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November 16, 2017: Prion
Beata Sikorska, Agata Gajos, Andrzej Bogucki, Emil Zielonka Christina Sigurdson, Pawel P Liberski
We report here on the ultrastructure of amyloid plaques in chronic wasting disease (CWD) transmitted to Tg20 transgenic mice overexpressing prion protein (PrP(c)). We identified three main types of amyloid deposits in mCWD: large amyloid deposits, unicentric plaques similar to kuru plaques in human prion diseases and multicentric plaques reminiscent of plaques typical of GSS. The most unique type of plaques were large subpial amyloid deposits. They were composed of large areas of amyloid fibrils but did not form "star-like" appearances of unicentric plaques...
November 6, 2017: Prion
Dimitri Renard, Giovanni Castelnovo, Laurent Collombier, Eric Thouvenot, Vincent Boudousq
OBJECTIVE: To assess the relationship between clinical pattern and cerebral glucose metabolism on [18F]fluoro-2-deoxy-D-glucose positron emission tomography (FDG-PET) in Creutzfeldt-Jakob disease (CJD). METHODS: Predefined clinical signs (ataxia, visual, pyramidal, myoclonus, limb apraxia, limb dystonia, sensory, parkinsonism, and corticobasal syndrome [CBS]) and FDG-PET data were assessed in consecutive CJD patients. Two types of statistical parametric mapping (SPM) analyses, using stringent level of significance p<0...
November 3, 2017: Prion
Suehiro Sakaguchi, Keiji Uchiyama
Conformational conversion of the cellular prion protein, PrP(C), into the abnormally folded isoform of prion protein, PrP(Sc), which leads to marked accumulation of PrP(Sc) in brains, is a key pathogenic event in prion diseases, a group of fatal neurodegenerative disorders caused by prions. However, the exact mechanism of PrP(Sc) accumulation in prion-infected neurons remains unknown. We recently reported a novel cellular mechanism to support PrP(Sc) accumulation in prion-infected neurons, in which PrP(Sc) itself promotes its accumulation by evading the cellular inhibitory mechanism, which is newly identified in our recent study...
November 3, 2017: Prion
Sireesha Manne, Naveen Kondru, Tracy Nichols, Aaron Lehmkuhl, Bruce Thomsen, Rodger Main, Patrick Halbur, Somak Dutta, Anumantha G Kanthasamy
Prion diseases are transmissible spongiform encephalopathies (TSEs) characterized by fatal, progressive neurologic diseases with prolonged incubation periods and an accumulation of infectious misfolded prion proteins. Antemortem diagnosis is often difficult due to a long asymptomatic incubation period, differences in the pathogenesis of different prions, and the presence of very low levels of infectious prion in easily accessible samples. Chronic wasting disease (CWD) is a TSE affecting both wild and captive populations of cervids, including mule deer, white-tailed deer, elk, moose, muntjac, and most recently, wild reindeer...
November 3, 2017: Prion
Tae-Young Suh, In Soon Roh, Hyo-Jin Kim, Peter C Griffiths, Kyung Je Park, Hoo Chang Park, James Hope, Hae Eun Kang, Dae-Yong Kim, Hyun Joo Sohn
M2B cells with persistent classical bovine spongiform encephalopathy (C-BSE) have been established previously. In this study, we performed strain characterization of the M2B cell line in bovine PrP(C) overexpressing mice (Tg 1896). Mice intracranially inoculated with M2B cells and C-BSE survived for 451 ± 7 and 465 ± 31 d post inoculation, respectively. Although biochemical properties, including deglycosylation and conformational stability, differed between M2B cells and C-BSE, inoculation with M2B cell lysate and C-BSE resulted in comparable phenotypes...
November 3, 2017: Prion
Ricardo Krause Martinez de Souza, Nalini Drieli Josviak, Meire Silva Batistela, Paulo Sergio Faro Santos, Michele Christine Landemberger, Ricardo Ramina
Here, we report the first case of V180I rare mutation in a Brazilian woman whose clinical condition started with memory impairment for recent events and insomnia with 2 months of evolution, without any other alterations in neurological examination. Both the electroencephalogram (EEG) and the routine biochemical examination of cerebrospinal fluid (CSF) were normal. CSF 14-3-3 protein search was positive. Magnetic resonance imaging (MRI) of the encephalon showed findings suggestive of Creutzfeldt-Jakob disease, confirmed by sequencing of PRNP gene that reveal V180I mutation also homozygosity for methionine at codon 129 (M129M)...
