175 results match your criteria Prion-Related Diseases


Evidence of p75 Neurotrophin Receptor Involvement in the Central Nervous System Pathogenesis of Classical Scrapie in Sheep and a Transgenic Mouse Model.

Int J Mol Sci 2021 Mar 8;22(5). Epub 2021 Mar 8.

Centro de Encefalopatías y Enfermedades Transmisibles Emergentes, Facultad de Veterinaria, Instituto Agroalimentario de Aragón - IA2 (Universidad de Zaragoza - CITA), 50013 Zaragoza, Spain.

Neurotrophins constitute a group of growth factor that exerts important functions in the nervous system of vertebrates. They act through two classes of transmembrane receptors: tyrosine-kinase receptors and the p75 neurotrophin receptor (p75). The activation of p75 can favor cell survival or apoptosis depending on diverse factors. Read More

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Distribution of microRNA profiles in pre-clinical and clinical forms of murine and human prion disease.

Commun Biol 2021 Mar 25;4(1):411. Epub 2021 Mar 25.

Department of Biochemistry and Genetics, La Trobe Institute for Molecular Science, La Trobe University, Bundoora, VIC, Australia.

Prion diseases are distinguished by long pre-clinical incubation periods during which prions actively propagate in the brain and cause neurodegeneration. In the pre-clinical stage, we hypothesize that upon prion infection, transcriptional changes occur that can lead to early neurodegeneration. A longitudinal analysis of miRNAs in pre-clinical and clinical forms of murine prion disease demonstrated dynamic expression changes during disease progression in the affected thalamus region and serum. Read More

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An Update on Autophagy in Prion Diseases.

Front Bioeng Biotechnol 2020 27;8:975. Epub 2020 Aug 27.

Laboratorio de Genética Bioquímica (LAGENBIO), Instituto Agroalimentario de Aragón-IA2, Instituto de Investigación Sanitaria Aragón-IISA, Universidad de Zaragoza, Zaragoza, Spain.

Autophagy is a dynamic intracellular mechanism involved in protein and organelle turnover through lysosomal degradation. When properly regulated, autophagy supports normal cellular and developmental processes, whereas defects in autophagic degradation have been associated with several pathologies, including prion diseases. Prion diseases, or transmissible spongiform encephalopathies (TSE), are a group of fatal neurodegenerative disorders characterized by the accumulation of the pathological misfolded isoform (PrP) of the physiological cellular prion protein (PrP) in the central nervous system. Read More

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Identification of the prion-related protein gene (PRNT) sequences in various species of the Cervidae family.

Mol Biol Rep 2020 Aug 31;47(8):6155-6164. Epub 2020 Jul 31.

Korea Zoonosis Research Institute, Jeonbuk National University, 820-120, Hana-ro, Iksan, Jeonbuk, 54531, Republic of Korea.

Chronic wasting disease (CWD) is caused by abnormal deleterious prion protein (PrP), and transmissible spongiform encephalopathy occurs in the Cervidae family. In recent studies, the susceptibility of prion disease has been affected by polymorphisms of the prion gene family. However, the study of the prion-related protein gene (PRNT) is rare, and the DNA sequence of this gene was not fully reported in all Cervidae families. Read More

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Chronic Wasting Disease in Cervids: Implications for Prion Transmission to Humans and Other Animal Species.

mBio 2019 07 23;10(4). Epub 2019 Jul 23.

National Prion Disease Pathology Surveillance Center, Case Western Reserve University, Cleveland, Ohio, USA.

Chronic wasting disease (CWD) is a prion-related transmissible spongiform encephalopathy of cervids, including deer, elk, reindeer, sika deer, and moose. CWD has been confirmed in at least 26 U.S. Read More

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Yeast as a Tool for Deeper Understanding of Human Manganese-Related Diseases.

Genes (Basel) 2019 07 17;10(7). Epub 2019 Jul 17.

Louvain Institute of Biomolecular Science and Technology, Université catholique de Louvain, B-1348 Louvain-la-Neuve, Belgium.

The biological importance of manganese lies in its function as a key cofactor for numerous metalloenzymes and as non-enzymatic antioxidant. Due to these two essential roles, it appears evident that disturbed manganese homeostasis may trigger the development of pathologies in humans. In this context, yeast has been extensively used over the last decades to gain insight into how cells regulate intra-organellar manganese concentrations and how human pathologies may be related to disturbed cellular manganese homeostasis. Read More

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Clinical trials of prion disease therapeutics.

