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https://www.readbyqxmd.com/read/28194643/ultra-efficient-amplification-of-abnormal-prion-protein-by-modified-protein-misfolding-cyclic-amplification-with-electric-current
#1
Jeong-Ho Park, Yeong-Gon Choi, Seok-Joo Park, Hong-Seok Choi, Eun-Kyoung Choi, Yong-Sun Kim
Prion diseases are clinically diagnosed and confirmed upon post-mortem histopathological examination of brain tissue. The only reliable molecular marker for prion diseases is abnormal prion protein (PrPSc), a pathologically conformed prion protein that primarily accumulates in the central nervous system and to a lesser extent in lymphoreticular tissues. However, the use of PrPSc as a marker for preclinical diagnoses is limited because the concentration of PrPSc in easily accessible body fluids is extremely low...
February 13, 2017: Molecular Neurobiology
https://www.readbyqxmd.com/read/28193724/neurodegenerative-disease-transmission-and-transgenesis-in-mice
#2
Brittany N Dugger, Daniel P Perl, George A Carlson
Although the discovery of the prion protein (PrP) resulted from its co-purification with scrapie infectivity in Syrian hamsters, work with genetically defined and genetically modified mice proved crucial for understanding the fundamental processes involved not only in prion diseases caused by PrP misfolding, aggregation, and spread but also in other, much more common, neurodegenerative brain diseases. In this review, we focus on methodological and conceptual approaches used to study scrapie and related PrP misfolding diseases in mice and how these approaches have advanced our understanding of related disorders including Alzheimer's and Parkinson's disease...
February 13, 2017: Cold Spring Harbor Perspectives in Biology
https://www.readbyqxmd.com/read/28178353/cystatin-f-is-a-biomarker-of-prion-pathogenesis-in-mice
#3
Mario Nuvolone, Nicolas Schmid, Gino Miele, Silvia Sorce, Rita Moos, Christian Schori, Roger R Beerli, Monika Bauer, Philippe Saudan, Klaus Dietmeier, Ingolf Lachmann, Michael Linnebank, Roland Martin, Ulf Kallweit, Veronika Kana, Elisabeth J Rushing, Herbert Budka, Adriano Aguzzi
Misfolding of the cellular prion protein (PrPC) into the scrapie prion protein (PrPSc) results in progressive, fatal, transmissible neurodegenerative conditions termed prion diseases. Experimental and epidemiological evidence point toward a protracted, clinically silent phase in prion diseases, yet there is no diagnostic test capable of identifying asymptomatic individuals incubating prions. In an effort to identify early biomarkers of prion diseases, we have compared global transcriptional profiles in brains from pre-symptomatic prion-infected mice and controls...
2017: PloS One
https://www.readbyqxmd.com/read/28154522/metal-dyshomeostasis-and-their-pathological-role-in-prion-and-prion-like-diseases-the-basis-for-a-nutritional-approach
#4
REVIEW
Mattia Toni, Maria L Massimino, Agnese De Mario, Elisa Angiulli, Enzo Spisni
Metal ions are key elements in organisms' life acting like cofactors of many enzymes but they can also be potentially dangerous for the cell participating in redox reactions that lead to the formation of reactive oxygen species (ROS). Any factor inducing or limiting a metal dyshomeostasis, ROS production and cell injury may contribute to the onset of neurodegenerative diseases or play a neuroprotective action. Transmissible spongiform encephalopathies (TSEs), also known as prion diseases, are a group of fatal neurodegenerative disorders affecting the central nervous system (CNS) of human and other mammalian species...
2017: Frontiers in Neuroscience
https://www.readbyqxmd.com/read/28144628/de-novo-generation-of-a-unique-cervid-prion-strain-using-protein-misfolding-cyclic-amplification
#5
Crystal Meyerett-Reid, A Christy Wyckoff, Terry Spraker, Bruce Pulford, Heather Bender, Mark D Zabel
Substantial evidence supports the hypothesis that prions are misfolded, infectious, insoluble, and protease-resistant proteins (PrP(RES)) devoid of instructional nucleic acid that cause transmissible spongiform encephalopathies (TSEs). Protein misfolding cyclic amplification (PMCA) has provided additional evidence that PrPRes acts as a template that can convert the normal cellular prion protein (PrP(C)) present in uninfected normal brain homogenate (NBH) into the infectious misfolded PrP(RES) isoform. Human PrP(C) has been shown to spontaneously convert to a misfolded pathological state causing sporadic Creutzfeldt-Jakob disease (sCJD)...
