Insulin-stimulated release of lipoprotein lipase by metabolism of its phosphatidylinositol anchor.
Insulin-stimulated release of lipoprotein lipase by metabolism of its phosphatidylinositol anchor.
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胰岛素通过其磷脂酰肌醇锚的代谢刺激脂蛋白脂肪酶的释放。
DOI：
10.1126/science.241.4873.1670
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发表时间：
1988
期刊：
影响因子：
--
通讯作者：
Saltiel,AR
中科院分区：
文献类型：
--
作者：
Chan,BL;Lisanti,MP;Rodriguez-Boulan,E;Saltiel,AR
脂蛋白脂肪酶（LPL）在血浆脂蛋白的代谢中起着至关重要的作用。在 3T3-L1 脂肪细胞中，胰岛素通过独立于能量代谢和蛋白质合成的机制引发 LPL 快速释放。胰岛素的一些代谢作用可能是由水解糖基磷脂酰肌醇 (PI) 分子的特定磷脂酶的激活介导的。胰岛素敏感的糖基-PI在结构上与许多蛋白质的糖脂膜锚相似。 LPL 似乎通过糖基-PI 锚定在 3T3-L1 细胞表面，胰岛素的快速释放可能是由于糖基-PI 特异性磷脂酶 C 的激活。
Lipoprotein lipase (LPL) plays a critical role in the metabolism of plasma lipoproteins. In 3T3-L1 adipocytes, insulin elicits the rapid release of LPL through mechanisms that are independent of energy metabolism and protein synthesis. Some of the metabolic actions of insulin may be mediated by the activation of a specific phospholipase that hydrolyzes a glycosyl phosphatidylinositol (PI) molecule. The insulin-sensitive glycosyl-PI is structurally similar to the glycolipid membrane anchor of a number of proteins. LPL appears to be anchored to the 3T3-L1 cell surface by glycosyl-PI, and its rapid release by insulin may be due to activation of a glycosyl-PI-specific phospholipase C.