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alzheimer's disease prion diseases

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https://www.readbyqxmd.com/read/28211008/injected-amyloid-beta-in-the-olfactory-bulb-transfers-to-other-brain-regions-via-neural-connections-in-mice
#1
Baixuan He, Minying Zheng, Qiang Liu, Zhe Shi, Simei Long, Xilin Lu, Zhong Pei, Ti-Fei Yuan, Huanxing Su, Xiaoli Yao
Alzheimer's disease (AD) is characterized by progressive neuronal degeneration and pathological accumulation of amyloid plaques in the brain. It has been proposed that the prion-like spreading of amyloid beta (Aβ) protein could contribute to the progression of the disease. Olfactory bulb (OB) is one of the earliest brain regions affected in AD and olfaction is easily impaired prior to cognitive symptoms. However, it remains unclear whether Aβ accumulation in the OB would spread along olfactory projections to other connected brain regions and trigger further neurodegeneration...
February 16, 2017: Molecular Neurobiology
https://www.readbyqxmd.com/read/28193770/%C3%AE-amyloid-prions-and-the-pathobiology-of-alzheimer-s-disease
#2
Joel C Watts, Stanley B Prusiner
Alzheimer's disease (AD) is the most common neurodegenerative disease in humans and will pose a considerable challenge to healthcare systems in the coming years. Aggregation of the β-amyloid (Aβ) peptide within the brain is thought to be an initiating event in AD pathogenesis. Many recent studies in transgenic mice have provided evidence that Aβ aggregates become self-propagating during disease, leading to a cascade of protein aggregation in the brain, which may underlie the progressive nature of AD. The ability to self-propagate and the existence of distinct "strains" reveals that Aβ aggregates exhibit many properties indistinguishable from those of prions composed of PrP(Sc) proteins...
February 13, 2017: Cold Spring Harbor Perspectives in Medicine
https://www.readbyqxmd.com/read/28193724/neurodegenerative-disease-transmission-and-transgenesis-in-mice
#3
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
#4
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/28164765/commonalities-in-biological-pathways-genetics-and-cellular-mechanism-between-alzheimer-disease-and-other-neurodegenerative-diseases-an-in-silico-updated-overview
#5
Khurshid Ahmad, Mohammad Hassan Baig, Gohar Mushtaq, Mohammad Amjad Kamal, Nigel H Greig, Inho Choi
Alzheimer's disease (AD) is the most common and well-studied neurodegenerative disease (ND). Biological pathways, pathophysiology and genetics of AD show commonalities with other NDs viz. Parkinson's disease (PD), Amyotrophic lateral sclerosis (ALS), Huntington's disease (HD), Prion Disease and Dentatorubral-pallidoluysian atrophy (DRPLA). Many of the NDs, sharing the common features and molecular mechanisms suggests that pathology may be directly comparable and be implicated in disease prevention and development of highly effective therapies...
February 3, 2017: Current Alzheimer Research
https://www.readbyqxmd.com/read/28159831/prion-like-protein-aggregates-and-type-2-diabetes
#6
Abhisek Mukherjee, Claudio Soto
Type 2 diabetes (T2D) is a highly prevalent metabolic disease characterized by chronic insulin resistance and β-cell dysfunction and loss, leading to impaired insulin release and hyperglycemia. Although the mechanism responsible for β-cell dysfunction and death is not completely understood, recent findings suggest that the accumulation of misfolded aggregates of the islet amyloid polypeptide (IAPP) in the islets of Langerhans may play an important role in pancreatic damage. Misfolding and aggregation of diverse proteins and their accumulation as amyloid in different organs is the hallmark feature in a group of chronic, degenerative diseases termed protein misfolding disorders (PMDs)...