January 2017: MSphere
https://www.readbyqxmd.com/read/28118747/in-silico-strategies-on-prion-pathogenic-conversion-and-inhibition-from-prp-c-prp-sc
#6
Nataraj S Pagadala, Khajamohiddin Syed, Rakesh Bhat
To date, various therapeutic strategies identified numerous anti-prion compounds and antibodies that stabilize PrP(C), block the conversion of PrP(C)-PrP(Sc) and increased effect on PrP(Sc) clearance. However, no suitable drug has been identified clinically so far due to the poor oral absorption, low blood-brain-barrier [BBB] penetration, and high toxicity. Although some of the drugs were proven to be effective in prion-infected cell culture and whole animal models, none of them increased the rate of survival compared to placebo...
February 2, 2017: Expert Opinion on Drug Discovery
https://www.readbyqxmd.com/read/28116677/a-heparin-purification-process-removes-spiked-transmissible-spongiform-encephalopathy-agent
#7
Cyrus Bett, Ksenija Grgac, Dianna Long, Michael Karfunkle, David A Keire, David M Asher, Luisa Gregori
In 2000, bovine heparin was withdrawn from the US market for fear of contamination with bovine spongiform encephalopathy (BSE) agent, the cause of variant Creutzfeldt-Jakob disease in humans. Thus, US heparin is currently sourced only from pig intestines. Availability of alternative sources of crude heparin, a life-saving drug, would benefit public health. Bovine heparin is an obvious option, but BSE clearance by the bovine heparin manufacturing process should be evaluated. To this end, using hamster 263K scrapie as a surrogate for BSE agent, we applied a four-step bench-scale heparin purification protocol resembling a typical heparin manufacturing process to investigate removal of the spiked scrapie agent...
January 23, 2017: AAPS Journal
https://www.readbyqxmd.com/read/28112164/divergent-prion-strain-evolution-driven-by-prp-c-expression-level-in-transgenic-mice
#8
Annick Le Dur, Thanh Lan Laï, Marie-George Stinnakre, Aude Laisné, Nathalie Chenais, Sabine Rakotobe, Bruno Passet, Fabienne Reine, Solange Soulier, Laetitia Herzog, Gaëlle Tilly, Human Rézaei, Vincent Béringue, Jean-Luc Vilotte, Hubert Laude
Prions induce a fatal neurodegenerative disease in infected host brain based on the refolding and aggregation of the host-encoded prion protein PrP(C) into PrP(Sc). Structurally distinct PrP(Sc) conformers can give rise to multiple prion strains. Constrained interactions between PrP(C) and different PrP(Sc) strains can in turn lead to certain PrP(Sc) (sub)populations being selected for cross-species transmission, or even produce mutation-like events. By contrast, prion strains are generally conserved when transmitted within the same species, or to transgenic mice expressing homologous PrP(C)...
January 23, 2017: Nature Communications
https://www.readbyqxmd.com/read/28109330/the-structure-of-mammalian-prions-and-their-aggregates
#9
E Vázquez-Fernández, H S Young, J R Requena, H Wille
Prion diseases, such as Creutzfeldt-Jakob disease in humans, bovine spongiform encephalopathy in cattle, chronic wasting disease in cervids (i.e., deer, elk, moose, and reindeer), and sheep scrapie, are caused by the misfolding of the cellular prion protein (PrP(C)) into a disease-causing conformer (PrP(Sc)). PrP(C) is a normal, GPI-anchored protein that is expressed on the surface of neurons and other cell types. The structure of PrP(C) is well understood, based on studies of recombinant PrP, which closely mimics the structure of native PrP(C)...
2017: International Review of Cell and Molecular Biology
https://www.readbyqxmd.com/read/28102071/temperature-induced-misfolding-in-prion-protein-evidence-of-multiple-partially-disordered-states-stabilized-by-non-native-hydrogen-bonds
#10
Neharika G Chamachi, Suman Chakrabarty
The structural basis of pathways of misfolding of a cellular prion (PrP(C)) into the toxic scrapie form (PrP(SC)) and identification of possible intermediates (e.g., PrP*) still eludes us. In this work, we have used a cumulative ∼65 μs of replica exchange molecular dynamics simulation data to construct the conformational free energy landscapes and capture the structural and thermodynamic characteristics associated with various stages of the thermal denaturation process in human prion protein. The temperature-dependent free energy surfaces consist of multiple metastable states stabilized by non-native contacts and hydrogen bonds, thus rendering the protein prone to misfolding...
