PrPc介导的细胞信号转导

Cellular Signaling Mediated by Prion Protein

朊病毒病的发生是由于细胞正常朊蛋白PrPc转变成了异常构象的PrPc形式。PrPc的生理学功能目前尚不完全明确，可能与铜离子代谢、脂质摄取以及细胞信号传递有关。PrPc可以与小窝蛋白相互作用而活化Fyn非受体酪氨酸激酶从而引起下游信号通路的转导；可以作为受体与PrPc键合多肽结合后激活cAMP／PKA信号通路；以及引起细胞内钙离子浓度变化而活化信号通路。

The pathogenesis of prion disease is due to misfolding of the cellular prion protein （ PrPc） into a pathogenic isoform （ PrPc ） . Although biological functions of PrPc are still unclear it is assumed that PrPc plays an important role in copper metabolism, lipold absorption and cell sighal mediation. In addition, PrPc can interact with caveolin-1 to activate Fyn and act as a receptor to activate cAMP/PKA through interacting with PrPc-bound peptides and cellular signaling pathways by changing the level of intracellular calcium.