February 3, 2017: Cold Spring Harbor Perspectives in Medicine
https://www.readbyqxmd.com/read/28154522/metal-dyshomeostasis-and-their-pathological-role-in-prion-and-prion-like-diseases-the-basis-for-a-nutritional-approach
#7
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/28148884/prions
#8
Dmitry Kryndushkin, Herman K Edskes, Frank P Shewmaker, Reed B Wickner
Infectious proteins (prions) are usually self-templating filamentous protein polymers (amyloids). Yeast prions are genes composed of protein and, like the multiple alleles of DNA-based genes, can have an array of "variants," each a distinct self-propagating amyloid conformation. Like the lethal mammalian prions and amyloid diseases, yeast prions may be lethal, or only mildly detrimental, and show an array of phenotypes depending on the protein involved and the prion variant. Yeast prions are models for both rare mammalian prion diseases and for several very common amyloidoses such as Alzheimer's disease, type 2 diabetes, and Parkinson's disease...
February 1, 2017: Cold Spring Harbor Protocols
https://www.readbyqxmd.com/read/28131204/thalamic-involvement-determined-using-vsrad-advance-on-mri-and-easy-z-score-analysis-of-99m-tc-ecd-spect-in-gerstmann-str%C3%A3-ussler-scheinker-syndrome-with-p102l-mutation
#9
Atsuhiko Sugiyama, Noriko Sato, Yukio Kimura, Tomoko Maekawa, Noritaka Wakasugi, Daichi Sone, Mikako Enokizono, Yuji Takahashi, Miho Murata, Hidehiro Mizusawa, Hiroshi Matsuda
Gerstmann-Sträussler-Scheinker syndrome caused by the P102L mutation in the prion protein gene (GSS102) is usually characterized by the onset of slowly progressive cerebellar ataxia, with dementia occurring much later. Because of the relatively long disease course and the prominence of progressive cerebellar ataxia in the early stage, GSS102 is often misdiagnosed as other neurodegenerative disorders. We present two cases of genetically proven GSS102L, both of which present with atrophy and decreased blood flow of the thalamus as determined by voxel-based specific regional analysis system for Alzheimer's disease (VSRAD) advance software and easy Z-score analysis for (99m)Tc-ethyl cysteinate dimer-SPECT, respectively...
February 15, 2017: Journal of the Neurological Sciences
https://www.readbyqxmd.com/read/28124594/strategies-of-engineering-nanoparticles-for-treating-neurodegenerative-disorders
#10
Khanh Tu Nguyen, Minh Nguyet Pham, Toi Van Vo, Wei Duan, Phuong Ha-Lien Tran, Tran Truong-Dinh Thao
Neurodegenerative disorders (NDs) are typically referred to Alzheimer's disease, Parkinson's diseases, amyotrophic lateral sclerosis and prion disease. These are commonly debilitating and, unfortunately, have few therapeutic options. One of the main difficulties in fighting against NDs is to overcome the shielding of blood-brain barrier (BBB), which greatly limits the penetration of various therapeutic drugs, which sometimes leads to severe side effects. Nanotechnology, by engineering materials of a size scale usually within 1-100 nm, fortunately offers an alternative approach for novel, promising and innovative solutions...
January 25, 2017: Current Drug Metabolism
https://www.readbyqxmd.com/read/28108532/tdp-43-prions
#11
Takashi Nonaka, Masato Hasegawa
The most common neurodegenerative diseases, such as Alzheimer's, Parkinson's, and amyotrophic lateral sclerosis, are all protein-misfolding diseases and are characterized by the presence of disease-specific protein aggregates in affected neuronal cells. Recent studies have shown that, like tau and α-synuclein, TAR-DNA binding protein of 43 kDa (TDP-43) can form aggregates in vitro in a seed-dependent, self-templating, prion-like manner. Insoluble TDP-43 prepared from the brains of patients has been classified into several strains, which can be transferred from cell to cell in vitro, suggesting the involvement of mechanisms reminiscent of those by which prions spread through the nervous system...
