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alzheimer's disease prion diseases

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https://www.readbyqxmd.com/read/27921253/aberrant-alterations-of-mitochondrial-factors-drp1-and-opa1-in-the-brains-of-scrapie-experiment-rodents
#1
Xiao -Dong Yang, Qi Shi, Jing Sun, Yan Lv, Yue Ma, Cao Chen, Kang Xiao, Wei Zhou, Xiao-Ping Dong
The abnormal mitochondrial dynamics has been reported in the brains of some neurodegenerative diseases, such as Alzheimer's disease (AD) and Parkinson's disease (PD), but limitedly described in prion disease. Dynamin-related protein 1 (Drpl) and optic atrophy protein 1 (Opa1) are two essential elements for mitochondria fission and fusion. To evaluate possible changes of mitochondria dynamics during prion infection, the situations of brain Drp1 and Opa1 of scrapie strains 139A, ME7, and S15 mice, as well as 263K-infected hamsters, were analyzed...
December 6, 2016: Journal of Molecular Neuroscience: MN
https://www.readbyqxmd.com/read/27916654/prion-like-mechanisms-and-potential-therapeutic-targets-in-neurodegenerative-disorders
#2
REVIEW
Masato Hasegawa, Takashi Nonaka, Masami Masuda-Suzukake
Prion-like propagation of abnormal intracytoplasmic proteins, which are the defining features of major neurodegenerative disorders, such as Alzheimer's disease (AD), Parkinson's disease (PD) and amyotrophic lateral sclerosis (ALS), has been proposed. A growing body of evidence strongly suggests that abnormal tau, α-synuclein and TDP-43 have prion-like properties, convert the corresponding normal proteins into abnormal forms, and are transmitted from cell to cell, spreading throughout the brain. This idea is extremely important not only for understanding the pathogenesis and progression of these diseases, but also for the development of molecular therapies...
December 1, 2016: Pharmacology & Therapeutics
https://www.readbyqxmd.com/read/27911827/tau-prions-from-alzheimer-s-disease-and-chronic-traumatic-encephalopathy-patients-propagate-in-cultured-cells
#3
Amanda L Woerman, Atsushi Aoyagi, Smita Patel, Sabeen A Kazmi, Iryna Lobach, Lea T Grinberg, Ann C McKee, William W Seeley, Steven H Olson, Stanley B Prusiner
Tau prions are thought to aggregate in the central nervous system, resulting in neurodegeneration. Among the tauopathies, Alzheimer's disease (AD) is the most common, whereas argyrophilic grain disease (AGD), corticobasal degeneration (CBD), chronic traumatic encephalopathy (CTE), Pick's disease (PiD), and progressive supranuclear palsy (PSP) are less prevalent. Brain extracts from deceased individuals with PiD, a neurodegenerative disorder characterized by three-repeat (3R) tau prions, were used to infect HEK293T cells expressing 3R tau fused to yellow fluorescent protein (YFP)...
November 28, 2016: Proceedings of the National Academy of Sciences of the United States of America
https://www.readbyqxmd.com/read/27911289/the-brain-s-structural-connectome-mediates-the-relationship-between-regional-neuroimaging-biomarkers-in%C3%A2-alzheimer-s-disease
#4
Sneha Pandya, Amy Kuceyeski, Ashish Raj
Alzheimer's disease (AD), one of the most common causes of dementia in adults, is a progressive neurodegenerative disorder exhibiting well-defined neuropathological hallmarks. It is known that disease pathology involves misfolded amyloid-β (Aβ) and tau proteins, and exhibits a relatively stereotyped progression over decades. The relationship between AD neuropathological hallmarks (Aβ, hypometabolism, and tau proteins) and imaging biomarkers (MRI, AV-45/FDG-PET) is not fully understood. In addition, biomarker pathologies are oftentimes discordant, wherein it may show varying levels of abnormality across brain regions...
November 28, 2016: Journal of Alzheimer's Disease: JAD
https://www.readbyqxmd.com/read/27910931/mutational-analysis-of-prnp-in-alzheimer-s-disease-and-frontotemporal-dementia-in-china
#5
Weiwei Zhang, Bin Jiao, Tingting Xiao, Chuzheng Pan, Xixi Liu, Lin Zhou, Beisha Tang, Lu Shen
The prion protein (PRNP) gene is associated with prion diseases, whereas variants of the PRNP gene may also explain some cases of Alzheimer disease (AD) and frontotemporal dementia (FTD) in Caucasian populations. To determine the prevalence of the PRNP gene in patients with AD and FTD in China, we screened all exons of the PRNP gene in a cohort of 683 cases (606 AD and 77 FTD) in the Chinese Han population and we detected a novel missense mutation p.S17G in a late-onset AD (LOAD) patient. Furthermore, we analyzed the PRNP M/V polymorphism at codon 129, which was previously reported as a risk factor...
