-synuclein-and-tau-a-molecular-conspiracy-in-neurodegeneration
#9
REVIEW
Xu Yan, Riikka-Liisa Uronen, Henri J Huttunen
α-synuclein and Tau are proteins prone to pathological misfolding and aggregation that are normally found in the presynaptic and axonal compartments of neurons. Misfolding initiates a homo-oligomerization and aggregation cascade culminating in cerebral accumulation of aggregated α-synuclein and Tau in insoluble protein inclusions in multiple neurodegenerative diseases. Traditionally, α-synuclein-containing Lewy bodies have been associated with Parkinson's disease and Tau-containing neurofibrillary tangles with Alzheimer's disease and various frontotemporal dementia syndromes...
May 5, 2018: Seminars in Cell & Developmental Biology
https://www.readbyqxmd.com/read/29734684/comparing-the-folds-of-prions-and-other-pathogenic-amyloids
#10
REVIEW
José Miguel Flores-Fernández, Vineet Rathod, Holger Wille
Pathogenic amyloids are the main feature of several neurodegenerative disorders, such as Creutzfeldt⁻Jakob disease, Alzheimer’s disease, and Parkinson’s disease. High resolution structures of tau paired helical filaments (PHFs), amyloid-β(1-42) (Aβ(1-42)) fibrils, and α-synuclein fibrils were recently reported using cryo-electron microscopy. A high-resolution structure for the infectious prion protein, PrPSc , is not yet available due to its insolubility and its propensity to aggregate, but cryo-electron microscopy, X-ray fiber diffraction, and other approaches have defined the overall architecture of PrPSc as a 4-rung β-solenoid...
May 4, 2018: Pathogens
https://www.readbyqxmd.com/read/29729013/the-role-of-heparan-sulfates-in-protein-aggregation-and-their-potential-impact-on-neurodegeneration
#11
REVIEW
Auriane Maïza, Sandrine Chantepie, Cecilia Vera, Alexandre Fifre, Min Bao Huynh, Olivier Stettler, Mohand Ouidir Ouidja, Dulce Papy-Garcia
Neurodegenerative disorders, such as Alzheimer's, Parkinson's, and prion diseases, are directly linked to the formation and accumulation of protein aggregates in the brain. These aggregates, principally made of proteins or peptides that clamp together after acquisition of β-folded structures, also contain heparan sulfates. Several lines of evidence suggest that heparan sulfates centrally participate in the protein aggregation process. In vitro, they trigger misfolding, oligomerisation, and fibrillation of amyloidogenic proteins, such as Aβ, tau, α-synuclein, prion protein, etc...
May 4, 2018: FEBS Letters
https://www.readbyqxmd.com/read/29704492/synergistic-amyloid-switch-triggered-by-early-heterotypic-oligomerization-of-intrinsically-disordered-%C3%AE-synuclein-and-tau
#12
Karishma Bhasne, Sanjana Sebastian, Neha Jain, Samrat Mukhopadhyay
Amyloidogenic intrinsically disordered proteins, α-synuclein and tau are linked to Parkinson's disease and Alzheimer's disease, respectively. A body of evidences suggests that α-synuclein and tau, both present in the presynaptic nerve terminals, co-aggregate in many neurological ailments. The molecular mechanism of α-synuclein-tau hetero-assembly is poorly understood. Here we show that amyloid formation is synergistically facilitated by heterotypic association mediated by binding-induced misfolding of both α-synuclein and tau K18...
