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alzheimer's disease prion diseases

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https://www.readbyqxmd.com/read/28922846/different-complicated-brain-pathologies-in-monozygotic-twins-with-gerstmann-str%C3%A3-ussler-scheinker-disease
#1
Hiroyuki Honda, Kensuke Sasaki, Hiroshi Takashima, Daisuke Mori, Sachiko Koyama, Satoshi O Suzuki, Toru Iwaki
Gerstmann-Sträussler-Scheinker disease (GSS) is an autosomal, dominantly inherited prion disease. In this study, we present different complicated brain pathologies determined postmortem of monozygotic GSS twin sisters. Case 1 showed cerebellar ataxia at the age of 58 years, and died at 66 years. Case 2 became symptomatic at the age of 75 years, and died at 79 years. There was a 17-year difference in the age of onset between the twins. Postmortem examination revealed numerous prion protein (PrP) plaques in the brains of both cases...
October 1, 2017: Journal of Neuropathology and Experimental Neurology
https://www.readbyqxmd.com/read/28922400/protein-folding-misfolding-and-aggregation-the-importance-of-two-electron-stabilizing-interactions
#2
Andrzej Stanisław Cieplak
Proteins associated with neurodegenerative diseases are highly pleiomorphic and may adopt an all-α-helical fold in one environment, assemble into all-β-sheet or collapse into a coil in another, and rapidly polymerize in yet another one via divergent aggregation pathways that yield broad diversity of aggregates' morphology. A thorough understanding of this behaviour may be necessary to develop a treatment for Alzheimer's and related disorders. Unfortunately, our present comprehension of folding and misfolding is limited for want of a physicochemical theory of protein secondary and tertiary structure...
2017: PloS One
https://www.readbyqxmd.com/read/28912682/extracellular-vesicles-in-brain-tumors-and-neurodegenerative-diseases
#3
REVIEW
Federica Ciregia, Andrea Urbani, Giuseppe Palmisano
Extracellular vesicles (EVs) can be classified into apoptotic bodies, microvesicles (MVs), and exosomes, based on their origin or size. Exosomes are the smallest and best characterized vesicles which derived from the endosomal system. These vesicles are released from many different cell types including neuronal cells and their functions in the nervous system are investigated. They have been proposed as novel means for intercellular communication, which takes part not only to the normal neuronal physiology but also to the transmission of pathogenic proteins...
2017: Frontiers in Molecular Neuroscience
https://www.readbyqxmd.com/read/28861793/insights-into-mechanisms-of-transmission-and-pathogenesis-from-transgenic-mouse-models-of-prion-diseases
#4
Julie A Moreno, Glenn C Telling
Prions represent a new paradigm of protein-mediated information transfer. In the case of mammals, prions are the cause of fatal, transmissible neurodegenerative diseases, sometimes referred to as transmissible spongiform encephalopathies (TSEs), which frequently occur as epidemics. An increasing body of evidence indicates that the canonical mechanism of conformational corruption of cellular prion protein (PrP(C)) by the pathogenic isoform (PrP(Sc)) that is the basis of prion formation in TSEs is common to a spectrum of proteins associated with various additional human neurodegenerative disorders, including the more common Alzheimer's and Parkinson's diseases...
2017: Methods in Molecular Biology
https://www.readbyqxmd.com/read/28852189/production-of-monoclonal-antibodies-to-pathologic-%C3%AE-sheet-oligomeric-conformers-in-neurodegenerative-diseases
#5
Fernando Goñi, Mitchell Martá-Ariza, Daniel Peyser, Krystal Herline, Thomas Wisniewski
We describe a novel approach to produce conformational monoclonal antibodies selected to specifically react with the β-sheet secondary structure of pathological oligomeric conformers, characteristic of many neurodegenerative diseases. Contrary to past and current efforts, we utilize a mammalian non-self-antigen as an immunogen. The small, non-self peptide selected was covalently polymerized with glutaraldehyde until it reached a high β-sheet secondary structure content, and species between 10-100kDa that are immunogenic, stable and soluble (p13Bri)...
