Title |
Heat shock protein 70 selectively mediates the degradation of cytosolic PrPs and restores the cytosolic PrP-induced cytotoxicity via a molecular interaction
|
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Published in |
Virology Journal, December 2012
|
DOI | 10.1186/1743-422x-9-303 |
Pubmed ID | |
Authors |
Jin Zhang, Ke Wang, Yan Guo, Qi Shi, Chan Tian, Cao Chen, Chen Gao, Bao-Yun Zhang, Xiao-Ping Dong |
Abstract |
Although the aggregation of PrPSc is thought to be crucial for the neuropathology of prion diseases, there is evidence in cultured cells and transgenic mice that neuronal death can be triggered by the accumulation of cytosolic PrPs, leading to the hypothesis that the accumulation of PrPs in the cytosol of neurons may be a primary neurotoxic culprit. Hsp70, a molecular chaperone involved in protein folding/refolding and degradation in the cytoplasm, has a protective effect in some models of neurodegenerative diseases, e.g., Alzheimer's and Parkinson's diseases, but its role in prion diseases remains unclear. |
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