The Role of Crowded Physiological Environments in Prion and Prion-like Protein Aggregation
AbstractPrion 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. View Full-Text
Scifeed alert for new publicationsNever miss any articles matching your research from any publisher
- Get alerts for new papers matching your research
- Find out the new papers from selected authors
- Updated daily for 49'000+ journals and 6000+ publishers
- Define your Scifeed now
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.
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.