Int. J. Mol. Sci. 2013, 14(11), 21339-21352; doi:10.3390/ijms141121339
Review

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

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Received: 31 August 2013; in revised form: 24 September 2013 / Accepted: 27 September 2013 / Published: 25 October 2013
(This article belongs to the Special Issue Protein Folding 2015)
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Abstract: 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.
Keywords: prion protein; Tau protein; prion-like protein; protein aggregation; macromolecular crowding; neurodegenerative diseases
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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MDPI and ACS Style

Ma, Q.; Hu, J.-Y.; Chen, J.; Liang, Y. The Role of Crowded Physiological Environments in Prion and Prion-like Protein Aggregation. Int. J. Mol. Sci. 2013, 14, 21339-21352.

AMA Style

Ma Q, Hu J-Y, Chen J, Liang Y. The Role of Crowded Physiological Environments in Prion and Prion-like Protein Aggregation. International Journal of Molecular Sciences. 2013; 14(11):21339-21352.

Chicago/Turabian Style

Ma, Qian; Hu, Ji-Ying; Chen, Jie; Liang, Yi. 2013. "The Role of Crowded Physiological Environments in Prion and Prion-like Protein Aggregation." Int. J. Mol. Sci. 14, no. 11: 21339-21352.


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