蛋白质感染颗粒与二价铜离子

Prion and Cu^(2+)

蛋白质感染颗粒 (PrP)的错误折叠被认为是引起一些神经退化性疾病的主因 ,但其正常构象 (PrPC)的功能却一直不为人所知 .近年来研究发现 ,在正常细胞中 ,尤其是脑细胞中 ,细胞膜PrPC 可通过内吞作用进入细胞质而将Cu2 + 载运至SOD1,从而参与调节SOD1的活性及细胞铜代谢 .另有研究表明 ,Cu2 + 对于PrPSc (错误构象 )的蛋白水解酶K抗性的恢复及不同“病株”

Since Prusiner, suggested the prion hypothesis in 1982, a wealth of experiments have supported it to be true. However, the function of the cellular prion protein (PrPC) remains unclear. But recently evidence is showing that PrPC could specifically bind to Cu2+ and may transport Cu2+ to SOD1 by endocytosis from the plasma membrane via clathrin-coated pits so that taking part in copper metabolism. Moreover, other evidence also shows that Cu2+ could enhance the reversibility of denatured PrPSc and may determine the difference of some PrPSc strains.