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通过其磷脂酰肌醇锚定物的代谢,胰岛素刺激脂蛋白脂肪酶的释放。

Insulin-stimulated release of lipoprotein lipase by metabolism of its phosphatidylinositol anchor.

作者信息

Chan B L, Lisanti M P, Rodriguez-Boulan E, Saltiel A R

机构信息

Laboratory of Biochemical Endocrinology, Rockefeller University, New York, NY 10021.

出版信息

Science. 1988 Sep 23;241(4873):1670-2. doi: 10.1126/science.241.4873.1670.

DOI:10.1126/science.241.4873.1670
PMID:2843987
Abstract

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.

摘要

脂蛋白脂肪酶(LPL)在血浆脂蛋白代谢中起关键作用。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的快速释放。胰岛素的一些代谢作用可能由特定磷脂酶的激活介导,该磷脂酶水解糖基磷脂酰肌醇(PI)分子。胰岛素敏感的糖基-PI在结构上类似于许多蛋白质的糖脂膜锚定物。LPL似乎通过糖基-PI锚定在3T3-L1细胞表面,胰岛素对其的快速释放可能是由于糖基-PI特异性磷脂酶C的激活。

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