Database : MEDLINE
Search on : Prion and Diseases [Words]
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[PMID]: 29468946
[Au] Autor:Haley NJ; Richt JA; Davenport KA; Henderson DM; Hoover EA; Manca M; Caughey B; Marthaler D; Bartz J; Gilch S
[Ad] Address:a Department of Microbiology and Immunology , Midwestern University , Glendale , AZ , USA.
[Ti] Title:Design, implementation, and interpretation of amplification studies for prion detection.
[So] Source:Prion;:1-10, 2018 Mar 09.
[Is] ISSN:1933-690X
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Amplification assays for transmissible spongiform encephalopathies have been in development for close to 15 years, with critical implications for the postmortem and antemortem diagnosis of human and animal prion diseases. Little has been published regarding the structured development, implementation and interpretation of experiments making use of protein misfolding cyclic amplification (PMCA) and real time quaking-induced conversion (RT-QuIC), and our goal with this Perspectives manuscript is to offer a framework which might allow for more efficient expansion of pilot studies into diagnostic trials in both human and animal subjects. This framework is made up of approaches common to diagnostic medicine, including a thorough understanding of analytical and diagnostic sensitivity and specificity, an a priori development of amplification strategy, and an effective experimental design. It is our hope that a structured framework for prion amplification assays will benefit not only experiments seeking to sensitively detect naturally-occurring cases of prion diseases and describe the pathogenesis of TSEs, but ultimately assist with future endeavors seeking to use these methods more broadly for other protein misfolding disorders, including Alzheimer's and Parkinson's disease.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1802
[Cu] Class update date: 180309
[Lr] Last revision date:180309
[St] Status:Publisher
[do] DOI:10.1080/19336896.2018.1443000

  2 / 9919 MEDLINE  
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[PMID]: 29330303
[Au] Autor:Chandramowlishwaran P; Sun M; Casey KL; Romanyuk AV; Grizel AV; Sopova JV; Rubel AA; Nussbaum-Krammer C; Vorberg IM; Chernoff YO
[Ad] Address:From the School of Biological Sciences, Georgia Institute of Technology, Atlanta, Georgia 30332.
[Ti] Title:Mammalian amyloidogenic proteins promote prion nucleation in yeast.
[So] Source:J Biol Chem;293(9):3436-3450, 2018 Mar 02.
[Is] ISSN:1083-351X
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Fibrous cross-ß aggregates (amyloids) and their transmissible forms (prions) cause diseases in mammals (including humans) and control heritable traits in yeast. Initial nucleation of a yeast prion by transiently overproduced prion-forming protein or its (typically, QN-rich) prion domain is efficient only in the presence of another aggregated (in most cases, QN-rich) protein. Here, we demonstrate that a fusion of the prion domain of yeast protein Sup35 to some non-QN-rich mammalian proteins, associated with amyloid diseases, promotes nucleation of Sup35 prions in the absence of pre-existing aggregates. In contrast, both a fusion of the Sup35 prion domain to a multimeric non-amyloidogenic protein and the expression of a mammalian amyloidogenic protein that is not fused to the Sup35 prion domain failed to promote prion nucleation, further indicating that physical linkage of a mammalian amyloidogenic protein to the prion domain of a yeast protein is required for the nucleation of a yeast prion. Biochemical and cytological approaches confirmed the nucleation of protein aggregates in the yeast cell. Sequence alterations antagonizing or enhancing amyloidogenicity of human amyloid-ß (associated with Alzheimer's disease) and mouse prion protein (associated with prion diseases), respectively, antagonized or enhanced nucleation of a yeast prion by these proteins. The yeast-based prion nucleation assay, developed in our work, can be employed for mutational dissection of amyloidogenic proteins. We anticipate that it will aid in the identification of chemicals that influence initial amyloid nucleation and in searching for new amyloidogenic proteins in a variety of proteomes.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1801
[Cu] Class update date: 180309
[Lr] Last revision date:180309
[St] Status:In-Data-Review
[do] DOI:10.1074/jbc.M117.809004

  3 / 9919 MEDLINE  
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[PMID]: 29330304
[Au] Autor:Pritzkow S; Morales R; Lyon A; Concha-Marambio L; Urayama A; Soto C
[Ad] Address:From the Mitchell Center for Alzheimer's Disease and Related Brain Disorders, Department of Neurology, University of Texas Houston Medical School, Houston, Texas 77030 and.
