Teoría Prión - Enfermedades Priónicas
PDF
HTML

Palabras clave

Encefalopatías Espongiformes
Enfermedades virales lentas
Enfermedades priónicas
Estructura molecular
Amiloide
Enfermedad de Alzheimer
Enfermedad de Parkinson (DECS)

Resumen

Un enorme progreso se ha logrado en la identificación, prevención, control y estudio de las enfermedades priónicas. El objetivo de esta actualización es presentar un breve Resumen de la historia de la Teoría Prión, de la participación nacional en relación con la salud humana y animal, así como algunos avances sobre la estructura molecular del amiloide priónico. Se explica, en parte, por qué hasta hoy solo tenemos en nuestro país presencia de la Enfermedad de Creutzfeldt-Jakob (ECJ) en su variedad esporádica y una ausencia comprobada de la Encefalopatía Espongiforme Bovina (EEB o “Enfermedad de las vacas locas”), lo que descarta la posible aparición de la variante de la ECJ (vCJ), de carácter zoonótico. Finalmente, como un avance reciente en investigación básica, se actualiza la evidencia experimental sobre una posible relación entre el amiloide de las enfermedades priónicas, el beta amiloide, ßA, de la enfermedad de Alzheimer y la alfa sinucleina de la enfermedad de Parkinson, que hasta hace muy poco se ha empezado a investigar. Se discute el mecanismo de neurotoxicidad, nucleación, transmisión del mal plegamiento y la restricción de su transmisión entre especies.

https://doi.org/10.22379/2422402215
PDF
HTML

Citas

AGUZZI A, HAASS C. Games played by rogue proteins in prion disorders and Alzheimer's disease. Science. 2003;302:814-8.

BRUNDIN P, MELKI R, KOPITO, R. Prion-like transmission of protein aggregates in neurodegenerative diseases. Nat. Rev. Mol. Cell Biol. 2010; 11, 301-307.

OLANOW CW, BRUNDIN P. Parkinson's disease and alpha synuclein: is Parkinson's disease a prion-like disorder? Mov Disord 2013; 28: 31-40.

TORO G, DÍAZ A, SAAD C. Ayer, hoy y mañana? de la teoría Prión. Acta Neurol Colomb. 2002;184:187-203.

KIRSBAUM WR. Creutzfeldt-Jakob Disease. New York-American Elsevier, 1968.

GAJDUSEK DC, GIBBS CJ JR, ALPERS M. Transmission and passage of experimenal "kuru" to chimpanzees. Science. 1967;155:212-4.

GAJDUSEK DC, GIBBS CJ JR, ALPERS M. Transmission and passage of experimenal "kuru" to chimpanzees. Science. 1967;155:212-4.

MATHEWS JD, GLASSE R, LINDENBAUM S. Kuru and cannibalism. Lancet. 1968;2:449-52.

DUFFY P, WOLF J, COLLINS G, DEVOE AG, STREETEN B, COWEN D. Possible person-to-person transmission of Creutzfeldt-Jakob disease. N Engl J Med. 1974;290:692

GRIFFITH JS. Self-replication and scrapie. Nature. 1967;215:1043-4.

LATARJET R, MUEL B, HAIG DA, CLARKE MC, ALPER T. Inactivation of the scrapie agent by near monochromatic ultraviolet light. Nature. 1970;227:1341-3.

PRUSINER SB. Novel proteinaceous infectious particles cause scrapie. Science. 1982;216:136-44.

CHIESA R, HARRIS DA. Prion diseases: what is the neurotoxic molecule? Neurobiol Dis. 2001;8:743-63.

FRADKIN JE, SCHONBERGER LB, MILLS JL, GUNN WJ, PIPER JM, WYSOWSKI DK, ET AL. Creutzfeldt-Jakob disease in pituitary growth hormone recipients in the United States. JAMA. 1991;265:880-4.

TORO G, PACHECO OE, SIERRA UE, BELTRAN M, DÍAZ A, PARRA EA, BONILLA E. Encefalopatías subagudas Espongiformes Transmisibles (ESET). La teoría prión-Enfermedades priónicas Acta Neurol Colomb. 2005;21:134-62.

BARON TG, BIACABE AG, BENCSIK A AND LANGEVELD JPM. Transmission of new bovine prion to mice. Emerg Infect Dis. 2006;12:1125-1128.

COMOY EE, CASALONEC, LESCOUTRA-ETCHEGARAY N, ZANUSSO G, FREIRE S, MARCÉ D, ET AL. 2008 Atypical BSE (BASE) Transmitted from Asymptomatic Aging Cattle to a Primate. PLoS ONE 3 (8): e3017. Doi:10.1371/journal.pone.0003017.

KONG Q, ZHENG M, CASALONE C, QUING L, HUANG S, CHAKRABORTY B, ET AL. Evaluation of the human transmission risk of an atypical bovine spongiform encephalopathy prion strain. J Virol. 2008;82:3697-701.