January 20, 2017: Cold Spring Harbor Perspectives in Medicine
https://www.readbyqxmd.com/read/28096242/developing-therapeutics-for-prp-prion-diseases
#12
Kurt Giles, Steven H Olson, Stanley B Prusiner
The prototypical PrP prion diseases are invariably fatal, and the search for agents to treat them spans more than 30 years, with limited success. However, in the last few years, the application of high-throughput screening, medicinal chemistry, and pharmacokinetic optimization has led to important advances. The PrP prion inoculation paradigm provides a robust assay for testing therapeutic efficacy, and a dozen compounds have been reported that lead to meaningful extension in survival of prion-infected mice...
January 17, 2017: Cold Spring Harbor Perspectives in Medicine
https://www.readbyqxmd.com/read/28077650/melanin-or-melanin-like-substance-interacts-with-the-n-terminal-portion-of-prion-protein-and-inhibits-abnormal-prion-protein-formation-in-prion-infected-cells
#13
Taichi Hamanaka, Keiko Nishizawa, Yuji Sakasegawa, Ayumi Oguma, Kenta Teruya, Hiroshi Kurahashi, Hideyuki Hara, Suehiro Sakaguchi, Katsumi Doh-Ura
Prion diseases are progressive fatal neurodegenerative illnesses caused by the accumulation of transmissible abnormal prion protein (PrP). To find treatments for prion diseases, we searched for substances from natural resources that inhibit abnormal PrP formation in prion-infected cells. We found that high-molecular-weight components from insect cuticle extracts reduced abnormal PrP levels. The chemical nature of these components was consistent with that of melanin. In fact, synthetic melanin produced from tyrosine or 3-hydroxy-l-tyrosine inhibited abnormal PrP formation...
January 11, 2017: Journal of Virology
https://www.readbyqxmd.com/read/28059790/combined-creutzfeldt-jakob-jacob-alzheimer-s-disease-cases-are-important-in-search-for-microbes-in-alzheimer-s-disease
#14
Frank O Bastian
The question whether Alzheimer's disease is infectious as brought up in the recent editorial published in the Journal of Alzheimer's Disease is complicated by the controversy whether the causal agent is a microbe or a misfolded host protein (amyloid). The replicating amyloid (prion) theory, based upon data from studies of Creutzfeldt-Jakob disease (CJD) and other transmissible spongiform encephalopathies (TSEs), has been challenged since the prion can be separated from TSE infectivity, and spiroplasma, a wall-less bacterium, has been shown to be involved in the pathogenesis of CJD...
December 3, 2017: Journal of Alzheimer's Disease: JAD
https://www.readbyqxmd.com/read/28052060/structural-variation-in-amyloid-%C3%AE-fibrils-from-alzheimer-s-disease-clinical-subtypes
#15
Wei Qiang, Wai-Ming Yau, Jun-Xia Lu, John Collinge, Robert Tycko
Aggregation of amyloid-β peptides into fibrils or other self-assembled states is central to the pathogenesis of Alzheimer's disease. Fibrils formed in vitro by 40- and 42-residue amyloid-β peptides (Aβ40 and Aβ42) are polymorphic, with variations in molecular structure that depend on fibril growth conditions. Recent experiments suggest that variations in amyloid-β fibril structure in vivo may correlate with variations in Alzheimer's disease phenotype, in analogy to distinct prion strains that are associated with different clinical and pathological phenotypes...
January 12, 2017: Nature
https://www.readbyqxmd.com/read/28049644/functional-prions-in-the-brain
#16
REVIEW
Joseph B Rayman, Eric R Kandel
Prions are proteins that can adopt self-perpetuating conformations and are traditionally regarded as etiological agents of infectious neurodegenerative diseases in humans, such as Creutzfeldt-Jakob disease, kuru, and transmissible encephalopathies. More recently, a growing consensus has emerged that prion-like, self-templating mechanisms also underlie a variety of neurodegenerative disorders, including amyotrophic lateral sclerosis, Alzheimer's disease, and Huntington's disease. Perhaps most surprising, not all prion-like aggregates are associated with pathological changes...
