膜联蛋白II抑制大鼠肝脏肝脂肪酶的钙依赖性磷脂酶A1和溶血磷脂酶活性，但不抑制三酰甘油脂肪酶活性。

Annexin II inhibits calcium-dependent phospholipase A1 and lysophospholipase but not triacyl glycerol lipase activities of rat liver hepatic lipase.

作者信息

Bohn E, Gerke V, Kresse H, Löffler B M, Kunze H

机构信息

Max-Planck-Institute für experimentelle Medizin, Göttingen, Germany.

出版信息

FEBS Lett. 1992 Jan 27;296(3):237-40. doi: 10.1016/0014-5793(92)80294-q.

DOI:10.1016/0014-5793(92)80294-q

PMID:1531641

Abstract

A member of the annexin family (the heterotetrameric annexin II2p11(2) complex purified from porcine intestinal epithelium) was tested for its ability to affect different calcium-dependent intrinsic lipolytic activities of rat liver hepatic lipase (HL). Whereas annexin II in the presence of calcium failed to interfere with HL triacyl glycerol lipase (EC 3.1.1.3) activity, it inhibited HL phospholipase A1 (EC 3.1.1.32) and lysophospholipase (EC 3.1.1.5) activities. Inhibition could be overcome by increasing the substrate concentration. Under phospholipase A1 assay conditions, annexin II did not bind to the purified HL enzyme. These results therefore suggest that only inhibitor/substrate interactions lead to inhibition of HL phospholipase A1 and lysophospholipase activities, an obviously general mechanism of phospholipase inhibition by annexins. Possible implications of HL inhibition in vivo by annexins are discussed.

摘要

对膜联蛋白家族的一个成员（从猪肠上皮中纯化得到的异源四聚体膜联蛋白II2p11(2)复合物）影响大鼠肝脏肝脂酶（HL）不同钙依赖性内在脂解活性的能力进行了测试。在有钙存在的情况下，膜联蛋白II未能干扰HL三酰甘油脂肪酶（EC 3.1.1.3）的活性，但它抑制了HL磷脂酶A1（EC 3.1.1.32）和溶血磷脂酶（EC 3.1.1.5）的活性。增加底物浓度可克服这种抑制作用。在磷脂酶A1测定条件下，膜联蛋白II不与纯化的HL酶结合。因此，这些结果表明，只有抑制剂/底物相互作用导致HL磷脂酶A1和溶血磷脂酶活性受到抑制，这显然是膜联蛋白抑制磷脂酶的一般机制。讨论了膜联蛋白在体内对HL抑制的可能影响。