February 2, 2017: Biochemistry
https://www.readbyqxmd.com/read/28091514/novel-strain-properties-distinguishing-sporadic-prion-diseases-sharing-prion-protein-genotype-and-prion-type
#11
Laura Cracco, Silvio Notari, Ignazio Cali, Man-Sun Sy, Shu G Chen, Mark L Cohen, Bernardino Ghetti, Brian S Appleby, Wen-Quan Zou, Byron Caughey, Jiri G Safar, Pierluigi Gambetti
In most human sporadic prion diseases the phenotype is consistently associated with specific pairings of the genotype at codon 129 of the prion protein gene and conformational properties of the scrapie PrP (PrP(Sc)) grossly identified types 1 and 2. This association suggests that the 129 genotype favours the selection of a distinct strain that in turn determines the phenotype. However, this mechanism cannot play a role in the phenotype determination of sporadic fatal insomnia (sFI) and a subtype of sporadic Creutzfeldt-Jakob disease (sCJD) identified as sCJDMM2, which share 129 MM genotype and PrP(Sc) type 2 but are associated with quite distinct phenotypes...
January 16, 2017: Scientific Reports
https://www.readbyqxmd.com/read/28072756/rapid-testing-for-creutzfeldt-jakob-disease-in-donors-of-cornea
#12
Luisa Gregori, Arthur Serer, Kristy L McDowell, Juraj Cervenak, David M Asher
BACKGROUND: Creutzfeldt-Jakob disease (CJD) has been accidentally transmitted by contaminated corneal transplants. Eye donors are not ordinarily tested for CJD, in part because an easy test is not available. We propose a relatively simple postmortem procedure to collect brain samples without performing full autopsy and show that a test currently marketed for veterinary diagnosis would offer an effective screening test. METHODS: We selected 6 brains from confirmed cases of human sporadic CJD and sampled each in triplicate (18 specimens), 28 control brains of individuals with non-CJD neurodegenerative diseases and 10 normal brains...
January 9, 2017: Transplantation
https://www.readbyqxmd.com/read/28068881/eu-approved-rapid-tests-might-underestimate-bovine-spongiform-encephalopathy-infection-in-goats
#13
Daniela Meloni, Elena Bozzetta, Jan P M Langeveld, Martin H Groschup, Wilfred Goldmann, Olivier Andrèoletti, Isabelle Lantier, Lucien Van Keulen, Alex Bossers, Danilo Pitardi, Romolo Nonno, Theodoros Sklaviadis, Francesco Ingravalle, Simone Peletto, Silvia Colussi, Pier Luigi Acutis
We report the diagnostic sensitivity of 3 EU-approved rapid tests (ELISAs; 1 from IDEXX and 2 from Bio-Rad) for the detection of transmissible spongiform encephalopathy diseases in goats. Ninety-eight goat brainstem samples were tested. All the rapid tests had 100% specificity and ≥80% sensitivity, with the IDEXX test significantly more sensitive than the 2 Bio-Rad tests. All tests detected 100% of samples from goats with clinical scrapie, but missed 8% (IDEXX) to 33% (Bio-Rad SG) of samples from preclinical goats...
January 1, 2017: Journal of Veterinary Diagnostic Investigation
https://www.readbyqxmd.com/read/28063003/effect-of-poly-l-arginine-in-inhibiting-scrapie-prion-protein-of-cultured-cells
#14
Muhammad Waqas, Hye-Mi Lee, Jeeyoung Kim, Glenn Telling, Jin-Ki Kim, Dae-Hwan Kim, Chongsuk Ryou
Biological effect of poly-L-arginine (PLR), the linear homopolymer comprised of L-arginine, was investigated to determine the activity of suppressing prions. PLR decreased the level of scrapie prion protein (PrP(Sc)) in cultured cells permanently infected with prions in a concentration-dependent manner. The PrP(Sc) inhibition efficacy of PLR was greater than that of another prion-suppressant poly-L-lysine (PLK) in a molecular mass-dependent fashion. The effective concentration of PLR to inhibit prions was achieved safely below the cytotoxic concentrations, and overall cytotoxicity of PLR was similar to that of PLK...
January 7, 2017: Molecular and Cellular Biochemistry
https://www.readbyqxmd.com/read/28030950/mechanism-of-unfolding-of-human-prion-protein
#15
Reman K Singh, Neharika G Chamachi, Suman Chakrabarty, Arnab Mukherjee
Misfolding and aggregation of prion proteins are associated with several neurodegenerative diseases. Therefore, understanding the mechanism of the misfolding process is of enormous interest in the scientific community. It has been speculated and widely discussed that the native cellular prion protein (PrP(C)) form needs to undergo substantial unfolding to a more stable PrP(C*) state, which may further oligomerize into the toxic scrapie (PrP(Sc)) form. Here, we have studied the mechanism of the unfolding of the human prion protein (huPrP) using a set of extensive well-tempered metadynamics simulations...