January 3, 2017: Cold Spring Harbor Perspectives in Biology
https://www.readbyqxmd.com/read/28040507/visualization-of-prion-like-transfer-in-huntington-s-disease-models
#17
REVIEW
Anne H P Jansen, Kevin L Batenburg, Eline Pecho-Vrieseling, Eric A Reits
Most neurodegenerative diseases such as Alzheimer's, Parkinson's and Huntington's disease are hallmarked by aggregate formation of disease-related proteins. In various of these diseases transfer of aggregation-prone proteins between neurons and between neurons and glial cells has been shown, thereby initiating aggregation in neighboring cells and so propagating the disease phenotype. Whereas this prion-like transfer is well studied in Alzheimer's and Parkinson's disease, only a few studies have addressed this potential mechanism in Huntington's disease...
December 29, 2016: Biochimica et Biophysica Acta
https://www.readbyqxmd.com/read/27997158/chaperone-like-activity-of-calnuc-prevents-amyloid-aggregation
#18
Madhavi Kanuru, Gopala Krishna Aradhyam
Calnuc is a ubiquitously expressed protein of the EF-hand Ca(2+)-binding superfamily. Previous studies have implicated it in Ca(2+)-sensitive physiological processes, whereas details of its function and involvement in human diseases are lacking. Drawing upon the sequence homology of calnuc with calreticulin, we propose it functions as a molecular chaperone-like protein. In cells under thermal, chemical [urea and guanidinium chloride (GdmCl)], and acidic stress, calnuc exhibits properties similar to those of established chaperone-like proteins (GRP78, spectrin, and α-crystallin), effectively demonstrated by its ability to suppress aggregation of malate dehydrogenase (MDH), alcohol dehydrogenase, and catalase...
December 20, 2016: Biochemistry
https://www.readbyqxmd.com/read/27995109/chitosan-myristate-nanogel-as-an-artificial-chaperone-protects-neuroserpin-from-misfolding
#19
Habib Nazem, Afshin Mohsenifar, Sahar Majdi
BACKGROUND: Molecular chaperon-like activity for protein refolding was studied using nanogel chitosan-myristic acid (CMA) and the protein neuroserpin (NS), a member of the serine proteinase inhibitor superfamily (serpin). MATERIALS AND METHODS: Recombinant his-tag fusion NS was expressed in Escherichia coli. For confirmation of refolding of the purified NS, structural analysis was performed by circular dichroism and spectrofluorometric along with its inhibitory activity, which was assayed by single-chain tissue plasminogen activator...
2016: Advanced Biomedical Research
https://www.readbyqxmd.com/read/27991860/m1-muscarinic-allosteric-modulators-slow-prion-neurodegeneration-and-restore-memory-loss
#20
Sophie J Bradley, Julie-Myrtille Bourgognon, Helen E Sanger, Nicholas Verity, Adrian J Mogg, David J White, Adrian J Butcher, Julie A Moreno, Colin Molloy, Timothy Macedo-Hatch, Jennifer M Edwards, Jurgen Wess, Robert Pawlak, David J Read, Patrick M Sexton, Lisa M Broad, Joern R Steinert, Giovanna R Mallucci, Arthur Christopoulos, Christian C Felder, Andrew B Tobin
The current frontline symptomatic treatment for Alzheimer's disease (AD) is whole-body upregulation of cholinergic transmission via inhibition of acetylcholinesterase. This approach leads to profound dose-related adverse effects. An alternative strategy is to selectively target muscarinic acetylcholine receptors, particularly the M1 muscarinic acetylcholine receptor (M1 mAChR), which was previously shown to have procognitive activity. However, developing M1 mAChR-selective orthosteric ligands has proven challenging...
February 1, 2017: Journal of Clinical Investigation
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