The molecular mechanism of the prion protein and the homolog which cause the neuro-degenerative/-protective function.

在本研究中，我们证实了Prion蛋白(PrP)与调节神经细胞内钙离子的谷氨酸I型受体(MGluR1)结合。因此，PrP的功能是通过与mGluR1受体相互作用来调节细胞内的钙离子，这提示神经元变性是由于这种机制的失败而引起的。PrP基因敲除小鼠(Ngsk PRNP-/-)的浦肯野细胞死亡和Prion病的神经变性可能是由该机制引起的。此外，我们还利用小鼠脑组织的cDNA文库，通过表达克隆的方法克隆了一个新的PrP内切相关基因：质膜泡相关蛋白(Plvap/PV-1)。此外，我们还证明了PrP的同源物DPL不受PrP感染的影响，而PrP的另一个同系物Shadoo可能促进PrPSc(异常类型的Prion蛋白)在培养细胞系统中的积累。

In this study, We proved that the Prion protein(PrP) bind to the glutaminic acid receptor type I (mGluR1) which regulated the Ca2+ in nerve cells. So the function of PrP is to regulate the Ca2+ in the cell by interacting with mGluR1 receptor, and this suggests that neuronal degeneration is caused by the adjustment this mechanism's failure. The Purkinje cell death in the PrP knockout mouse (Ngsk Prnp-/-) and the neurodegeneration of prion disease might be caused by this mechanism. In addition, We cloned a new PrP intracting gene : plasmalemma vesicle associated protein (Plvap/PV-1) by expression cloning method using the cDNA library from mouse brain. Additionally we proved that Dpl which is homolog of PrP isn't influenced prion infection, and Shadoo which is another homolog of PrP may promote accumulation of PrPSc(abnormal type of Prion protein) in culture cell systems.