December 2, 2016: Scientific Reports
https://www.readbyqxmd.com/read/27908423/copper-brain-protein-protection-against-free-radical-induced-neuronal-death-survival-ratio-in-sh-sy5y-neuroblastoma-cell-cultures
#6
Roger Deloncle, Bernard Fauconneau, Olivier Guillard, José Delaval, Gérard Lesage, Alain Pineau
In Creutzfeldt Jakob, Alzheimer and Parkinson diseases, copper metalloproteins such as prion, amyloid protein precursor and α-synuclein are able to protect against free radicals by reduction from cupric Cu(+2) to cupreous Cu(+). In these pathologies, a regional copper (Cu) brain decrease correlated with an iron, zinc or manganese (Mn) increase has previously been observed, leading to local neuronal death and abnormal deposition of these metalloproteins in β-sheet structures. In this study we demonstrate the protective effect of Cu metalloproteins against deleterious free-radical effects...
January 2017: Journal of Trace Elements in Medicine and Biology
https://www.readbyqxmd.com/read/27900898/non-alzheimer-s-and-atypical-dementia-geschwind-michael-d-and-racine-caroline-eds-non-alzheimer-s-and-atypical-dementia-232pp-%C3%A2-94-99-wiley-blackwell-9781444336245-144433624x-formula-see-text
#7
(no author information available yet)
This comprehensive overview of atypical dementia, including Lewy body, prion diseases, and leukoencephalopathies, was written specifically for multidisciplinary teams.
November 30, 2016: Nursing Older People
https://www.readbyqxmd.com/read/27893962/proteopathic-strains-and-the-heterogeneity-of-neurodegenerative-diseases
#8
Lary C Walker
Most age-related neurodegenerative diseases are associated with the misfolding and aberrant accumulation of specific proteins in the nervous system. The proteins self-assemble and spread by a prion-like process of corruptive molecular templating, whereby abnormally folded proteins induce the misfolding and aggregation of like proteins into characteristic lesions. Despite the apparent simplicity of this process at the molecular level, diseases such as Alzheimer's, Parkinson's, Creutzfeldt-Jakob, and others display remarkable phenotypic heterogeneity, both clinically and pathologically...
November 23, 2016: Annual Review of Genetics
https://www.readbyqxmd.com/read/27886009/diagnostic-accuracy-of-a-combined-analysis-of-cerebrospinal-fluid-t-prp-t-tau-p-tau-and-a%C3%AE-42-in-the-differential-diagnosis-of-creutzfeldt-jakob-disease-from-alzheimer-s-disease-with-emphasis-on-atypical-disease-variants
#9
Samir Abu Rumeileh, Francesca Lattanzio, Michelangelo Stanzani Maserati, Romana Rizzi, Sabina Capellari, Piero Parchi
According to recent studies, the determination of cerebrospinal fluid (CSF) total tau (t-tau)/phosphorylated tau (p-tau) ratio and total prion protein (t-PrP) levels significantly improves the accuracy of the diagnosis of Alzheimer's disease (AD) in atypical cases with clinical or laboratory features mimicking Creutzfeldt-Jakob disease (CJD). However, this has neither been validated nor tested in series including atypical CJD variants. Furthermore, the added diagnostic value of amyloid-β (Aβ)42 remains unclear...
November 19, 2016: Journal of Alzheimer's Disease: JAD
https://www.readbyqxmd.com/read/27837530/freeze-fracture-electron-microscopy-on-domains-in-lipid-mono-and-bilayer-on-nano-resolution-scale
#10
Brigitte Papahadjopoulos-Sternberg
Freeze-fracture electron microscopy (FFEM) as a cryofixation, replica, and transmission electron microscopy technique is unique in membrane bilayer and lipid monolayer research because it enables us to excess and visualize pattern such as domains in the hydrophobic center of lipid bilayer as well as the lipid/gas interface of lipid monolayer. Since one of the preparation steps of this technique includes fracturing the frozen sample and since during this fracturing process the fracture plane follows the area of weakest forces, these areas are exposed allowing us to explore pattern built up by lipids and/or intrinsic proteins but also initiated by peptides, drugs, and toxins reaching into these normally hard to access areas...
