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The Role of Crowded Physiological Environments in Prion and Prion-like Protein Aggregation

Prion diseases and prion- like protein misfolding diseases are related to the accumulation of abnormal aggregates of the normal host proteins including prion proteins and Tau protein. These proteins possess self-templating and transmissible characteristics. The crowded physiological environments whe...

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Detalles Bibliográficos
Autores principales: Ma, Qian, Hu, Ji-Ying, Chen, Jie, Liang, Yi
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Molecular Diversity Preservation International (MDPI) 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3856008/
https://www.ncbi.nlm.nih.gov/pubmed/24284393
http://dx.doi.org/10.3390/ijms141121339
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author Ma, Qian
Hu, Ji-Ying
Chen, Jie
Liang, Yi
author_facet Ma, Qian
Hu, Ji-Ying
Chen, Jie
Liang, Yi
author_sort Ma, Qian
collection PubMed
description Prion diseases and prion- like protein misfolding diseases are related to the accumulation of abnormal aggregates of the normal host proteins including prion proteins and Tau protein. These proteins possess self-templating and transmissible characteristics. The crowded physiological environments where the aggregation of these amyloidogenic proteins takes place can be imitated in vitro by the addition of macromolecular crowding agents such as inert polysaccharides. In this review, we summarize the aggregation of prion proteins in crowded physiological environments and discuss the role of macromolecular crowding in prion protein aggregation. We also summarize the aggregation of prion- like proteins including human Tau protein, human α-synuclein, and human copper, zinc superoxide dismutase under macromolecular crowding environments and discuss the role of macromolecular crowding in prion- like protein aggregation. The excluded-volume effects caused by macromolecular crowding could accelerate the aggregation of neurodegenerative disease-associated proteins while inhibiting the aggregation of the proteins that are not neurodegenerative disease-associated.
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spelling pubmed-38560082013-12-09 The Role of Crowded Physiological Environments in Prion and Prion-like Protein Aggregation Ma, Qian Hu, Ji-Ying Chen, Jie Liang, Yi Int J Mol Sci Review Prion diseases and prion- like protein misfolding diseases are related to the accumulation of abnormal aggregates of the normal host proteins including prion proteins and Tau protein. These proteins possess self-templating and transmissible characteristics. The crowded physiological environments where the aggregation of these amyloidogenic proteins takes place can be imitated in vitro by the addition of macromolecular crowding agents such as inert polysaccharides. In this review, we summarize the aggregation of prion proteins in crowded physiological environments and discuss the role of macromolecular crowding in prion protein aggregation. We also summarize the aggregation of prion- like proteins including human Tau protein, human α-synuclein, and human copper, zinc superoxide dismutase under macromolecular crowding environments and discuss the role of macromolecular crowding in prion- like protein aggregation. The excluded-volume effects caused by macromolecular crowding could accelerate the aggregation of neurodegenerative disease-associated proteins while inhibiting the aggregation of the proteins that are not neurodegenerative disease-associated. Molecular Diversity Preservation International (MDPI) 2013-10-28 /pmc/articles/PMC3856008/ /pubmed/24284393 http://dx.doi.org/10.3390/ijms141121339 Text en © 2013 by the authors; licensee MDPI, Basel, Switzerland http://creativecommons.org/licenses/by/3.0/ This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).
spellingShingle Review
Ma, Qian
Hu, Ji-Ying
Chen, Jie
Liang, Yi
The Role of Crowded Physiological Environments in Prion and Prion-like Protein Aggregation
title The Role of Crowded Physiological Environments in Prion and Prion-like Protein Aggregation
title_full The Role of Crowded Physiological Environments in Prion and Prion-like Protein Aggregation
title_fullStr The Role of Crowded Physiological Environments in Prion and Prion-like Protein Aggregation
title_full_unstemmed The Role of Crowded Physiological Environments in Prion and Prion-like Protein Aggregation
title_short The Role of Crowded Physiological Environments in Prion and Prion-like Protein Aggregation
title_sort role of crowded physiological environments in prion and prion-like protein aggregation
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3856008/
https://www.ncbi.nlm.nih.gov/pubmed/24284393
http://dx.doi.org/10.3390/ijms141121339
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