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Functional Mammalian Amyloids and Amyloid-Like Proteins
Amyloids are highly ordered fibrous cross-β protein aggregates that are notorious primarily because of association with a variety of incurable human and animal diseases (termed amyloidoses), including Alzheimer’s disease (AD), Parkinson’s disease (PD), type 2 diabetes (T2D), and prion diseases. Some...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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MDPI
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7555005/ https://www.ncbi.nlm.nih.gov/pubmed/32825636 http://dx.doi.org/10.3390/life10090156 |
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author | Rubel, Maria S. Fedotov, Sergey A. Grizel, Anastasia V. Sopova, Julia V. Malikova, Oksana A. Chernoff, Yury O. Rubel, Aleksandr A. |
author_facet | Rubel, Maria S. Fedotov, Sergey A. Grizel, Anastasia V. Sopova, Julia V. Malikova, Oksana A. Chernoff, Yury O. Rubel, Aleksandr A. |
author_sort | Rubel, Maria S. |
collection | PubMed |
description | Amyloids are highly ordered fibrous cross-β protein aggregates that are notorious primarily because of association with a variety of incurable human and animal diseases (termed amyloidoses), including Alzheimer’s disease (AD), Parkinson’s disease (PD), type 2 diabetes (T2D), and prion diseases. Some amyloid-associated diseases, in particular T2D and AD, are widespread and affect hundreds of millions of people all over the world. However, recently it has become evident that many amyloids, termed “functional amyloids,” are involved in various activities that are beneficial to organisms. Functional amyloids were discovered in diverse taxa, ranging from bacteria to mammals. These amyloids are involved in vital biological functions such as long-term memory, storage of peptide hormones and scaffolding melanin polymerization in animals, substrate attachment, and biofilm formation in bacteria and fungi, etc. Thus, amyloids undoubtedly are playing important roles in biological and pathological processes. This review is focused on functional amyloids in mammals and summarizes approaches used for identifying new potentially amyloidogenic proteins and domains. |
format | Online Article Text |
id | pubmed-7555005 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-75550052020-10-14 Functional Mammalian Amyloids and Amyloid-Like Proteins Rubel, Maria S. Fedotov, Sergey A. Grizel, Anastasia V. Sopova, Julia V. Malikova, Oksana A. Chernoff, Yury O. Rubel, Aleksandr A. Life (Basel) Review Amyloids are highly ordered fibrous cross-β protein aggregates that are notorious primarily because of association with a variety of incurable human and animal diseases (termed amyloidoses), including Alzheimer’s disease (AD), Parkinson’s disease (PD), type 2 diabetes (T2D), and prion diseases. Some amyloid-associated diseases, in particular T2D and AD, are widespread and affect hundreds of millions of people all over the world. However, recently it has become evident that many amyloids, termed “functional amyloids,” are involved in various activities that are beneficial to organisms. Functional amyloids were discovered in diverse taxa, ranging from bacteria to mammals. These amyloids are involved in vital biological functions such as long-term memory, storage of peptide hormones and scaffolding melanin polymerization in animals, substrate attachment, and biofilm formation in bacteria and fungi, etc. Thus, amyloids undoubtedly are playing important roles in biological and pathological processes. This review is focused on functional amyloids in mammals and summarizes approaches used for identifying new potentially amyloidogenic proteins and domains. MDPI 2020-08-21 /pmc/articles/PMC7555005/ /pubmed/32825636 http://dx.doi.org/10.3390/life10090156 Text en © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Rubel, Maria S. Fedotov, Sergey A. Grizel, Anastasia V. Sopova, Julia V. Malikova, Oksana A. Chernoff, Yury O. Rubel, Aleksandr A. Functional Mammalian Amyloids and Amyloid-Like Proteins |
title | Functional Mammalian Amyloids and Amyloid-Like Proteins |
title_full | Functional Mammalian Amyloids and Amyloid-Like Proteins |
title_fullStr | Functional Mammalian Amyloids and Amyloid-Like Proteins |
title_full_unstemmed | Functional Mammalian Amyloids and Amyloid-Like Proteins |
title_short | Functional Mammalian Amyloids and Amyloid-Like Proteins |
title_sort | functional mammalian amyloids and amyloid-like proteins |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7555005/ https://www.ncbi.nlm.nih.gov/pubmed/32825636 http://dx.doi.org/10.3390/life10090156 |
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