2017: Methods in Molecular Biology
https://www.readbyqxmd.com/read/27830791/the-activities-of-amyloids-from-a-structural-perspective
#11
Roland Riek, David S Eisenberg
The aggregation of proteins into structures known as amyloids is observed in many neurodegenerative diseases, including Alzheimer's disease. Amyloids are composed of pairs of tightly interacting, many stranded and repetitive intermolecular β-sheets, which form the cross-β-sheet structure. This structure enables amyloids to grow by recruitment of the same protein and its repetition can transform a weak biological activity into a potent one through cooperativity and avidity. Amyloids therefore have the potential to self-replicate and can adapt to the environment, yielding cell-to-cell transmissibility, prion infectivity and toxicity...
November 9, 2016: Nature
https://www.readbyqxmd.com/read/27830781/mammalian-prions-and-their-wider-relevance-in-neurodegenerative-diseases
#12
John Collinge
Prions are notorious protein-only infectious agents that cause invariably fatal brain diseases following silent incubation periods that can span a lifetime. These diseases can arise spontaneously, through infection or be inherited. Remarkably, prions are composed of self-propagating assemblies of a misfolded cellular protein that encode information, generate neurotoxicity and evolve and adapt in vivo. Although parallels have been drawn with Alzheimer's disease and other neurodegenerative conditions involving the deposition of assemblies of misfolded proteins in the brain, insights are now being provided into the usefulness and limitations of prion analogies and their aetiological and therapeutic relevance...
November 9, 2016: Nature
https://www.readbyqxmd.com/read/27809932/tunneling-nanotube-tnt-mediated-neuron-to-neuron-transfer-of-pathological-tau-protein-assemblies
#13
Meryem Tardivel, Séverine Bégard, Luc Bousset, Simon Dujardin, Audrey Coens, Ronald Melki, Luc Buée, Morvane Colin
A given cell makes exchanges with its neighbors through a variety of means ranging from diffusible factors to vesicles. Cells use also tunneling nanotubes (TNTs), filamentous-actin-containing membranous structures that bridge and connect cells. First described in immune cells, TNTs facilitate HIV-1 transfer and are found in various cell types, including neurons. We show that the microtubule-associated protein Tau, a key player in Alzheimer's disease, is a bona fide constituent of TNTs. This is important because Tau appears beside filamentous actin and myosin 10 as a specific marker of these fine protrusions of membranes and cytosol that are difficult to visualize...
November 4, 2016: Acta Neuropathologica Communications
https://www.readbyqxmd.com/read/27803826/a-corticobasal-syndrome-variant-of-familial-creutzfeldt-jakob-disease-with-stroke-like-onset
#14
Ján Necpál, Martin Stelzer, Silvia Koščová, Michal Patarák
Creutzfeldt-Jakob disease (CJD) is an untreatable rare human prion disease characterized by rapidly progressive dementia along with various neurological features, including myoclonus and sometimes other movement disorders. The clinical course is typically insidious and rapid, leading to an early death. In general, the most common form is sporadic CJD; however, Slovakia is typical for a high percentage of genetic cases. We present an unusual case report of a 65-year-old man with a sudden, stroke-like onset of motor aphasia with right-sided levodopa unresponsive parkinsonism, alien hand, and other characteristic features of corticobasal syndrome (CBS), with rapid deterioration and death on the 32nd day of the disease...
2016: Case Reports in Neurological Medicine
https://www.readbyqxmd.com/read/27793967/the-three-dimensional-structures-of-amyloids
#15
Roland Riek
Amyloids are highly ordered protein aggregates that are associated with both disease (including PrP prion, Alzheimer's, and Parkinson's) and biological function. The amyloid structure is composed of the cross-β-sheet entity, which is an almost indefinitely repeating two-layered intermolecular β-sheet motif. The three-dimensional (3D) structure is unique among protein folds because it folds only upon intermolecular contacts (for a folding to occur, only short sequences of amino acid residues are required), and the structure repeats itself at the atomic level (i...