November 2, 2017: Prion
Yuichi Hayashi
No abstract text is available yet for this article.
November 2, 2017: Prion
James Alibhai, Abigail Diack, Jean Manson
Chronic neurodegenerative diseases, such as prion diseases or Alzheimer's disease, are associated with progressive accumulation of host proteins which misfold and aggregate. Neurodegeneration is restricted to specific neuronal populations which show clear accumulation of misfolded proteins, whilst neighbouring neurons remain unaffected. Such data raise interesting questions about the vulnerability of specific neuronal populations to neurodegeneration and much research has concentrated only on the mechanisms of neurodegeneration in afflicted neuronal populations...
October 12, 2017: Prion
Yuichi Hayashi, Megumi Yamada, Akio Kimura, Takahiko Asano, Katsuya Satoh, Tetsuyuki Kitamoto, Maokoto Yoneda, Takashi Inuzuka
We report the case of a 76-year-old woman presenting with 47-month history of progressive dementia and cortical blindness with no family history. Antibodies against thyroid glands and the N-terminus of α-enolase (NAE) were detected in her serum. Neurological examination revealed progressive dementia, frontal signs, visual disturbance, and exaggerated bilateral tendon reflexes in both legs. Diffusion MRI showed cortical hyper-intensities in the bilateral occipital and parietal, and the left frontal and temporal cortices...
October 2, 2017: Prion
Alex J McDonald, Bei Wu, David A Harris
The normal function of PrP(C), the cellular prion protein, has remained mysterious since its first description over 30 years ago. Amazingly, although complete deletion of the gene encoding PrP(C) has little phenotypic consequence, expression in transgenic mice of PrP molecules carrying certain internal deletions produces dramatic neurodegenerative phenotypes. In our recent paper, (1) we have demonstrated that the flexible, N-terminal domain of PrP(C) possesses toxic effector functions, which are regulated by a docking interaction with the structured, C-terminal domain...
September 29, 2017: Prion
Pardis Tabaee Damavandi, Martin T Dove, Richard W Pickersgill
BACKGROUND: Sporadic fatal insomnia (sFI) is a rapid progressive neurodegenerative disease characterised by gradual to perpetual insomnia, followed by dysautonomia, coma and death. (1) The cause of sFI was recently mapped to a mutation in a protein, the prion, found in the human brain. It is the unfolding of the prion that leads to the generation of toxic oligomers that destroy brain tissue and function. Recent studies have confirmed that a methionine mutation at codon 129 of the human Prion is characteristic of sFI...
September 3, 2017: Prion
Ryan Taschuk, Erin Scruten, Murray Woodbury, Neil Cashman, Andrew Potter, Philip Griebel, Suresh K Tikoo, Scott Napper
The ongoing epidemic of chronic wasting disease (CWD) within cervid populations indicates the need for novel approaches for disease management. A vaccine that either reduces susceptibility to infection or reduces shedding of prions by infected animals, or a combination of both, could be of benefit for disease control. The development of such a vaccine is challenged by the unique nature of prion diseases and the requirement for formulation and delivery in an oral format for application in wildlife settings. To address the unique nature of prions, our group targets epitopes, termed disease specific epitopes (DSEs), whose exposure for antibody binding depends on disease-associated misfolding of PrP(C) into PrP(Sc)...
September 3, 2017: Prion
Douglas R Lyke, Anita L Manogaran
Prions are misfolded, aggregated, infectious proteins found in a range of organisms from mammals to bacteria. In mammals, prion formation is difficult to study because misfolding and aggregation take place prior to symptom presentation. The study of the yeast prion [PSI(+)], which is the misfolded infectious form of Sup35p, provides a tractable system to monitor prion formation in real time. Recently, we showed that the de novo formation of prion aggregates begins with the appearance of highly mobile cytoplasmic foci, called early foci, which assemble into larger ring or dot structures...
