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RNA-binding protein FXR1 is presented in rat brain in amyloid form

Amyloids are β-sheets-rich protein fibrils that cause neurodegenerative and other incurable human diseases affecting millions of people worldwide. However, a number of proteins is functional in the amyloid state in various organisms from bacteria to humans. Using an original proteomic approach, we i...

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Autores principales: Sopova, Julia V., Koshel, Elena I., Belashova, Tatiana A., Zadorsky, Sergey P., Sergeeva, Alexandra V., Siniukova, Vera A., Shenfeld, Alexandr A., Velizhanina, Maria E., Volkov, Kirill V., Nizhnikov, Anton A., Kachkin, Daniel V., Gaginskaya, Elena R., Galkin, Alexey P.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6908614/
https://www.ncbi.nlm.nih.gov/pubmed/31831836
http://dx.doi.org/10.1038/s41598-019-55528-6
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author Sopova, Julia V.
Koshel, Elena I.
Belashova, Tatiana A.
Zadorsky, Sergey P.
Sergeeva, Alexandra V.
Siniukova, Vera A.
Shenfeld, Alexandr A.
Velizhanina, Maria E.
Volkov, Kirill V.
Nizhnikov, Anton A.
Kachkin, Daniel V.
Gaginskaya, Elena R.
Galkin, Alexey P.
author_facet Sopova, Julia V.
Koshel, Elena I.
Belashova, Tatiana A.
Zadorsky, Sergey P.
Sergeeva, Alexandra V.
Siniukova, Vera A.
Shenfeld, Alexandr A.
Velizhanina, Maria E.
Volkov, Kirill V.
Nizhnikov, Anton A.
Kachkin, Daniel V.
Gaginskaya, Elena R.
Galkin, Alexey P.
author_sort Sopova, Julia V.
collection PubMed
description Amyloids are β-sheets-rich protein fibrils that cause neurodegenerative and other incurable human diseases affecting millions of people worldwide. However, a number of proteins is functional in the amyloid state in various organisms from bacteria to humans. Using an original proteomic approach, we identified a set of proteins forming amyloid-like aggregates in the brain of young healthy rats. One of them is the FXR1 protein, which is known to regulate memory and emotions. We showed that FXR1 clearly colocalizes in cortical neurons with amyloid-specific dyes Congo-Red, Thioflavines S and T. FXR1 extracted from brain by immunoprecipitation shows yellow-green birefringence after staining with Congo red. This protein forms in brain detergent-resistant amyloid oligomers and insoluble aggregates. RNA molecules that are colocalized with FXR1 in cortical neurons are insensitive to treatment with RNase A. All these data suggest that FXR1 functions in rat brain in amyloid form. The N-terminal amyloid-forming fragment of FXR1 is highly conserved across mammals. We assume that the FXR1 protein may be presented in amyloid form in brain of different species of mammals, including humans.
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spelling pubmed-69086142019-12-16 RNA-binding protein FXR1 is presented in rat brain in amyloid form Sopova, Julia V. Koshel, Elena I. Belashova, Tatiana A. Zadorsky, Sergey P. Sergeeva, Alexandra V. Siniukova, Vera A. Shenfeld, Alexandr A. Velizhanina, Maria E. Volkov, Kirill V. Nizhnikov, Anton A. Kachkin, Daniel V. Gaginskaya, Elena R. Galkin, Alexey P. Sci Rep Article Amyloids are β-sheets-rich protein fibrils that cause neurodegenerative and other incurable human diseases affecting millions of people worldwide. However, a number of proteins is functional in the amyloid state in various organisms from bacteria to humans. Using an original proteomic approach, we identified a set of proteins forming amyloid-like aggregates in the brain of young healthy rats. One of them is the FXR1 protein, which is known to regulate memory and emotions. We showed that FXR1 clearly colocalizes in cortical neurons with amyloid-specific dyes Congo-Red, Thioflavines S and T. FXR1 extracted from brain by immunoprecipitation shows yellow-green birefringence after staining with Congo red. This protein forms in brain detergent-resistant amyloid oligomers and insoluble aggregates. RNA molecules that are colocalized with FXR1 in cortical neurons are insensitive to treatment with RNase A. All these data suggest that FXR1 functions in rat brain in amyloid form. The N-terminal amyloid-forming fragment of FXR1 is highly conserved across mammals. We assume that the FXR1 protein may be presented in amyloid form in brain of different species of mammals, including humans. Nature Publishing Group UK 2019-12-12 /pmc/articles/PMC6908614/ /pubmed/31831836 http://dx.doi.org/10.1038/s41598-019-55528-6 Text en © The Author(s) 2019 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Article
Sopova, Julia V.
Koshel, Elena I.
Belashova, Tatiana A.
Zadorsky, Sergey P.
Sergeeva, Alexandra V.
Siniukova, Vera A.
Shenfeld, Alexandr A.
Velizhanina, Maria E.
Volkov, Kirill V.
Nizhnikov, Anton A.
Kachkin, Daniel V.
Gaginskaya, Elena R.
Galkin, Alexey P.
RNA-binding protein FXR1 is presented in rat brain in amyloid form
title RNA-binding protein FXR1 is presented in rat brain in amyloid form
title_full RNA-binding protein FXR1 is presented in rat brain in amyloid form
title_fullStr RNA-binding protein FXR1 is presented in rat brain in amyloid form
title_full_unstemmed RNA-binding protein FXR1 is presented in rat brain in amyloid form
title_short RNA-binding protein FXR1 is presented in rat brain in amyloid form
title_sort rna-binding protein fxr1 is presented in rat brain in amyloid form
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6908614/
https://www.ncbi.nlm.nih.gov/pubmed/31831836
http://dx.doi.org/10.1038/s41598-019-55528-6
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