Curr Opin Pharmacol 2019 02 17;44:53-60. Epub 2019 May 17.

Fondazione IRCCS Istituto Neurologico "Carlo Besta", Milano, Italy.

Prion-related encephalopathies or transmissible spongiform encephalopathies (TSEs) are a group of rare progressive neurodegenerative disorders that are invariably fatal with often only six months elapsing from diagnosis to patient death. This makes the development of effective therapeutic strategies challenging. Nonetheless, compounds have been identified in animal models of TSE that prolong survival and, in some instances, eradicate the disease. Read More

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February 2019

Genetic Perturbation of TIA1 Reveals a Physiological Role in Fear Memory.

Cell Rep 2019 03;26(11):2970-2983.e4

Department of Neuroscience, Mortimer B. Zuckerman Mind Brain Behavior Institute, Columbia University, New York, NY 10027, USA; Department of Psychiatry, College of Physicians and Surgeons of Columbia University, New York, NY 10032, USA; Howard Hughes Medical Institute at Columbia University, New York, NY 10032, USA; Kavli Institute for Brain Science, Columbia University, New York, NY 10032, USA. Electronic address:

TIA1 is a prion-related RNA-binding protein whose capacity to form various types of intracellular aggregates has been implicated in neurodegenerative disease. However, its role in normal brain function is poorly understood. Here, we show that TIA1 bidirectionally modulates stress-dependent synaptic plasticity in the hippocampus, a brain region involved in fear memory and olfactory discrimination learning. Read More

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Prion-like protein gene (PRND) polymorphisms associated with scrapie susceptibility in Korean native black goats.

PLoS One 2018 25;13(10):e0206209. Epub 2018 Oct 25.

Korea Zoonosis Research Institute, Chonbuk National University, Iksan, Jeonbuk, Republic of Korea.

The polymorphisms of the prion protein (PRNP) gene, which encodes normal prion proteins (PrP), are known to be involved in the susceptibility of prion diseases. The prion-like protein (Doppel) gene (PRND) is the paralog of the PRNP gene and is closely located downstream of the PRNP gene. In addition, the polymorphisms of PRND correlate with disease susceptibility in several animals. Read More

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Prion-related peripheral neuropathy in sporadic Creutzfeldt-Jakob disease.

J Neurol Neurosurg Psychiatry 2019 04 24;90(4):424-427. Epub 2018 Oct 24.

IRCCS Istituto delle Scienze Neurologiche di Bologna, Bologna, Italy

Objective: To assess whether the involvement of the peripheral nervous system (PNS) belongs to the phenotypic spectrum of sporadic Creutzfeldt-Jakob disease (sCJD).

Methods: We examined medical records of 117 sCJDVV2 (ataxic type), 65 sCJDMV2K (kuru-plaque type) and 121 sCJDMM(V)1 (myoclonic type) subjects for clinical symptoms, objective signs and neurophysiological data. We reviewed two diagnostic nerve biopsies and looked for abnormal prion protein (PrP) by western blotting and real-time quaking-induced conversion (RT-QuIC) in postmortem PNS samples from 14 subjects. Read More

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Mammalian prion propagation in PrP transgenic Drosophila.

Brain 2018 09;141(9):2700-2710

University of Cambridge, Department of Veterinary Medicine, Madingley Road, Cambridge, CB3 OES, UK.

Mammalian prions propagate by template-directed misfolding and aggregation of normal cellular prion related protein PrPC as it converts into disease-associated conformers collectively referred to as PrPSc. Mammalian species may be permissive for prion disease because these hosts have co-evolved specific co-factors that assist PrPC conformational change and prion propagation. We have tested this hypothesis by examining whether faithful prion propagation occurs in the normally PrPC-null invertebrate host Drosophila melanogaster. Read More

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September 2018

First report of prion-related protein gene () polymorphisms in cattle.

Vet Rec 2018 06 17;182(25):717. Epub 2018 Apr 17.

Department of Bioactive Material Sciences, Chonbuk National University, Jeonju, Jeonbuk, Republicof Korea.

Prion diseases are caused by structural changes in normal prion protein (PrP). The prion gene family includes four members: prion protein (), prion-like protein (), shadow of () and prion-related protein (). Genetic association studies of prion diseases and the other genes in the prion gene family, except for , have been performed in cattle. Read More

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Discovery of small molecules binding to the normal conformation of prion by combining virtual screening and multiple biological activity evaluation methods.