[Ti] Title:Efficient prion disease transmission through common environmental materials.
[So] Source:J Biol Chem;293(9):3363-3373, 2018 Mar 02.
[Is] ISSN:1083-351X
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Prion diseases are a group of fatal neurodegenerative diseases associated with a protein-based infectious agent, termed prion. Compelling evidence suggests that natural transmission of prion diseases is mediated by environmental contamination with infectious prions. We hypothesized that several natural and man-made materials, commonly found in the environments of wild and captive animals, can bind prions and may act as vectors for disease transmission. To test our hypothesis, we exposed surfaces composed of various common environmental materials ( wood, rocks, plastic, glass, cement, stainless steel, aluminum, and brass) to hamster-adapted 263K scrapie prions and studied their attachment and retention of infectivity and Our results indicated that these surfaces, with the sole exception of brass, efficiently bind, retain, and release prions. Prion replication was studied using the protein misfolding cyclic amplification technology, and infectivity of surface-bound prions was analyzed by intracerebrally challenging hamsters with contaminated implants. Our results revealed that virtually all prion-contaminated materials transmitted the disease at high rates. To investigate a more natural form of exposure to environmental contamination, we simply housed animals with large contaminated spheres made of the different materials under study. Strikingly, most of the hamsters developed classical clinical signs of prion disease and typical disease-associated brain changes. Our findings suggest that prion contamination of surfaces commonly present in the environment can be a source of disease transmission, thus expanding our understanding of the mechanisms for prion spreading in nature.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1801
[Cu] Class update date: 180309
[Lr] Last revision date:180309
[St] Status:In-Data-Review
[do] DOI:10.1074/jbc.M117.810747

  4 / 9919 MEDLINE  
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[PMID]: 28470584
[Au] Autor:Jang B; Jeon YC; Shin HY; Lee YJ; Kim H; Kondo Y; Ishigami A; Kim YS; Choi EK
[Ad] Address:Ilsong Institute of Life Science, Hallym University, 15 Gwanpyeong-ro 170beon-gil, Anyang, Gyeonggi-do, 14066, Republic of Korea.
[Ti] Title:Myelin Basic Protein Citrullination, a Hallmark of Central Nervous System Demyelination, Assessed by Novel Monoclonal Antibodies in Prion Diseases.
[So] Source:Mol Neurobiol;55(4):3172-3184, 2018 Apr.
[Is] ISSN:1559-1182
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Myelin basic protein (MBP) citrullination by peptidylarginine deiminase (PAD) enzymes leads to incomplete protein-lipid bilayer interactions and vulnerability to proteolytic enzymes, resulting in disorganization of the myelin sheath in the central nervous system. Therefore, citrullinated MBP (citMBP) has been suggested as a hallmark of demyelination, but how citMBP is implicated in prion diseases remains unknown. For the first time, we developed mouse monoclonal anti-citMBP IgG1 (clones 1B8, 1H1, and 3C6) and IgM (clone 3G5) antibodies that recognize human citMBP at its R25, R122, and R130 residues and at its C-terminal region (or the corresponding sites in mouse MBP), respectively. Using a biochemical, immunohistochemical, and immunogold-silver staining for electron microscopy techniques, we found that MBP residue R23 (corresponding to human R25) was specifically citrullinated, was stained as intense punctae in the corpus callosum, the striatum, and the cerebellar white matter, and was predominantly localized in disorganized myelin in the brains of scrapie-infected mice. In the brains of Creutzfeldt-Jakob disease (CJD) patients, MBP residues R25, R122, and R130 were markedly citrullinated and were stained as fibrils and punctae. In particular, white matter regions, such as the midbrain and the medulla, exhibited high levels of citMBP compared to other regions. However, the high levels of citMBP were not correlated with PAD2 expression. The clone 3G5 recognized significantly increased expression of the 18.5 kDa and/or 21.5 kDa variants of MBP in prion disease. Our findings suggest that significantly increased levels of citMBP may reflect demyelinating neuropathology, and that these newly developed antibodies may be useful for identifying demyelination.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1705
[Cu] Class update date: 180309
[Lr] Last revision date:180309
[St] Status:In-Data-Review
[do] DOI:10.1007/s12035-017-0560-0

  5 / 9919 MEDLINE  
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[PMID]: 29514050
[Au] Autor:Sabareesan AT; Mathew MK; Udgaonkar JB
[Ad] Address:National Centre for Biological Sciences, Tata Institute of Fundamental Research, Bangalore 560065, India.