August 29, 2017: Scientific Reports
https://www.readbyqxmd.com/read/28842494/cellular-prion-protein-targets-amyloid-%C3%AE-fibril-ends-via-its-c-terminal-domain-to-prevent-elongation
#6
Erin Bove-Fenderson, Ryo Urano, John E Straub, David A Harris
Oligomeric forms of the amyloid-β (Aβ) peptide are thought to represent the primary synaptotoxic species underlying the neurodegenerative changes seen in Alzheimer's disease. It has been proposed that the cellular prion protein (PrP(C)) functions as a cell-surface receptor, which binds to Aβ oligomers and transduces their toxic effects. However, the molecular details of the PrP(C)-Aβ interaction remain uncertain. Here, we investigated the effect of PrP(C) on polymerization of Aβ under rigorously controlled conditions in which Aβ converts from a monomeric to a fibrillar state via a series of kinetically defined steps...
August 23, 2017: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/28842420/conditional-deletion-of-prnp-rescues-behavioral-and-synaptic-deficits-after-disease-onset-in-transgenic-alzheimer-s-disease
#7
Santiago V Salazar, Christopher Gallardo, Adam C Kaufman, Charlotte S Herber, Laura T Haas, Sophie Robinson, Jean C Manson, Michael K Lee, Stephen M Strittmatter
Biochemical and genetic evidence implicate soluble oligomeric amyloid-beta (Aβo) in triggering Alzheimer's disease (AD) pathophysiology. Moreover, constitutive deletion of the Aβo-binding cellular prion protein (PrP(C)) prevents development of memory deficits in APPswe/PS1ΔE9 mice, a model of familial AD. Here, we define the role of PrP(C) to rescue or halt established AD endophenotypes in a therapeutic disease-modifying time window after symptom onset. Deletion of Prnp at either 12 or 16 months of age fully reverses hippocampal synapse loss, and completely rescues pre-existing behavioral deficits by 17 months...
August 21, 2017: Journal of Neuroscience: the Official Journal of the Society for Neuroscience
https://www.readbyqxmd.com/read/28838669/protein-misfolding-cyclic-amplification-of-infectious-prions
#8
Fabio Moda
Transmissible spongiform encephalopathies, or prion diseases, are a group of incurable disorders caused by the accumulation of an abnormally folded prion protein (PrP(Sc)) in the brain. According to the "protein-only" hypothesis, PrP(Sc) is the infectious agent able to propagate the disease by acting as a template for the conversion of the correctly folded prion protein (PrP(C)) into the pathological isoform. Recently, the mechanism of PrP(C) conversion has been mimicked in vitro using an innovative technique named protein misfolding cyclic amplification (PMCA)...
2017: Progress in Molecular Biology and Translational Science
https://www.readbyqxmd.com/read/28838656/functions-of-the-prion-protein
#9
Théo Z Hirsch, Séverine Martin-Lannerée, Sophie Mouillet-Richard
Although initially disregarded compared to prion pathogenesis, the functions exerted by the cellular prion protein PrP(C) have gained much interest over the past two decades. Research aiming at unraveling PrP(C) functions started to intensify when it became appreciated that it would give clues as to how it is subverted in the context of prion infection and, more recently, in the context of Alzheimer's disease. It must now be admitted that PrP(C) is implicated in an incredible variety of biological processes, including neuronal homeostasis, stem cell fate, protection against stress, or cell adhesion...
2017: Progress in Molecular Biology and Translational Science
https://www.readbyqxmd.com/read/28833749/amyloidogenesis-of-tau-protein
#10
REVIEW
Bartosz Nizynski, Wojciech Dzwolak, Krzysztof Nieznanski
The role of microtubule-associated protein Tau in neurodegeneration has been extensively investigated since the discovery of Tau amyloid aggregates in the brains of patients with Alzheimer's disease (AD). The process of formation of amyloid fibrils is known as amyloidogenesis and attracts much attention as a potential target in the prevention and treatment of neurodegenerative conditions linked to protein aggregation. Cerebral deposition of amyloid aggregates of Tau is observed not only in AD but also in numerous other tauopathies and prion diseases...
August 17, 2017: Protein Science: a Publication of the Protein Society
https://www.readbyqxmd.com/read/28832529/assessment-of-autophagy-in-neurons-and-brain-tissue
#11
REVIEW
Irene Benito-Cuesta, Héctor Diez, Lara Ordoñez, Francisco Wandosell
Autophagy is a complex process that controls the transport of cytoplasmic components into lysosomes for degradation. This highly conserved proteolytic system involves dynamic and complex processes, using similar molecular elements and machinery from yeast to humans. Moreover, autophagic dysfunction may contribute to a broad spectrum of mammalian diseases. Indeed, in adult tissues, where the capacity for regeneration or cell division is low or absent (e.g., in the mammalian brain), the accumulation of proteins/peptides that would otherwise be recycled or destroyed may have pathological implications...