J Comput Aided Mol Des 2017 12 20;31(12):1053-1062. Epub 2017 Nov 20.

State Key Laboratory of Applied Organic Chemistry and Department of Chemistry, Lanzhou University, Lanzhou, 730000, People's Republic of China.

Conformational conversion of the normal cellular prion protein, PrP, into the misfolded isoform, PrP, is considered to be a central event in the development of fatal neurodegenerative diseases. Stabilization of prion protein at the normal cellular form (PrP) with small molecules is a rational and efficient strategy for treatment of prion related diseases. However, few compounds have been identified as potent prion inhibitors by binding to the normal conformation of prion. Read More

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December 2017

Semisynthetic prion protein (PrP) variants carrying glycan mimics at position 181 and 197 do not form fibrils.

Chem Sci 2017 Sep 24;8(9):6626-6632. Epub 2017 Jul 24.

Institute of Biological Chemistry , Department of Chemistry , University of Vienna , Waehringer Strasse 38 , 1090 , Vienna-AT , Austria . Email:

The prion protein (PrP) is an -glycosylated protein attached to the outer leaflet of eukaryotic cell membranes a glycosylphosphatidylinositol (GPI) anchor. Different prion strains have distinct glycosylation patterns and the extent of glycosylation of potentially pathogenic misfolded prion protein (PrP) has a major impact on several prion-related diseases (transmissible spongiform encephalopathies, TSEs). Based on these findings it is hypothesized that posttranslational modifications (PTMs) of PrP influence conversion of cellular prion protein (PrP) into PrP and, as such, modified PrP variants are critical tools needed to investigate the impact of PTMs on the pathogenesis of TSEs. Read More

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September 2017

Chicken RNA-binding protein T-cell internal antigen-1 contributes to stress granule formation in chicken cells and tissues.

J Vet Sci 2018 Jan;19(1):3-12

Department of Avian Infectious Diseases, Shanghai Veterinary Research Institute, Chinese Academy of Agricultural Science, Shanghai 200241, China.

T-cell internal antigen-1 (TIA-1) has roles in regulating alternative pre-mRNA splicing, mRNA translation, and stress granule (SG) formation in human cells. As an evolutionarily conserved response to environmental stress, SGs have been reported in various species. However, SG formation in chicken cells and the role of chicken TIA-1 (cTIA-1) in SG assembly has not been elucidated. Read More

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January 2018

The first report of prion-related protein gene (PRNT) polymorphisms in goat.

Acta Vet Hung 2017 06;65(2):291-300

Korea Zoonosis Research Institute, Chonbuk National University , 820-120, Hana-ro, Iksan, Jeonbuk 570-390 , Republic of Korea.

Prion protein is encoded by the prion protein gene (PRNP). Polymorphisms of several members of the prion gene family have shown association with prion diseases in several species. Recent studies on a novel member of the prion gene family in rams have shown that prion-related protein gene (PRNT) has a linkage with codon 26 of prion-like protein (PRND). Read More

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Regulation of RhoA activity by the cellular prion protein.

Cell Death Dis 2017 03 16;8(3):e2668. Epub 2017 Mar 16.

Ilsong Institute of Life Science, Hallym University, Anyang, Republic of Korea.

The cellular prion protein (PrP) is a highly conserved glycosylphosphatidylinositol (GPI)-anchored membrane protein that is involved in the signal transduction during the initial phase of neurite outgrowth. The Ras homolog gene family member A (RhoA) is a small GTPase that is known to have an essential role in regulating the development, differentiation, survival, and death of neurons in the central nervous system. Although recent studies have shown the dysregulation of RhoA in a variety of neurodegenerative diseases, the role of RhoA in prion pathogenesis remains unclear. Read More

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Prion Function and Pathophysiology in Non-Mammalian Models.

Curr Mol Med 2017 ;17(1):13-23

Institute of Biomedical Sciences (Sector A, Second Floor), Universidad de Chile, Independencia 1027, Santiago, P.O. Box 70031. Chile.

More than thirty years have passed since the discovery of the prion protein (PrP) and its causative role in transmissible spongiform encephalopathy. Since a combination of both gain- and loss-of-function mechanisms may underlay prion pathogenesis, understanding the physiological role of PrP may give important clues about disease mechanisms. Historically, the primary strategy for prion research has involved the use of human tissue, cell cultures and mammalian animal models. Read More

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TIA-1 Is a Functional Prion-Like Protein.