[Ti] Title:Mechanism of aggregation and membrane interactions of mammalian prion protein.
[So] Source:Biochim Biophys Acta;, 2018 Mar 04.
[Is] ISSN:0006-3002
[Cp] Country of publication:Netherlands
[La] Language:eng
[Ab] Abstract:The cellular prion protein (PrP ), which is present ubiquitously in all mammalian neurons, is normally found to be linked to the cell membrane through a glycosylphosphatidylinositol (GPI) anchor. The conformational conversion of PrP into misfolded and aggregated forms is associated with transmissible neurodegenerative diseases known as prion diseases. The importance of different misfolded conformations in prion diseases, and the mechanism by which prion aggregates induce neurotoxicity remain poorly understood. Multiple studies have been shown that the toxicity of misfolded prion protein is directly correlated with its ability to interact with and perturb membranes. This review describes the current progress toward understanding prion protein misfolding and aggregation, as well as the interaction of prion protein aggregates with lipid membrane.
[Pt] Publication type:JOURNAL ARTICLE; REVIEW
[Em] Entry month:1803
[Cu] Class update date: 180307
[Lr] Last revision date:180307
[St] Status:Publisher

  6 / 9919 MEDLINE  
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[PMID]: 29458424
[Au] Autor:Race B; Williams K; Hughson AG; Jansen C; Parchi P; Rozemuller AJM; Chesebro B
[Ad] Address:Laboratory of Persistent Viral Diseases, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, National Institutes of Health, 903 South Fourth Street, Hamilton, MT, 59840, USA. raceb@nih.gov.
[Ti] Title:Familial human prion diseases associated with prion protein mutations Y226X and G131V are transmissible to transgenic mice expressing human prion protein.
[So] Source:Acta Neuropathol Commun;6(1):13, 2018 02 20.
[Is] ISSN:2051-5960
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:Human familial prion diseases are associated with mutations at 34 different prion protein (PrP) amino acid residues. However, it is unclear whether infectious prions are found in all cases. Mutant PrP itself may be neurotoxic, or alternatively, PrP mutation might predispose to spontaneous formation of infectious PrP isoforms. Previous reports demonstrated transmission to animal models by human brain tissue expressing 7 different PrP mutations, but 3 other mutations were not transmissible. In the present work, we tested transmission using brain homogenates from patients expressing 3 untested PrP mutants: G131V, Y226X, and Q227X. Human brain homogenates were injected intracerebrally into tg66 transgenic mice overexpressing human PrP. Mice were followed for nearly 800 days.From 593 to 762 dpi, 4 of 8 mice injected with Y226X brain had PrPSc detectable in brain by immunostaining, immunoblot, and PrP amyloid seeding activity assayed by RT-QuIC. From 531 to 784 dpi, 11 of 11 G131V-injected mice had PrPSc deposition in brain, but none were positive by immunoblot or RT-QuIC assay. In contrast, from 529 to 798 dpi, no tg66 mice injected with Q227X brain had PrPSc or PrP amyloid seeding activity detectable by these methods. Y226X is the only one of 4 known PrP truncations associated with familial disease which has been shown to be transmissible. This transmission of prion infectivity from a patient expressing truncated human PrP may have implications for the spread and possible transmission of other aggregated truncated proteins in prion-like diseases such as Alzheimer's disease, Parkinson's disease and tauopathies.
