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

本研究证明朊蛋白（PrP）与调节神经细胞内Ca ~（2+）的谷氨酸受体（mGluR_1）结合。因此PrP的作用是通过与mGluR 1受体相互作用来调节细胞内Ca ~（2+），提示神经元变性是由于这种调节机制失效所致。PrP基因敲除小鼠（Ngsk Prnp-/-）的浦肯野细胞死亡和朊病毒病的神经退行性变可能是由这一机制引起的。另外，我们利用小鼠脑cDNA文库，通过表达克隆的方法，克隆了一个新的PrP内分泌基因：质膜囊泡相关蛋白（Plvap/PV-1）。此外，我们还证明了PrP的同源物Dpl不影响朊病毒的感染，而PrP的另一个同源物Shadoo可能促进PrPSc（异常型朊病毒蛋白）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.