January 13, 2017: Journal of Physical Chemistry. B
https://www.readbyqxmd.com/read/27998976/sialylation-controls-prion-fate-in-vivo
#16
Saurabh Srivastava, Elizaveta Katorcha, Martin L Daus, Peter Lasch, Michael Beekes, Ilia V Baskakov
Prions or PrP(Sc) are proteinaceous infectious agents that consist of misfolded, self-replicating states of a sialoglycoprotein called the prion protein or PrP(C) The current work tests a new hypothesis that sialylation determines the fate of prions in an organism. To begin, we produced control PrP(Sc) from PrP(C) using Protein Misfolding Cyclic Amplification (PMCAb), and also generated PrP(Sc) with reduced sialylation levels using the same method but with partially desialylated PrP(C) as a substrate (dsPMCAb)...
December 20, 2016: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/27991723/comparative-proteomics-analyses-for-139a-and-me7-scrapie-infected-mice-brains-in-the-middle-and-terminal-stages
#17
Qi Shi, Li-Na Chen, Yan Lv, Bao-Yun Zhang, Kang Xiao, Wei Zhou, Cao Chen, Jing Sun, Xiao-Dong Yang, Xiao-Ping Dong
PURPOSE: To analyze the proteomics patterns in the cortex regions of scrapie strains 139A- and ME7-infected mice collected in the middle and terminal stages. EXPERIMENTAL DESIGN: Western Blot and immunohistochemistry methods are used to analyze the pathological changes in mice collected in the middle and terminal stages. The technique of iTRAQ and multidimensional LC and MS are used to analyze the proteomics patterns of mice in different stages. RESULTS: In total, 2891 with 95% confidence interval are identified...
December 19, 2016: Proteomics. Clinical Applications
https://www.readbyqxmd.com/read/27959866/quiescin-sulfhydryl-oxidase-inhibits-prion-formation-in-vitro
#18
Yi-An Zhan, Romany Abskharon, Yu Li, Jue Yuan, Liang Zeng, Johnny Dang, Manuel Camacho Martinez, Zerui Wang, Jacqueline Mikol, Sylvain Lehmann, Shizhong Bu, Jan Steyaert, Li Cui, Robert B Petersen, Qingzhong Kong, Gong-Xiang Wang, Alexandre Wohlkonig, Wen-Quan Zou
Prions are infectious proteins that cause a group of fatal transmissible diseases in animals and humans. The scrapie isoform (PrP(Sc)) of the cellular prion protein (PrP(C)) is the only known component of the prion. Several lines of evidence have suggested that the formation and molecular features of PrP(Sc) are associated with an abnormal unfolding/refolding process. Quiescin-sulfhydryl oxidase (QSOX) plays a role in protein folding by introducing disulfides into unfolded reduced proteins. Here we report that QSOX inhibits human prion propagation in protein misfolding cyclic amplification reactions and murine prion propagation in scrapie-infected neuroblastoma cells...
December 11, 2016: Aging
https://www.readbyqxmd.com/read/27959774/increased-circulating-micrornas-mir-342-3p-and-mir-21-5p-in-natural-sheep-prion-disease
#19
David Sanz Rubio, Óscar López-Pérez, Alvaro de Andrés Pablo, Rosa Bolea, Rosario Osta, Juan J Badiola, Pilar Zaragoza, Inmaculada Martín-Burriel, Janne M Toivonen
Scrapie is a transmissible spongiform encephalopathy (TSE), or prion disease, of sheep and goats. As no simple diagnostic tests are yet available to detect TSEs in vivo, easily accessible biomarkers could facilitate the eradication of scrapie agents from the food chain. To this end, we analysed by quantitative RT-PCR a selected set of candidate microRNAs (miRNAs) from circulating blood plasma of naturally infected, classical scrapie sheep that demonstrated clear scrapie symptoms and pathology. Significant scrapie-associated increase was repeatedly found for miR-342-3p and miR-21-5p...
December 13, 2016: Journal of General Virology
https://www.readbyqxmd.com/read/27936597/quantitating-prp-polymorphisms-present-in-prions-from-heterozygous-scrapie-infected-sheep
#20
Christopher J Silva, Melissa L Erickson-Beltran, Colleen Hui, Juan José Badiola, Eric M Nicholson, Jesus Rodriguez Requena, Rosa Bolea
Scrapie is a prion (PrP(Sc)) disease of sheep. The incubation period of sheep scrapie is strongly influenced by polymorphisms at positions 136, 154, and 171 of a sheep's normal cellular prion protein (PrP(C)). Chymotrypsin was used to digest sheep recombinant PrP to identify a set of characteristic peptides [M132LGS<u>X</u>MSRPL141 (X = A or V), Y153<u>X</u>ENMY158 (X= H or R), and Y166RPVD<u>X</u>Y172 (X = H, K, Q, or R)] that could be used to detect and quantitate polymorphisms at positions 136, 154, and 171 of sheep PrP(C) or PrP(Sc)...
December 11, 2016: Analytical Chemistry
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