[Pt] Publication type:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., INTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Em] Entry month:1802
[Cu] Class update date: 180307
[Lr] Last revision date:180307
[St] Status:In-Process
[do] DOI:10.1186/s40478-018-0516-2

  7 / 9919 MEDLINE  
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[PMID]: 29378654
[Au] Autor:Datki Z; Olah Z; Hortobagyi T; Macsai L; Zsuga K; Fulop L; Bozso Z; Galik B; Acs E; Foldi A; Szarvas A; Kalman J
[Ad] Address:Department of Psychiatry, Faculty of Medicine, University of Szeged, Kalvaria sgt. 57, Szeged, H-6725, Hungary. datki.zsolt@med.u-szeged.hu.
[Ti] Title:Exceptional in vivo catabolism of neurodegeneration-related aggregates.
[So] Source:Acta Neuropathol Commun;6(1):6, 2018 01 29.
[Is] ISSN:2051-5960
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:Neurodegenerative diseases are linked to a systemic enzyme resistance of toxic aggregated molecules and their pathological consequences. This paper presents a unique phenomenon that Philodina acuticornis, a bdelloid rotifer, is able to catabolize different types of neurotoxic peptide and protein aggregates (such as beta-amyloids /Aß/, alpha-synuclein, and prion) without suffering any damage. P. acuticornis is capable of using these aggregates as an exclusive energy source (i.e., as 'food', identified in the digestive system and body) in a hermetically isolated microdrop environment, increasing their survival. As regards Aß1-42, five other bdelloid rotifer species were also found to be able to perform this phenomenon. Based on our experiments, the Aß1-42-treated bdelloid rotifers demonstrate significantly increased survival (e.g. mean lifespan = 51 ± 2.71 days) compared to their untreated controls (e.g. mean lifespan = 14 ± 2.29 days), with similar improvements in a variety of phenotypic characteristics. To our knowledge, no other animal species have so far been reported to have a similar capability. For all other microscopic species tested, including monogonant rotifers and non-rotifers, the treatment with Aß1-42 aggregates proved to be either toxic or simply ineffective. This paper describes and proves the existence of an unprecedented in vivo catabolic capability of neurotoxic aggregates by bdelloid rotifers, with special focus on P. acuticornis. Our results may provide the basis for a new preclinical perspective on therapeutic research in human neurodegenerative diseases.
[Pt] Publication type:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Em] Entry month:1801
[Cu] Class update date: 180307
[Lr] Last revision date:180307
[St] Status:In-Process
[do] DOI:10.1186/s40478-018-0507-3

  8 / 9919 MEDLINE  
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[PMID]: 29310723
[Au] Autor:Cali I; Cohen ML; HaÑ—k S; Parchi P; Giaccone G; Collins SJ; Kofskey D; Wang H; McLean CA; Brandel JP; Privat N; Sazdovitch V; Duyckaerts C; Kitamoto T; Belay ED; Maddox RA; Tagliavini F; Pocchiari M; Leschek E; Appleby BS; Safar JG; Schonberger LB; Gambetti P
[Ad] Address:Departments of Pathology, Case Western Reserve University, School of Medicine, Cleveland, OH, 44106, USA. ixc20@case.edu.
[Ti] Title:Iatrogenic Creutzfeldt-Jakob disease with Amyloid-ß pathology: an international study.
[So] Source:Acta Neuropathol Commun;6(1):5, 2018 01 08.
