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How an Infection of Sheep Revealed Prion Mechanisms in Alzheimer's Disease and Other Neurodegenerative Disorders.
Carlson, George A; Prusiner, Stanley B.
Afiliación
  • Carlson GA; Institute for Neurodegenerative Diseases, Weill Institute for Neurosciences, University of California San Francisco, San Francisco, CA 94158, USA.
  • Prusiner SB; Department of Neurology, Weill Institute for Neurosciences, University of California San Francisco, San Francisco, CA 94158, USA.
Int J Mol Sci ; 22(9)2021 May 04.
Article en En | MEDLINE | ID: mdl-34064393
Although it is not yet universally accepted that all neurodegenerative diseases (NDs) are prion disorders, there is little disagreement that Alzheimer's disease (AD), Parkinson's disease, frontotemporal dementia (FTD), and other NDs are a consequence of protein misfolding, aggregation, and spread. This widely accepted perspective arose from the prion hypothesis, which resulted from investigations on scrapie, a common transmissible disease of sheep and goats. The prion hypothesis argued that the causative infectious agent of scrapie was a novel proteinaceous pathogen devoid of functional nucleic acids and distinct from viruses, viroids, and bacteria. At the time, it seemed impossible that an infectious agent like the one causing scrapie could replicate and exist as diverse microbiological strains without nucleic acids. However, aggregates of a misfolded host-encoded protein, designated the prion protein (PrP), were shown to be the cause of scrapie as well as Creutzfeldt-Jakob disease (CJD) and Gerstmann-Sträussler-Scheinker syndrome (GSS), which are similar NDs in humans. This review discusses historical research on diseases caused by PrP misfolding, emphasizing principles of pathogenesis that were later found to be core features of other NDs. For example, the discovery that familial prion diseases can be caused by mutations in PrP was important for understanding prion replication and disease susceptibility not only for rare PrP diseases but also for far more common NDs involving other proteins. We compare diseases caused by misfolding and aggregation of APP-derived Aß peptides, tau, and α-synuclein with PrP prion disorders and argue for the classification of NDs caused by misfolding of these proteins as prion diseases. Deciphering the molecular pathogenesis of NDs as prion-mediated has provided new approaches for finding therapies for these intractable, invariably fatal disorders and has revolutionized the field.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Scrapie / Péptidos beta-Amiloides / Proteínas tau / Alfa-Sinucleína / Enfermedad de Alzheimer / Proteínas Priónicas Tipo de estudio: Etiology_studies Idioma: En Revista: Int J Mol Sci Año: 2021 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Suiza

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Scrapie / Péptidos beta-Amiloides / Proteínas tau / Alfa-Sinucleína / Enfermedad de Alzheimer / Proteínas Priónicas Tipo de estudio: Etiology_studies Idioma: En Revista: Int J Mol Sci Año: 2021 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Suiza