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Amyloids assemble as part of recognizable structures during oogenesis in Xenopus

A hallmark of Alzheimer's, Huntington's and similar diseases is the assembly of proteins into amyloids rather than folding into their native state. There is an increasing appreciation that amyloids, under specific conditions, may be non-pathogenic. Here we show that amyloids form as a norm...

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Autores principales: Hayes, Michael H., Weeks, Daniel L.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Company of Biologists Ltd 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4920187/
https://www.ncbi.nlm.nih.gov/pubmed/27215327
http://dx.doi.org/10.1242/bio.017384
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author Hayes, Michael H.
Weeks, Daniel L.
author_facet Hayes, Michael H.
Weeks, Daniel L.
author_sort Hayes, Michael H.
collection PubMed
description A hallmark of Alzheimer's, Huntington's and similar diseases is the assembly of proteins into amyloids rather than folding into their native state. There is an increasing appreciation that amyloids, under specific conditions, may be non-pathogenic. Here we show that amyloids form as a normal part of Xenopus oocyte development. Amyloids are detectable in the cytosol and the nucleus using an amyloid binding dye and antibodies that recognize amyloid structure. In the cytosol, yolk platelets are amyloid reactive, as are a number of yet to be characterized particles. In the nucleus, we find particles associated with transcription by RNA polymerase I, II and III and RNA processing contain amyloids. Nuclear amyloids remain intact for hours following isolation; however, RNase treatment rapidly disrupts nuclear amyloids.
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spelling pubmed-49201872016-07-07 Amyloids assemble as part of recognizable structures during oogenesis in Xenopus Hayes, Michael H. Weeks, Daniel L. Biol Open Research Article A hallmark of Alzheimer's, Huntington's and similar diseases is the assembly of proteins into amyloids rather than folding into their native state. There is an increasing appreciation that amyloids, under specific conditions, may be non-pathogenic. Here we show that amyloids form as a normal part of Xenopus oocyte development. Amyloids are detectable in the cytosol and the nucleus using an amyloid binding dye and antibodies that recognize amyloid structure. In the cytosol, yolk platelets are amyloid reactive, as are a number of yet to be characterized particles. In the nucleus, we find particles associated with transcription by RNA polymerase I, II and III and RNA processing contain amyloids. Nuclear amyloids remain intact for hours following isolation; however, RNase treatment rapidly disrupts nuclear amyloids. The Company of Biologists Ltd 2016-05-23 /pmc/articles/PMC4920187/ /pubmed/27215327 http://dx.doi.org/10.1242/bio.017384 Text en © 2016. Published by The Company of Biologists Ltd http://creativecommons.org/licenses/by/3.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0), which permits unrestricted use, distribution and reproduction in any medium provided that the original work is properly attributed.
spellingShingle Research Article
Hayes, Michael H.
Weeks, Daniel L.
Amyloids assemble as part of recognizable structures during oogenesis in Xenopus
title Amyloids assemble as part of recognizable structures during oogenesis in Xenopus
title_full Amyloids assemble as part of recognizable structures during oogenesis in Xenopus
title_fullStr Amyloids assemble as part of recognizable structures during oogenesis in Xenopus
title_full_unstemmed Amyloids assemble as part of recognizable structures during oogenesis in Xenopus
title_short Amyloids assemble as part of recognizable structures during oogenesis in Xenopus
title_sort amyloids assemble as part of recognizable structures during oogenesis in xenopus
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4920187/
https://www.ncbi.nlm.nih.gov/pubmed/27215327
http://dx.doi.org/10.1242/bio.017384
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