August 23, 2017: Cells
https://www.readbyqxmd.com/read/28827536/cellular-internalization-of-alpha-synuclein-aggregates-by-cell-surface-heparan-sulfate-depends-on-aggregate-conformation-and-cell-type
#12
Elisabet Ihse, Hodaka Yamakado, Xander M van Wijk, Roger Lawrence, Jeffrey D Esko, Eliezer Masliah
Amyloid aggregates found in the brain of patients with neurodegenerative diseases, including Alzheimer's and Parkinson's disease, are thought to spread to increasingly larger areas of the brain through a prion-like seeding mechanism. Not much is known about which cell surface receptors may be involved in the cell-to-cell transfer, but proteoglycans are of interest due to their well-known propensity to interact with amyloid aggregates. In this study, we investigated the involvement of plasma membrane-bound heparan and chondroitin sulfate proteoglycans in cellular uptake of aggregates consisting of α-synuclein, a protein forming amyloid aggregates in Parkinson's disease...
August 21, 2017: Scientific Reports
https://www.readbyqxmd.com/read/28811866/preliminary-data-on-the-interaction-between-some-biometals-and-oxidative-stress-status-in-mild-cognitive-impairment-and-alzheimer-s-disease-patients
#13
Ioana-Miruna Balmuș, Stefan-Adrian Strungaru, Alin Ciobica, Mircea-Nicusor Nicoara, Romeo Dobrin, Gabriel Plavan, Cristinel Ștefănescu
Increased interest regarding the biometal mechanisms of action and the pathways in which they have regulatory roles was lately observed. Particularly, it was shown that biometal homeostasis dysregulation may lead to neurodegeneration including Alzheimer's disease, Parkinson disease, or prion protein disease, since important molecular signaling mechanisms in brain functions implicate both oxidative stress and redox active biometals. Oxidative stress could be a result of a breakdown in metal-ion homeostasis which leads to abnormal metal protein chelation...
2017: Oxidative Medicine and Cellular Longevity
https://www.readbyqxmd.com/read/28811267/app-a%C3%AE-structural-diversity-and-alzheimer-s-disease-pathogenesis
#14
REVIEW
Alex E Roher, Tyler A Kokjohn, Steven G Clarke, Michael R Sierks, Chera L Maarouf, Geidy E Serrano, Marwan S Sabbagh, Thomas G Beach
The amyloid cascade hypothesis of Alzheimer's disease (AD) proposes amyloid- β (Aβ) is a chief pathological element of dementia. AD therapies have targeted monomeric and oligomeric Aβ 1-40 and 1-42 peptides. However, alternative APP proteolytic processing produces a complex roster of Aβ species. In addition, Aβ peptides are subject to extensive posttranslational modification (PTM). We propose that amplified production of some APP/Aβ species, perhaps exacerbated by differential gene expression and reduced peptide degradation, creates a diverse spectrum of modified species which disrupt brain homeostasis and accelerate AD neurodegeneration...
August 12, 2017: Neurochemistry International
https://www.readbyqxmd.com/read/28797122/cross-seeding-of-prions-by-aggregated-%C3%AE-synuclein-leads-to-transmissible-spongiform-encephalopathy
#15
Elizaveta Katorcha, Natallia Makarava, Young Jin Lee, Iris Lindberg, Mervyn J Monteiro, Gabor G Kovacs, Ilia V Baskakov
Aggregation of misfolded proteins or peptides is a common feature of neurodegenerative diseases including Alzheimer's, Parkinson's, Huntington's, prion and other diseases. Recent years have witnessed a growing number of reports of overlap in neuropathological features that were once thought to be unique to only one neurodegenerative disorder. However, the origin for the overlap remains unclear. One possibility is that diseases with mixed brain pathologies might arise from cross-seeding of one amyloidogenic protein by aggregated states of unrelated proteins...