Cold Spring Harb Perspect Biol 2017 May 1;9(5). Epub 2017 May 1.

Department of Neuroscience, College of Physicians and Surgeons of Columbia University, New York, New York 10032.

Prions are self-propagating protein conformations that are traditionally regarded as agents of neurodegenerative disease in animals. However, it has become evident that prion-like aggregation of endogenous proteins can also occur under normal physiological conditions (e.g. Read More

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Differentially expressed genes in iron-induced prion protein conversion.

Biochem Biophys Res Commun 2016 11 29;480(4):734-740. Epub 2016 Oct 29.

Laboratory of Immunology and Research Institute for Veterinary Science, College of Veterinary Medicine, Seoul National University, Seoul 08826, Republic of Korea. Electronic address:

The conversion of the cellular prion protein (PrP) to the protease-resistant isoform is the key event in chronic neurodegenerative diseases, including transmissible spongiform encephalopathies (TSEs). Increased iron in prion-related disease has been observed due to the prion protein-ferritin complex. Additionally, the accumulation and conversion of recombinant PrP (rPrP) is specifically derived from Fe(III) but not Fe(II). Read More

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November 2016

Insights from Therapeutic Studies for PrP Prion Disease.

Cold Spring Harb Perspect Med 2017 Mar 1;7(3). Epub 2017 Mar 1.

Department of Neurochemistry, Tohoku University Graduate School of Medicine, Seiryo-cho, Aoba-ku, Sendai 980-8575, Japan.

Although an effective therapy for prion disease has not yet been established, many advances have been made toward understanding its pathogenesis, which has facilitated research into therapeutics for the disease. Several compounds, including flupirtine, quinacrine, pentosan polysulfate, and doxycycline, have recently been used on a trial basis for patients with prion disease. Concomitantly, several lead antiprion compounds, including compound B (compB), IND series, and anle138b, have been discovered. Read More

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Almost a century of prion protein(s): From pathology to physiology, and back to pathology.

Biochem Biophys Res Commun 2017 02 28;483(4):1148-1155. Epub 2016 Aug 28.

Department of Biomedical Sciences, University of Padova, Via Bassi 58/B, 35131 Padova, Italy; C.N.R. Institute of Neuroscience, University of Padova, Via Bassi 58/B, 35131 Padova, Italy. Electronic address:

Prions are one of the few pathogens whose name is renowned at all population levels, after the dramatic years pervaded by the fear of eating prion-infected food. If now this, somehow irrational, scare of bovine meat inexorably transmitting devastating brain disorders is largely subdued, several prion-related issues are still unsolved, precluding the design of therapeutic approaches that could slow, if not halt, prion diseases. One unsolved issue is, for example, the role of the prion protein (PrP), whole conformational misfolding originates the prion but whose physiologic reason d'etre in neurons, and in cells at large, remains enigmatic. Read More

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February 2017

Disparate Modes of Evolution Shaped Modern Prion (PRNP) and Prion-Related Doppel (PRND) Variation in Domestic Cattle.

PLoS One 2016 25;11(5):e0155924. Epub 2016 May 25.

Department of Veterinary Pathobiology, College of Veterinary Medicine, Texas A&M University, College Station, Texas 77843-4467, United States of America.

Previous investigations aimed at determining whether the mammalian prion protein actually facilitates tangible molecular aspects of either a discrete or pleiotropic functional niche have been debated, especially given the apparent absence of overt behavioral or physiological phenotypes associated with several mammalian prion gene (PRNP) knockout experiments. Moreover, a previous evaluation of PRNP knockout cattle concluded that they were normal, suggesting that the bovine prion protein is physiologically dispensable. Herein, we examined the frequency and distribution of nucleotide sequence variation within the coding regions of bovine PRNP and the adjacent Doppel (PRND) gene, a proximal paralogue to PRNP on BTA13. Read More

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Effect of osmolytes on the conformation and aggregation of some amyloid peptides: CD spectroscopic data.

Data Brief 2016 Jun 4;7:1643-51. Epub 2016 May 4.

Biomaterials and Advanced Drug Delivery Laboratory, School of Medicine, Stanford University, Palo Alto, CA 94304, USA; Cardiovascular Pharmacology Division, Cardiovascular Institute, School of Medicine, Stanford University, Stanford, CA 94305, USA.