[Is] ISSN:2051-5960
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:The presence of pathology related to the deposition of amyloid-ß (Aß) has been recently reported in iatrogenic Creutzfeldt-Jakob disease (iCJD) acquired from inoculation of growth hormone (GH) extracted from human cadaveric pituitary gland or use of cadaveric dura mater (DM) grafts.To investigate this phenomenon further, a cohort of 27 iCJD cases - 21 with adequate number of histopathological sections - originating from Australia, France, Italy, and the Unites States, were examined by immunohistochemistry, amyloid staining, and Western blot analysis of the scrapie prion protein (PrP ), and compared with age-group matched cases of sporadic CJD (sCJD), Alzheimer disease (AD) or free of neurodegenerative diseases (non-ND).Cases of iCJD and sCJD shared similar profiles of proteinase K-resistant PrP with the exception of iCJD harboring the "MMi" phenotype. Cerebral amyloid angiopathy (CAA), either associated with, or free of, Thioflavin S-positive amyloid core plaques (CP), was observed in 52% of 21 cases of iCJD, which comprised 37.5% and 61.5% of the cases of GH- and DM-iCJD, respectively. If only cases younger than 54 years were considered, Aß pathology affected 41%, 2% and 0% of iCJD, sCJD and non-ND, respectively. Despite the patients' younger age CAA was more severe in iCJD than sCJD, while Aß diffuse plaques, in absence of Aß CP, populated one third of sCJD. Aß pathology was by far most severe in AD. Tau pathology was scanty in iCJD and sCJD.In conclusion, (i) despite the divergences in the use of cadaveric GH and DM products, our cases combined with previous studies showed remarkably similar iCJD and Aß phenotypes indicating that the occurrence of Aß pathology in iCJD is a widespread phenomenon, (ii) CAA emerges as the hallmark of the Aß phenotype in iCJD since it is observed in nearly 90% of all iCJD with Aß pathology reported to date including ours, and it is shared by GH- and DM-iCJD, (iii) although the contributions to Aß pathology of other factors, including GH deficiency, cannot be discounted, our findings increase the mounting evidence that this pathology is acquired by a mechanism resembling that of prion diseases.
[Pt] Publication type:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, P.H.S.
[Em] Entry month:1801
[Cu] Class update date: 180307
[Lr] Last revision date:180307
[St] Status:In-Process
[do] DOI:10.1186/s40478-017-0503-z

  9 / 9919 MEDLINE  
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[PMID]: 28449707
[Au] Autor:Llorens F; Thüne K; Sikorska B; Schmitz M; Tahir W; Fernández-Borges N; Cramm M; Gotzmann N; Carmona M; Streichenberger N; Michel U; Zafar S; Schuetz AL; Rajput A; Andréoletti O; Bonn S; Fischer A; Liberski PP; Torres JM; Ferrer I; Zerr I
[Ad] Address:Department of Neurology, University Medical Center Göttingen, and German Center for Neurodegenerative Diseases (DZNE), Robert Koch Strasse 40, 37075, Göttingen, Germany. franc.llorens@gmail.com.
[Ti] Title:Altered Ca homeostasis induces Calpain-Cathepsin axis activation in sporadic Creutzfeldt-Jakob disease.
[So] Source:Acta Neuropathol Commun;5(1):35, 2017 04 27.
[Is] ISSN:2051-5960
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:Sporadic Creutzfeldt-Jakob disease (sCJD) is the most prevalent form of human prion disease and it is characterized by the presence of neuronal loss, spongiform degeneration, chronic inflammation and the accumulation of misfolded and pathogenic prion protein (PrP ). The molecular mechanisms underlying these alterations are largely unknown, but the presence of intracellular neuronal calcium (Ca ) overload, a general feature in models of prion diseases, is suggested to play a key role in prion pathogenesis.Here we describe the presence of massive regulation of Ca responsive genes in sCJD brain tissue, accompanied by two Ca -dependent processes: endoplasmic reticulum stress and the activation of the cysteine proteases Calpains 1/2. Pathogenic Calpain proteins activation in sCJD is linked to the cleavage of their cellular substrates, impaired autophagy and lysosomal damage, which is partially reversed by Calpain inhibition in a cellular prion model. Additionally, Calpain 1 treatment enhances seeding activity of PrP in a prion conversion assay. Neuronal lysosomal impairment caused by Calpain over activation leads to the release of the lysosomal protease Cathepsin S that in sCJD mainly localises in axons, although massive Cathepsin S overexpression is detected in microglial cells. Alterations in Ca homeostasis and activation of Calpain-Cathepsin axis already occur at pre-clinical stages of the disease as detected in a humanized sCJD mouse model.Altogether our work indicates that unbalanced Calpain-Cathepsin activation is a relevant contributor to the pathogenesis of sCJD at multiple molecular levels and a potential target for therapeutic intervention.
