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

International Journal of Molecular Sciences

Qian Ma¹  Ji-Ying Hu¹  Jie Chen¹ 

[1] State Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan 430072, China;

关键词: prion protein;    Tau protein;    prion- like protein;    protein aggregation;    macromolecular crowding;    neurodegenerative diseases;   

DOI  :  10.3390/ijms141121339

来源: mdpi

【 摘 要 】

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.

【 授权许可】

CC BY   
© 2013 by the authors; licensee MDPI, Basel, Switzerland