Sortilin is the major 110-kDa protein in GLUT4 vesicles from adipocytes
Sortilin is the major 110-kDa protein in GLUT4 vesicles from adipocytes
复制标题
DOI：
10.1074/jbc.273.6.3582
复制
发表时间：
1998-02-06
影响因子：
4.8
通讯作者：
Lienhard, GE
中科院分区：
文献类型：
--
作者：
Morris, NJ;Ross, SA;Lienhard, GE
从大鼠脂肪细胞中提取的含有葡萄糖转运蛋白GLUT 4的囊泡中含有一个分子量为110 kDa的主要蛋白质，我们分离了该蛋白质，获得了肽段序列，并克隆了其大部分cDNA，这表明该蛋白质是分拣蛋白，一种新的膜蛋白，在这项工作进行的同时，在另一个背景下从人类来源克隆。大鼠和3 T3-L1脂肪细胞的亚细胞分级分离以及GLUT 4囊泡分离显示分拣蛋白主要位于含有GLUT 4的囊泡中的低密度微粒体中。通过细胞表面生物素化评估，胰岛素导致3 T3-L1脂肪细胞质膜上分拣蛋白的量增加1.7倍，分拣蛋白在3 T3-L1细胞中的表达仅发生在分化后。以前的特性分拣蛋白导致的建议，它的功能，从反式高尔基体的内腔蛋白质排序。其胰岛素刺激的增加在细胞表面和其表达的分化后的意义将需要明确的描绘其功能。
Vesicles containing the glucose transporter GLUT4 from rat adipocytes contain a major protein of 110 kDa, We have isolated this protein, obtained the sequences of peptides, and cloned a large portion of its cDNA, This revealed that the protein is sortilin, a novel membrane protein that was cloned in another context from a human source while this work was in progress. Subcellular fractionation of rat and 3T3-L1 adipocytes, together with GLUT4 vesicle isolation, showed that sortilin was primarily located in the low density microsomes in vesicles containing GLUT4, Insulin caused a 1.7-fold increase in the amount of sortilin at the plasma membranes of 3T3-L1 adipocytes, as assessed by cell surface biotinylation, The expression of sortilin in 3T3-L1 cells occurred only upon differentiation. Previous characterization of sortilin has led to the suggestion that it functions to sort lumenal proteins from the trans Golgi. The significance of its insulin stimulated increase at the cell surface and of its expression upon differentiation will require definitive delineation of its function.