Censullo P, Davitz M A
Division of Immunology, New York University School of Medicine, NY 10016.
Semin Immunol. 1994 Apr;6(2):81-8. doi: 10.1006/smim.1994.1012.
Glycosylphosphatidylinositol (GPI)-anchored proteins comprise a diverse class of membrane molecules. They protect cells from complement-mediated lysis, control cell to cell adhesion, activate T cells, and play a role in the etiology of slow viral diseases. Despite their functional diversity, GPI-anchored proteins are all attached to the plasma membrane by a common glycolipid anchor. In this review we will examine how the GPI anchor is metabolized after arrival at the cell membrane. The conclusion is that break-down of the GPI anchor is potentially as diverse as the proteins themselves. The GPI-anchored protein can be endocytosed and degraded, cleaved and released, vesiculated, or exchanged onto another cell. The chimeric nature--lipid and protein--of the GPI-anchored molecules affords a unique window into the dynamic processes of lipid biosynthesis, movement, transport and maintenance.
糖基磷脂酰肌醇(GPI)锚定蛋白构成了一类多样的膜分子。它们保护细胞免受补体介导的裂解,控制细胞间黏附,激活T细胞,并在慢病毒疾病的病因学中发挥作用。尽管其功能多样,但GPI锚定蛋白均通过一种共同的糖脂锚定连接到质膜上。在本综述中,我们将研究GPI锚在到达细胞膜后是如何进行代谢的。结论是,GPI锚的分解可能与蛋白质本身一样具有多样性。GPI锚定蛋白可以被内吞并降解、切割并释放、形成囊泡或转移到另一个细胞上。GPI锚定分子的嵌合性质——脂质和蛋白质——为脂质生物合成、移动、运输和维持的动态过程提供了一个独特的窗口。