[Mh] MeSH terms primary: Brain/metabolism
Calcium/metabolism
Calpain/metabolism
Cathepsins/metabolism
Creutzfeldt-Jakob Syndrome/metabolism
Homeostasis/physiology
[Mh] MeSH terms secundary: Animals
Brain/pathology
Cations, Divalent/metabolism
Cells, Cultured
Creutzfeldt-Jakob Syndrome/pathology
Disease Models, Animal
Humans
Lysosomes/metabolism
Lysosomes/pathology
Mesocricetus
Mice, Transgenic
Neurons/metabolism
Neurons/pathology
PrPSc Proteins/metabolism
Rats, Wistar
Recombinant Proteins/metabolism
Sheep
[Pt] Publication type:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Name of substance:0 (Cations, Divalent); 0 (PrPSc Proteins); 0 (Recombinant Proteins); EC 3.4.- (Cathepsins); EC 3.4.22.- (Calpain); SY7Q814VUP (Calcium)
[Em] Entry month:1712
[Cu] Class update date: 180307
[Lr] Last revision date:180307
[Js] Journal subset:IM
[Da] Date of entry for processing:170429
[St] Status:MEDLINE
[do] DOI:10.1186/s40478-017-0431-y

  10 / 9919 MEDLINE  
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[PMID]: 29184404
[Au] Autor:Jeong JK; Lee YJ; Jeong SY; Jeong S; Lee GW; Park SY
[Ad] Address:Biosafety Research Institute, College of Veterinary Medicine, Chonbuk National University, Iksan.
[Ti] Title:Autophagic flux induced by graphene oxide has a neuroprotective effect against human prion protein fragments.
[So] Source:Int J Nanomedicine;12:8143-8158, 2017.
[Is] ISSN:1178-2013
[Cp] Country of publication:New Zealand
[La] Language:eng
[Ab] Abstract:Graphene oxide (GO) is a nanomaterial with newly developing biological applications. Autophagy is an intracellular degradation system that has been associated with the progression of neurodegenerative disorders. Although induction of autophagic flux by GO has been reported, the underlying signaling pathway in neurodegenerative disorders and how this is involved in neuroprotection remain obscure. We show that GO itself activates autophagic flux in neuronal cells and confers a neuroprotective effect against prion protein (PrP) (106-126)-mediated neurotoxicity. GO can be detected in SK-N-SH neuronal cells, where it triggers autophagic flux signaling. GO-induced autophagic flux prevented PrP (106-126)-induced neurotoxicity in SK-N-SH cells. Moreover, inactivation of autophagic flux blocked GO-induced neuroprotection against prion-mediated mitochondrial neurotoxicity. This is the first study to demonstrate that GO regulates autophagic flux in neuronal cells, and that activation of autophagic flux signals, induced by GO, plays a neuroprotective role against prion-mediated mitochondrial neurotoxicity. These results suggest that the nanomaterial GO may be used to activate autophagic flux and could be used in neuroprotective strategies for treatment of neurodegenerative disorders, including prion diseases.
[Mh] MeSH terms primary: Autophagy/drug effects
Graphite/pharmacology
Neurons/drug effects
Neuroprotective Agents/pharmacology
Peptide Fragments/toxicity
Prions/toxicity
[Mh] MeSH terms secundary: Cell Line
Graphite/chemistry
Humans
Mitochondria/metabolism
Neurons/pathology
Neuroprotective Agents/chemistry
Oxides/chemistry
Signal Transduction/drug effects
[Pt] Publication type:JOURNAL ARTICLE
[Nm] Name of substance:0 (Neuroprotective Agents); 0 (Oxides); 0 (Peptide Fragments); 0 (Prions); 0 (prion protein (106-126)); 7782-42-5 (Graphite)
[Em] Entry month:1803
[Cu] Class update date: 180305
[Lr] Last revision date:180305
[Js] Journal subset:IM
[Da] Date of entry for processing:171130
[St] Status:MEDLINE
[do] DOI:10.2147/IJN.S146398


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