BERINGUE V, BENCSIK A, LE DUR A, REINE F, LAI TL, CHENAIS N, ET AL. TAFS Position Paper on Atypical scrapie and Atypical BSE. (May 16, 2007), Isolation from cattle of a Prion Strain distinct that causing Bovine Spongiform Encephalopathy. PLoS Pathogens. 2006;2:E112. 0956-0963.

CASALONE G, ZANUSSO P, ACUTIS S, FERRARI L, CAPUCCI F, TAGLIAVINI S, ET AL. Identification of a second bovine amyloidotic spongiform encephalopathy: Molecular similarities with sporadic Creutzfeldt-Jakob disease C. Proc Nat Acad Sci. 2004; 101:3065-70.

BUSCHMANN A, GRETZSCHEL A, BIACABE AG, SCHIEBEL K, CORONA C, HOFFMANN C, ET AL. Atypical BSE in Germany proof of transmissibility and biochemical characterization. Vet Microbiol. 2006;117:103-16.

ORGANIZACIÓN MUNDIAL DE SANIDAD ANIMAL OIE. Manual de las pruebas de Diagnóstico y de las Vacunas para los animales Terrestres. 2013; Capítulo 2.4.6 Encefalopatía espongiforme bovina (NB: Versión adoptada en mayo de 2010).

CAPOBIANCO R, CASALONE C, SUARDI S, MANGIERI M, MICCOLO C, LUMIDO L, ET AL. Conversion of the BASE Prion Strain into the BSE strain: The Origin of BSE. PLoS Pathogens. 2007;3:e31. 1-8.

AGUILAR-CALVO P, GARCÍA C, ESPINOSA JC. Prion and prion-like diseases in animals. Virus Res. (2014), http://dx.doi.org/10.1016/j.virusres.2014.11.026

LUNDMARK K,WESTERMARK GT, NYSTROM S, MURPHY CL, SOLOMON A, WESTERMARK P. Transmissibility of systemic amyloidosis by a prion-like mechanism. Proc. Natl. Acad. Sci. USA. 202; 99:6979-84

KRAUS A, GROVEMAN BR, CAUGHEY B. Prions and the Potential Transmissibility of Protein Misfolding Diseases. Annu. Rev. Microbiol. 2013. 67:543-64

BRAAK H, BRAAK E. Demonstration of amyloid deposits and neurofibrillary changes in whole brain sections. Brain Pathol. 1991;1:213-6.

HARDY J, SELKOE DJ. The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science. 2002;297:353-6.

STÖHR J, WATTS JC, MENSINGER ZL, OEHLER A, GRILLO SK, DEARMOND SJ, ET AL. Purified and synthetic Alzheimer's amyloid beta (A?) prions. Proc Natl Acad Sci U S A. 2012;109:11025-30.

EISELE YS, OBERMÜLLER U, HEILBRONNER G, BAUMANN F, KAESER SA, WOLBURG H, et al. Peripherally applied A beta-containing inoculates induce cerebral beta-amyloidosis. Science. 2010;330:980-82.

SCHENK D, BARBOUR R, DUNN W, GORDON G, GRAJEDA H, GUIDO T, ET AL. Immunization with amyloid-beta attenuates Alzheimer-disease-like pathology in the PDAPP mouse. Nature.1999; 400:173-7.

JANUS C, PEARSON J, MCLAURIN J, MATHEWS PM, JIANG Y, SCHMIDT SD, ET AL. A beta peptide immunization reduces behavioural impairment and plaques in a model of Alzheimer's disease. Nature. 2000; 408:979-82.

ORGOGOZO JM, GILMAN S, DARTIGUES JF, LAURENT B, PUEL M, KIRBY LC, ET AL. Subacute meningoencephalitis in a subset of patients with AD after Abeta42 immunization. Neurology. 2003;61:46-54.

GILMAN S, KOLLER M, BLACK RS, JENKINS L, GRIFFITH SG, FOX NC, ET AL. Clinical effects of Abeta immunization (AN1792) in patients with AD in an interrupted trial. Neurology. 2005;64:1553-62.

ANGOT E, STEINER JA, HANSEN C, LI JY, BRUNDIN P. Are synucleinopathies prion-like disorders? Lancet Neurol. 2010;9:1128-38.

DUNNING CJ, GEORGE S., AND BRUNDIN, P. (2013) What's to like about the prion-like hypothesis for the spreading of aggregated ?-synuclein in Parkinson disease? Prion 2013;7:92-7.

COLLINGE J. Prion diseases of humans and animals: their causes and molecular basis. Annu Rev Neurosci. 2001;24:519-50.