August 2017: PLoS Pathogens
https://www.readbyqxmd.com/read/28783058/evolution-of-diagnostic-tests-for-chronic-wasting-disease-a-naturally-occurring-prion-disease-of-cervids
#16
REVIEW
Nicholas J Haley, Jürgen A Richt
Since chronic wasting disease (CWD) was first identified nearly 50 years ago in a captive mule deer herd in the Rocky Mountains of the United States, it has slowly spread across North America through the natural and anthropogenic movement of cervids and their carcasses. As the endemic areas have expanded, so has the need for rapid, sensitive, and cost effective diagnostic tests-especially those which take advantage of samples collected antemortem. Over the past two decades, strategies have evolved from the recognition of microscopic spongiform pathology and associated immunohistochemical staining of the misfolded prion protein to enzyme-linked immunoassays capable of detecting the abnormal prion conformer in postmortem samples...
August 5, 2017: Pathogens
https://www.readbyqxmd.com/read/28768713/a-meta-analysis-and-review-examining-a-possible-role-for-oxidative-stress-and-singlet-oxygen-in-diverse-diseases
#17
REVIEW
Athinoula L Petrou, Athina Terzidaki
From kinetic data (k, T) we calculated the thermodynamic parameters for various processes (nucleation, elongation, fibrillization, etc.) of proteinaceous diseases that are related to the β-amyloid protein (Alzheimer's), to tau protein (Alzheimer's, Pick's), to α-synuclein (Parkinson's), prion, amylin (type II diabetes), and to α-crystallin (cataract). Our calculations led to ΔG(≠) values that vary in the range 92.8-127 kJ mol(-1) at 310 K. A value of ∼10-30 kJ mol(-1) is the activation energy for the diffusion of reactants, depending on the reaction and the medium...
August 2, 2017: Biochemical Journal
https://www.readbyqxmd.com/read/28762306/emerging-targets-and-latest-proteomics-based-therapeutic-approaches-in-neurodegenerative-diseases
#18
Munazza Tamkeen Fatima, Zeyaul Islam, Ejaj Ahmad, Parveen Salahuddin
Protein homeostasis (proteostasis) is achieved by the interplay among various components and pathways inside a cell. Dysfunction in proteostasis leads to protein misfolding and aggregation which is ubiquitously associated with many neurodegenerative disorders, although the exact role of these aggregate in the pathogenesis remains unknown. Many neurodegenerative diseases, including Alzheimer's disease, Parkinson's disease, Huntington's disease, amyotrophic lateral sclerosis, and others are characterized by the conversion of specific proteins aggregates into protein inclusions and/or plaques in degenerating brains...
July 31, 2017: Current Protein & Peptide Science
https://www.readbyqxmd.com/read/28760925/the-cholesterol-ester-cycle-regulates-signalling-complexes-and-synapse-damage-caused-by-amyloid-%C3%AE
#19
Ewan West, Craig Osborne, Clive Bate
Cholesterol is required for the formation and function of some signalling platforms. In synaptosomes amyloid-β (Aβ) oligomers, the causative agent in Alzheimer's disease, bind to cellular prion proteins (PrP(C)) resulting in increased cholesterol concentrations, translocation of cytoplasmic phospholipase A2 (cPLA2) to lipid rafts and activation of cPLA2 The formation of Aβ:PrP(C) complexes was controlled by the cholesterol ester cycle. Aβ activated cholesterol ester hydrolases which released cholesterol from stores of cholesterol esters and stabilised Aβ:PrP(C) complexes resulting in activated cPLA2 Conversely, cholesterol esterification reduced cholesterol concentrations causing the dispersal of Aβ:PrP(C) complexes...
July 31, 2017: Journal of Cell Science
https://www.readbyqxmd.com/read/28758631/statins-are-ineffective-at-reducing-neuroinflammation-or-prolonging-survival-in-scrapie-infected-mice
#20
James A Carroll, Brent Race, Katie Phillips, James F Striebel, Bruce Chesebro
Neuroinflammation is a prominent component of several neurodegenerative diseases, including multiple sclerosis, Alzheimer's disease, Parkinson's disease, tauopathies, amyotrophic lateral sclerosis and prion diseases. In such conditions, the ability to decrease neuroinflammation by drug therapy may influence disease progression. Statins have been used to treat hyperlipidemia as well as reduce neuroinflammation and oxidative stress in various tissues. In previous studies, treatment of scrapie-infected mice with the type 1 statins, simvastatin or pravastatin, showed a small beneficial effect on survival time...
August 2017: Journal of General Virology
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