October 28, 2016: Cold Spring Harbor Perspectives in Biology
https://www.readbyqxmd.com/read/27793194/activation-of-the-unfolded-protein-response-and-granulovacuolar-degeneration-are-not-common-features-of-human-prion-pathology
#16
Vera I Wiersma, Wim van Hecke, Wiep Scheper, Martijn A J van Osch, Will J M Hermsen, Annemieke J M Rozemuller, Jeroen J M Hoozemans
Human prion diseases are fatal neurodegenerative disorders with a genetic, sporadic or infectiously acquired aetiology. Neuropathologically, human prion diseases are characterized by deposition of misfolded prion protein and neuronal loss. In post-mortem brain tissue from patients with other neurodegenerative diseases characterized by protein misfolding, including Alzheimer's disease (AD) and frontotemporal lobar degeneration with tau pathology (FTLD-tau), increased activation of the unfolded protein response (UPR) has been observed...
October 28, 2016: Acta Neuropathologica Communications
https://www.readbyqxmd.com/read/27782447/dynamics-of-proteins-aggregation-i-universal-scaling-in-unbounded-media
#17
Size Zheng, Leili Javidpour, Katherine S Shing, Muhammad Sahimi
It is well understood that in some cases proteins do not fold correctly and, depending on their environment, even properly-folded proteins change their conformation spontaneously, taking on a misfolded state that leads to protein aggregation and formation of large aggregates. An important factor that contributes to the aggregation is the interactions between the misfolded proteins. Depending on the aggregation environment, the aggregates may take on various shapes forming larger structures, such as protein plaques that are often toxic...
October 7, 2016: Journal of Chemical Physics
https://www.readbyqxmd.com/read/27744334/shape-matters-the-complex-relationship-between-aggregation-and-toxicity-in-protein-misfolding-diseases
#18
Heidrun Maja Ries, Carmen Nussbaum-Krammer
A particular subgroup of protein-misfolding diseases, comprising Alzheimer's and Parkinson's disease, involves amyloidogenic proteins that can form alternative pathogenic conformations with a high tendency to self-assemble into oligomeric and fibrillar species. Although misfolded proteins have been clearly linked to disease, the exact nature of the toxic species remains highly controversial. Increasing evidence suggests that there is little correlation between the occurrence of macroscopic protein deposits and toxic phenotypes in affected cells and tissues...
October 15, 2016: Essays in Biochemistry
https://www.readbyqxmd.com/read/27735933/the-real-time-quaking-induced-conversion-assay-for-detection-of-human-prion-disease-and-study-of-other-protein-misfolding-diseases
#19
Matthias Schmitz, Maria Cramm, Franc Llorens, Dominik Müller-Cramm, Steven Collins, Ryuichiro Atarashi, Katsuya Satoh, Christina D Orrù, Bradley R Groveman, Saima Zafar, Walter J Schulz-Schaeffer, Byron Caughey, Inga Zerr
The development and adaption of in vitro misfolded protein amplification systems has been a major innovation in the detection of abnormally folded prion protein scrapie (PrP(Sc)) in human brain and cerebrospinal fluid (CSF) samples. Herein, we describe a fast and efficient protein amplification technique, real-time quaking-induced conversion (RT-QuIC), for the detection of a PrP(Sc) seed in human brain and CSF. In contrast to other in vitro misfolded protein amplification assays-such as protein misfolding cyclic amplification (PMCA)-which are based on sonication, the RT-QuIC technique is based on prion seed-induced misfolding and aggregation of recombinant prion protein substrate, accelerated by alternating cycles of shaking and rest in fluorescence plate readers...
November 2016: Nature Protocols
https://www.readbyqxmd.com/read/27729845/in-absence-of-the-cellular-prion-protein-alterations-in-copper-metabolism-and-copper-dependent-oxidase-activity-affect-iron-distribution
#20
Lisa Gasperini, Elisa Meneghetti, Giuseppe Legname, Federico Benetti
Essential elements as copper and iron modulate a wide range of physiological functions. Their metabolism is strictly regulated by cellular pathways, since dysregulation of metal homeostasis is responsible for many detrimental effects. Neurodegenerative disorders such as Alzheimer's disease, Parkinson's disease and prion diseases are characterized by alterations of metal ions. These neurodegenerative maladies involve proteins that bind metals and mediate their metabolism through not well-defined mechanisms. Prion protein, for instance, interacts with divalent cations via multiple metal-binding sites and it modulates several metal-dependent physiological functions, such as S-nitrosylation of NMDA receptors...
2016: Frontiers in Neuroscience
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