April 25, 2018: Journal of Molecular Biology
https://www.readbyqxmd.com/read/29700597/cerebrospinal-fluid-neurogranin-concentration-in-neurodegeneration-relation-to-clinical-phenotypes-and-neuropathology
#13
Erik Portelius, Bob Olsson, Kina Höglund, Nicholas C Cullen, Hlin Kvartsberg, Ulf Andreasson, Henrik Zetterberg, Åsa Sandelius, Leslie M Shaw, Virginia M Y Lee, David J Irwin, Murray Grossman, Daniel Weintraub, Alice Chen-Plotkin, David A Wolk, Leo McCluskey, Lauren Elman, Jennifer McBride, Jon B Toledo, John Q Trojanowski, Kaj Blennow
Neurogranin (Ng) is a post-synaptic protein that previously has been shown to be a biomarker for synaptic function when measured in cerebrospinal fluid (CSF). The CSF concentration of Ng is increased in Alzheimer's disease dementia (ADD), and even in the pre-dementia stage. In this prospective study, we used an enzyme-linked immunosorbent assay that quantifies Ng in CSF to test the performance of Ng as a marker of synaptic function. In 915 patients, CSF Ng was evaluated across several different neurodegenerative diseases...
April 26, 2018: Acta Neuropathologica
https://www.readbyqxmd.com/read/29689721/reaction-of-amyloid-%C3%AE-peptide-antibody-with-different-infectious-agents-involved-in-alzheimer-s-disease
#14
Aristo Vojdani, Elroy Vojdani, Evan Saidara, Datis Kharrazian
As early as the 1980s, molecular virologist Ruth Itzhaki began to investigate if there was a causal connection between infections and neurodegenerative disorder. Although the theory has yet to be universally embraced, in 2016 Itzhaki and 33 other scientists from all over the world published a review article in this very journal presenting evidence for the causal role of pathogens in Alzheimer's disease (AD). Exactly how and in what way pathogens affect the induction of AD has yet to be determined, but one possible answer may involve the cross-reactivity of different pathogens with amyloid-β (Aβ)...
2018: Journal of Alzheimer's Disease: JAD
https://www.readbyqxmd.com/read/29675576/gintonin-mitigates-mptp-induced-loss-of-nigrostriatal-dopaminergic-neurons-and-accumulation-of-%C3%AE-synuclein-via-the-nrf2-ho-1-pathway
#15
Min Gi Jo, Muhammad Ikram, Myeung Hoon Jo, Lang Yoo, Kwang Chul Chung, Seung-Yeol Nah, Hongik Hwang, Hyewhon Rhim, Myeong Ok Kim
Gintonin, a ginseng-derived glycolipoprotein isolated from ginseng, has been shown to be neuroprotective in several neurological disorders such as Alzheimer's disease models and depressive-like behaviors. In this study, we sought to investigate the potential protective mechanisms of gintonin in an in vivo MPTP and in vitro MPP+ -mediated Parkinson's disease (PD) model. We hypothesized that activation of nuclear factor erythroid 2-related factor 2/heme oxygenase-1 (Nrf2/HO-1, potential therapeutic targets for neurodegeneration) with gintonin could abrogate PD-associated neurotoxicity by modulating the accumulation of α-synuclein, neuroinflammation, and apoptotic cell death in an MPTP/MPP+ models of PD...
April 19, 2018: Molecular Neurobiology
https://www.readbyqxmd.com/read/29660838/tdp-43-pathology-in-multiple-system-atrophy-colocalization-of-tdp-43-and-%C3%AE-synuclein-in-glial-cytoplasmic-inclusions
#16
Shunsuke Koga, Wen-Lang Lin, Ronald L Walton, Owen A Ross, Dennis W Dickson
AIMS: This study aimed to assess clinicopathologic features of transactive response DNA-binding protein of 43 kDa (TDP-43) pathology and its risk factors in multiple system atrophy (MSA). METHODS: Paraffin-embedded sections of the amygdala and basal forebrain from 186 autopsy-confirmed MSA cases were screened with immunohistochemistry for phospho-TDP-43. In cases having TDP-43 pathology, additional brain regions were assessed. Immunohistochemical and immunofluorescence double-staining and immunogold electron microscopy (IEM) were performed to evaluate colocalization of TDP-43 and α-synuclein...
