Wolff J M, Brümmendorf T, Rathjen F G
Max-Planck-Institut für Entwicklungsbiologie, Tübingen, Federal Republic of Germany.
Biochem Biophys Res Commun. 1989 Jun 15;161(2):931-8. doi: 10.1016/0006-291x(89)92688-0.
The mode of membrane insertion of F11 130 kDa protein, a neural chick cell surface glycoprotein involved in neurite fasciculation, has been investigated. Up to 41% of total F11 130 kDa is released from adult chick brain plasma membranes by phosphatidylinositol specific phospholipase C (PI-PLC), whereas no release is mediated by lecithin/cephalin specific phospholipase C (PLC). PI-PLC dependent release of F11 is also observed from embryonal chick brain plasma membranes and from the surface of intact retinal cells. Biosynthetic labelling experiments demonstrate that F11 contains ethanolamine. Taken together, these results suggest that F11 interacts with the plasma membrane at least partially through covalently linked glycosyl-phosphatidylinositol (GPI) or a structurally similar lipid.
已对F11 130 kDa蛋白（一种参与神经突束状化的鸡神经细胞表面糖蛋白）的膜插入模式进行了研究。高达41%的总F11 130 kDa可被磷脂酰肌醇特异性磷脂酶C（PI-PLC）从成年鸡脑细胞膜中释放出来，而卵磷脂/脑磷脂特异性磷脂酶C（PLC）则不会介导其释放。从胚胎鸡脑细胞膜和完整视网膜细胞表面也观察到F11依赖于PI-PLC的释放。生物合成标记实验表明，F11含有乙醇胺。综合这些结果表明，F11至少部分通过共价连接的糖基磷脂酰肌醇（GPI）或结构相似的脂质与细胞膜相互作用。
