Expanding spectrum of prion diseases.
| Autor: | Ayers JI; Institute for Neurodegenerative Diseases, Weill Institute for Neurosciences, University of California, San Francisco, San Francisco, CA, U.S.A.; Department of Neurology, Weill Institute for Neurosciences, University of California, San Francisco, San Francisco, CA, U.S.A., Paras NA; Institute for Neurodegenerative Diseases, Weill Institute for Neurosciences, University of California, San Francisco, San Francisco, CA, U.S.A.; Department of Neurology, Weill Institute for Neurosciences, University of California, San Francisco, San Francisco, CA, U.S.A., Prusiner SB; Institute for Neurodegenerative Diseases, Weill Institute for Neurosciences, University of California, San Francisco, San Francisco, CA, U.S.A.; Department of Neurology, Weill Institute for Neurosciences, University of California, San Francisco, San Francisco, CA, U.S.A.; Department of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, CA, U.S.A. |
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| Jazyk: | angličtina |
| Zdroj: | Emerging topics in life sciences [Emerg Top Life Sci] 2020 Sep 08; Vol. 4 (2), pp. 155-167. |
| DOI: | 10.1042/ETLS20200037 |
| Abstrakt: | Prions were initially discovered in studies of scrapie, a transmissible neurodegenerative disease (ND) of sheep and goats thought to be caused by slow viruses. Once scrapie was transmitted to rodents, it was discovered that the scrapie pathogen resisted inactivation by procedures that modify nucleic acids. Eventually, this novel pathogen proved to be a protein of 209 amino acids, which is encoded by a chromosomal gene. After the absence of a nucleic acid within the scrapie agent was established, the mechanism of infectivity posed a conundrum and eliminated a hypothetical virus. Subsequently, the infectious scrapie prion protein (PrPSc) enriched for β-sheet was found to be generated from the cellular prion protein (PrPC) that is predominantly α-helical. The post-translational process that features in nascent prion formation involves a templated conformational change in PrPC that results in an infectious copy of PrPSc. Thus, prions are proteins that adopt alternative conformations, which are self-propagating and found in organisms ranging from yeast to humans. Prions have been found in both Alzheimer's (AD) and Parkinson's (PD) diseases. Mutations in APP and α-synuclein genes have been shown to cause familial AD and PD. Recently, AD was found to be a double prion disorder: both Aβ and tau prions feature in this ND. Increasing evidence argues for α-synuclein prions as the cause of PD, multiple system atrophy, and Lewy body dementia. (© 2020 The Author(s). Published by Portland Press Limited on behalf of the Biochemical Society and the Royal Society of Biology.) |
| Databáze: | MEDLINE |
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