April 16, 2018: Neuropathology and Applied Neurobiology
https://www.readbyqxmd.com/read/29624752/biomarkers-for-cognitive-impairment-in-lewy-body-disorders-status-and-relevance-for-clinical-trials
#17
REVIEW
Andrew Siderowf, Dag Aarsland, Brit Mollenhauer, Jennifer G Goldman, Bernard Ravina
Biomarkers have the potential to improve diagnosis and prognosis, and guide clinical treatment decisions. In research, biomarkers can be used for patient selection and as outcome measures in clinical trials. A range of biochemical and imaging biomarkers are relevant to patients with Lewy body disorders, including PD, PD dementia, and dementia with Lewy bodies. Dopaminergic imaging is used for differential diagnosis of parkinsonian disorders versus tremor disorders without dopamingeric deficits, and also to differentiate dementia with Lewy bodies from Alzheimer's disease...
April 2018: Movement Disorders: Official Journal of the Movement Disorder Society
https://www.readbyqxmd.com/read/29615738/abundant-fish-protein-inhibits-%C3%AE-synuclein-amyloid-formation
#18
Tony Werner, Ranjeet Kumar, Istvan Horvath, Nathalie Scheers, Pernilla Wittung-Stafshede
The most common allergen in fish, the highly-abundant protein β-parvalbumin, forms amyloid structures as a way to avoid gastrointestinal degradation and transit to the blood. In humans, the same amyloid structures are mostly associated with neurodegenerative disorders such as Alzheimer's and Parkinson's. We here assessed a putative connection between these amyloids using recombinant Atlantic cod β-parvalbumin and the key amyloidogenic protein in Parkinson's disease, α-synuclein. Using a set of in vitro biophysical methods, we discovered that β-parvalbumin readily inhibits amyloid formation of α-synuclein...
April 3, 2018: Scientific Reports
https://www.readbyqxmd.com/read/29604263/cerebrospinal-fluid-%C3%AE-synuclein-contributes-to-the-differential-diagnosis-of-alzheimer-s-disease
#19
Min Shi, Lu Tang, Jon B Toledo, Carmen Ginghina, Hua Wang, Patrick Aro, Poul H Jensen, Daniel Weintraub, Alice S Chen-Plotkin, David J Irwin, Murray Grossman, Leo McCluskey, Lauren B Elman, David A Wolk, Edward B Lee, Leslie M Shaw, John Q Trojanowski, Jing Zhang
INTRODUCTION: The ability of Alzheimer's disease (AD) cerebrospinal fluid (CSF) biomarkers (amyloid β peptide 1-42, total tau, and phosphorylated tau) to discriminate AD from related disorders is limited. Biomarkers for other concomitant pathologies (e.g., CSF α-synuclein [α-syn] for Lewy body pathology) may be needed to further improve the differential diagnosis. METHODS: CSF total α-syn, phosphorylated α-syn at Ser129, and AD CSF biomarkers were evaluated with Luminex immunoassays in 367 participants, followed by validation in 74 different neuropathologically confirmed cases...
March 28, 2018: Alzheimer's & Dementia: the Journal of the Alzheimer's Association
https://www.readbyqxmd.com/read/29571747/cdk5-suppression-blocks-sirt1-degradation-via-the-ubiquitin-proteasome-pathway-in-parkinson-s-disease-models
#20
Qian Zhang, Pei Zhang, Guang-Jian Qi, Zheng Zhang, Feng He, Ze-Xi Lv, Xiang Peng, Hong-Wei Cai, Tong-Xia Li, Xue-Min Wang, Bo Tian
The NAD+ -dependent protein deacetylase sirtuin 1 (SIRT1), a member of the sirtuin family, may have a neuroprotective effect in multiple neurodegenerative disorders such as Alzheimer's disease (AD), Parkinson's disease (PD) and Amyotrophic lateral sclerosis (ALS). Many studies have suggested that overexpression-induced or resveratrol-treated activation of SIRT1 could significantly ameliorate several neurodegenerative diseases in mouse models. However, the type of SIRT1, protein expression levels and underlying mechanisms remain unclear, especially in PD...
March 20, 2018: Biochimica et Biophysica Acta
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