期刊
SCIENCE
卷 298, 期 5599, 页码 1785-1788出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1073619
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资金
- NIGMS NIH HHS [GMS 25874] Funding Source: Medline
A rare conformation of the prion protein, PrPSc, is found only in mammals with transmissible prion diseases and represents either the infectious agent itself or a major component of it. The mechanism for initiating PrPSc formation is unknown. We report that PrP retrogradely transported out of the endoplasmic reticulum produced both amorphous aggregates and a PrPSc-like conformation in the cytosol. The distribution between these forms correlated with the rate of appearance in the cytosol. Once conversion to the PrPSc-like conformation occurred, it was sustained. Thus, PrP has an inherent capacity to promote its own conformational conversion in mammalian cells. These observations might explain the origin of PrPSc.
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