TORO G, ROMÁN G, URIBE C. Neurociencia. Contribución a la historia. Enfermedades "viejas" y "nuevas". Editor Mauricio Pérez. Instituto Nacional de Salud. Bogotá. Colombia. Primera edición. 2006: 1-113.

SHEWMAKER F, WICKNER RB, TYCKO R. Amyloid of the prion domain of Sup35p has an in-register parallel -sheet structure. Proc Natl Acad Sci USA.2006;103:19754-9.

BAXA U, WICKNER RB, STEVEN AC, ANDERSON D, MAREKOV L, YAU W-M, ET AL. Characterization of sheet structure in Ure2p1-89 yeast prion fibrils by solid state nuclear magnetic resonance. Biochemistry. 2007;46:13149-62.

CHIEN P, WEISSMAN JS, DEPACE AH. Emerging principles of conformation-based prion inheritance. Annu Rev Biochem. 2004;73:617-56.

RITTER C, MADDELEIN ML, SIEMER AB, LUHRS T, ERNST M, MEIER BH, ET AL. Correlation of structural elements and infectivity of the HET-s prion. Nature. 2005; 435:844-8.

WASMER C, LANGE A, VAN MELCKEBEKE H, SIEMER AB, RIEK R, MEIER BH. Amyloid fibrils of the HET-s(218-279) prion form a beta solenoid with a triangular hydrophobic core. Science. 2008;319:1523-6.

ANTZUTKIN ON, BALBACH JJ, LEAPMAN RD, RIZZO NW, REED J, TYCKO R. Multiple quantum solid-state NMR indicates a parallel, not antiparallel, organization of beta-sheets in Alzheimer's beta-amyloid fibrils. Proc Natl Acad Sci USA. 2000;97:13045-50.

TYCKO R. Molecular structure of amyloid fibrils: insights from solid-state NMR. Quart Revs Biophys. 2006;1:1-55

PETKOVA AT, YAU WM, TYCKO R. Experimental constraints on quaternary structure in Alzheimer's beta-amyloid fibrils. Biochemistry. 2006;45:498-512.

ANTZUTKIN ON, BALBACH JJ, TYCKO R. Site-specific identification of non-beta-strand conformations in Alzheimer's beta-amyloid fibrils by solid-state NMR. Biophys J. 2003;84:3326-35.

PARAVASTU AK, LEAPMAN RD, YAU WM, TYCKO R. Molecular structural basis for polymorphism in Alzheimer's -amyloid fibrils. Proc Natl Acad Sci USA. 2008; 105:18349-54.

ROSS ED, MINTON AP, WICKNER RB. Prion domains: sequences, structures and interactions. Nat Cell Biol. 2005;7:1039-44.

NICOLL AJ, PANICO S, FREIR DB, WRIGHT D, TERRY C, RISSE E, ET AL. Amyloid-ß nanotubes are associated with prion protein-dependent synaptotoxicity. Nat Commun. 2013;4:2416.

DERDOWSKI A, SINDI SS, KLAIPS CL, DISALVO S, SERIO TR. A size threshold limits prion transmission and establishes phenotypic diversity. Science. 2010;330:680-3.

PARK L, ZHOU J, ZHOU P, PISTICK R, EL JAMAL S, YOUNKIN L, ET AL. Innate Immunity receptor CD36 promotes cerebral amyloid angiopathy. Proc Natl Acad Sci U S A. 2013;110:3089-94. doi: 10.1073/pnas.1300021110.

PEGGION C, SORGATO MC, BERTOLI A. Prions and Prion-Like Pathogens in Neurodegenerative Disorders. Pathogens 2014;3:149-163; doi:10.3390/pathogens3010149.

COHEN SIA, AROSIO P, PRESTO J, KURUDENKANDY FR, BIVERSTAL H, DOLFE L, ET AL. A molecular chaperone braks the catalytic cycle that generate toxic AB oligomers. Nat Struct Mol Biol. 2015; Advanced publication doi:10.1038/nsmb.2971

ZHO M, OTTENBERG G, SFERRAZZA GF, HUBB C, FALLAHI M, RUMBAUGH G, ET AL. Neuronal death induced by misfolded prion protein is due to NAD+ deletion and can be relieved in vitro and in vivo by NAD+ replenishment. 2015; Advanced publication doi:10.1093/brain/awv002.

GJONESKA E, PFENNING AR, MATHYS H, QUON G, KUNDAJE A, TSAI LH, ET AL. Conserved epigenomic signals in mice and humans reveal immune basis of Alzheimer's disease. Nature. 2015; 518:365-72. doi:10.1038/nature14252.

GENEREUX JC, QU S, ZHOU MH, RYNO LM, WANG SY, SHOULDERS MD, ET AL. Embo J. 2015;31:4-19.

Creative Commons License

Esta obra está bajo una licencia internacional Creative Commons Atribución-NoComercial-SinDerivadas 4.0.

Descargas

Los datos de descargas todavía no están disponibles.