Protein misfolding and aggregation are responsible for a large number of diseases called protein conformational diseases or disorders that include Alzheimer׳s disease, Huntington׳s diseases, Prion related encephalopathies and type-II diabetes (http://dx.doi.org/10. Read More

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Polymorphism of amyloid fibrils formed by a peptide from the yeast prion protein Sup35: AFM and Tip-Enhanced Raman Scattering studies.

Ultramicroscopy 2016 06 30;165:26-33. Epub 2016 Mar 30.

Department of Pharmaceutical Sciences, University of Nebraska Medical Center, 986025 Nebraska Medical Center, Omaha, NE 68198, United States. Electronic address:

Aggregation of prion proteins is the cause of various prion related diseases. The infectious form of prions, amyloid aggregates, exist as multiple strains. The strains are thought to represent structurally different prion protein molecules packed into amyloid aggregates, but the knowledge on the structure of different types of aggregates is limited. Read More

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Metallothioneins in Prion- and Amyloid-Related Diseases.

J Alzheimers Dis 2016 ;51(3):637-56

Department of Chemistry and Biochemistry, Mendel University in Brno, Zemedelska 1, Brno, Czech Republic.

Prion and other amyloid-forming diseases represent a group of neurodegenerative disorders that affect both animals and humans. The role of metal ions, especially copper and zinc is studied intensively in connection with these diseases. Their involvement in protein misfolding and aggregation and their role in creation of reactive oxygen species have been shown. Read More

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December 2016

ERp57 as a novel cellular factor controlling prion protein biosynthesis: Therapeutic potential of protein disulfide isomerases.

Prion 2016 ;10(1):50-6

a Biomedical Neuroscience Institute, Faculty of Medicine, University of Chile , Santiago , Chile.

Disturbance of endoplasmic reticulum (ER) proteostasis is observed in Prion-related disorders (PrDs). The protein disulfide isomerase ERp57 is a stress-responsive ER chaperone up-regulated in the brain of Creutzfeldt-Jakob disease patients. However, the actual role of ERp57 in prion protein (PrP) biogenesis and the ER stress response remained poorly defined. Read More

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January 2017

Prion Diseases.

Continuum (Minneap Minn) 2015 Dec;21(6 Neuroinfectious Disease):1612-38

Purpose Of Review: This article presents an update on the clinical aspects of human prion disease, including the wide spectrum of their presentations.

Recent Findings: Prion diseases, a group of disorders caused by abnormally shaped proteins called prions, occur in sporadic (Jakob-Creutzfeldt disease), genetic (genetic Jakob-Creutzfeldt disease, Gerstmann-Sträussler-Scheinker syndrome, and fatal familial insomnia), and acquired (kuru, variant Jakob-Creutzfeldt disease, and iatrogenic Jakob-Creutzfeldt disease) forms. This article presents updated information on the clinical features and diagnostic methods for human prion diseases. Read More

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December 2015

Effects of lysine residues on structural characteristics and stability of tau proteins.

Biochem Biophys Res Commun 2015 Oct 14;466(3):486-92. Epub 2015 Sep 14.

Department of Mechanical Engineering Korea University, Seoul 136-701, Republic of Korea. Electronic address:

Pathological amyloid proteins have been implicated in neuro-degenerative diseases, specifically Alzheimer's, Parkinson's, Lewy-body diseases and prion related diseases. In prion related diseases, functional tau proteins can be transformed into pathological agents by environmental factors, including oxidative stress, inflammation, Aβ-mediated toxicity and covalent modification. These pathological agents are stable under physiological conditions and are not easily degraded. Read More

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October 2015

Neuroprotective effect of cellular prion protein (PrPC) is related with activation of alpha7 nicotinic acetylcholine receptor (α7nAchR)-mediated autophagy flux.

Oncotarget 2015 Sep;6(28):24660-74

Biosafety Research Institute, College of Veterinary Medicine, Chonbuk National University, Jeonju, Korea.

Activation of the alpha7 nicotinic acetylcholine receptor (α7nAchR) is regulated by prion protein (PrPC) expression and has a neuroprotective effect by modulating autophagic flux. In this study, we hypothesized that PrPC may regulate α7nAchR activation and that may prevent prion-related neurodegenerative diseases by regulating autophagic flux. PrP(106-126) treatment decreased α7nAchR expression and activation of autophagic flux. Read More

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September 2015