September 3, 2017: Prion
Ren-Qing Zhang, Cao Chen, Li-Jie Xiao, Jing Sun, Yue Ma, Xiao-Dong Yang, Xiao-Feng Xu, Kang Xiao, Qi Shi, Zhi-Bao Chen, Xiao-Ping Dong
The aberrant alterations of calmodulin (CaM) and its downstream substrates have been reported in some neurodegenerative diseases, but rarely described in prion disease. In this study, the potential changes of Ca(2+)/CaM and its associated agents in the brains of scrapie agent 263K-infected hamsters and the prion infected cell line SMB-S15 were evaluated by various methodologies. We found that the level of CaM in the brains of 263K-infected hamsters started to increase at early stage and maintained at high level till terminal stage...
September 3, 2017: Prion
K S Antonets, A A Nizhnikov
Amyloids represent protein fibrils that have highly ordered structure with unique physical and chemical properties. Amyloids have long been considered lethal pathogens that cause dozens of incurable diseases in humans and animals. Recent data show that amyloids may not only possess pathogenic properties but are also implicated in the essential biological processes in a variety of prokaryotes and eukaryotes. Functional amyloids have been identified in archaea, bacteria, fungi, and animals, including humans. Plants are one of the most poorly studied groups of organisms in the field of amyloid biology...
September 3, 2017: Prion
Marie C Lechler, Della C David
Low complexity (LC) prion-like domains are over-represented among RNA-binding proteins (RBPs) and contribute to the dynamic nature of RNA granules. Importantly, several neurodegenerative diseases are characterized by cytoplasmic "solid" aggregates formed by mainly nuclear RBPs harboring LC prion-like domains. Although RBP aggregation in disease has been extensively characterized, it remains unknown how the process of aging disturbs RBP dynamics. Our recent study revealed that RNA granule components including 2 key stress granule RBPs with LC prion-like domains, PAB-1 and TIAR-2, aggregate in aged Caenorhabditis elegans in the absence of disease...
September 3, 2017: Prion
Cao Chen, Xiao-Feng Xu, Ren-Qing Zhang, Yue Ma, Yan Lv, Jian-Le Li, Qiang Shi, Kang Xiao, Jing Sun, Xiao-Dong Yang, Qi Shi, Xiao-Ping Dong
α1-Antichymotrypsin (α1-ACT) belongs to a kind of acute-phase inflammatory protein. Recently, such protein has been proved exist in the amyloid deposits which is the hallmark of Alzheimer's disease, but limitedly reported in prion disease. To estimate the change of α1-ACT during prion infection, the levels of α1-ACT in the brain tissues of scrapie agents 263K-, 139A- and ME7-infected rodents were analyzed, respectively. Results shown that α1-ACT levels were significantly increased in the brain tissues of the three kinds of scrapie-infected rodents, displaying a time-dependent manner during prion infection...
September 3, 2017: Prion
Sean M Cascarina, Kacy R Paul, Eric D Ross
Considerable advances in understanding the protein features favoring prion formation in yeast have facilitated the development of effective yeast prion prediction algorithms. Here we discuss a recent study in which we systematically explored the utility of the yeast prion prediction algorithm PAPA for designing mutations to modulate the aggregation activity of the human prion-like protein hnRNPA2B1. Mutations in hnRNPA2B1 cause multisystem proteinopathy in humans, and accelerate aggregation of the protein in vitro...
September 3, 2017: Prion
Yoshifumi Iwamaru, Candace K Mathiason, Glenn C Telling, Edward A Hoover
A possible strategy to develop more diverse cell culture systems permissive to infection with naturally occurring prions is to exploit culture of neurospheres from transgenic mice expressing the normal prion protein (PrP) of the native host species. Accordingly, we developed differentiated neurosphere cultures from the cervid PrP-expressing mice to investigate whether this in vitro system would support replication of non-adapted cervid-origin chronic wasting disease (CWD) prions. Here we report the successful amplification of disease-associated PrP in differentiated neurosphere cultures within 3 weeks after exposure to CWD prions from both white-tailed deer or elk...
July 4, 2017: Prion
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