Action of lipoprotein lipase on phospholipid monolayers. Activation by apolipoprotein C-II.
Action of lipoprotein lipase on phospholipid monolayers. Activation by apolipoprotein C-II.
复制标题
DOI：
10.1021/bi00278a033
复制
发表时间：
1983-04
期刊：
影响因子：
2.9
通讯作者：
P. Vainio;J. Virtanen;P. Kinnunen;J. Voyta;L. C. Smith;A. Gotto;J. Sparrow;F. Pattus;R. Verger
中科院分区：
文献类型：
--
作者：
P. Vainio;J. Virtanen;P. Kinnunen;J. Voyta;L. C. Smith;A. Gotto;J. Sparrow;F. Pattus;R. Verger
Petri Vainio、* Jorma A. Virtanen、Paavo K. J. Kinnunen、* John C. Voyta、Louis C. Smith、Antonio M. Gotto, Jr.、James T. Sparrow、Franc Pattus 和 Robert Verger 摘要：用单分子膜研究了脂蛋白脂肪酶的作用及其载脂蛋白 C-II (apoC-II) 的激活作用 L, 2-二十二烷酰基-5 «-甘油-3-磷酸甘油作为底物。无论存在还是不存在 apoC-II，酶速度和界面结合酶的比活性均显示出作为脂质堆积函数的钟形曲线。在高于 20 dyn cm"1 的临界表面压力时，单独的脂蛋白脂肪酶不再能够水解单层 1,2-二十二烷酰基-j-β-甘油-3-磷酸甘油。然而，在表面压力超过 40 dyn cm"1 时，脂蛋白脂肪酶很容易渗透到磷脂界面，而不受 apoC-II 的任何影响。 apoC-II 对脂蛋白脂肪酶的激活可归因于两个特定效应。在 20 dyn cm" 1 的临界表面压力以下，apoC-II 仅增加脂蛋白的周转数Ijipo 蛋白脂肪酶 (EC 3.1. 1.34) 是一种三酰甘油水解酶，位于外周组织（如心脏、肌肉和脂肪组织）的毛细血管内皮 [有关评论，请参阅 Smith 等人 (1978) 和 Kinnunen 等人 等（1983）]。它的作用似乎是消除环路的限速步骤
Petri Vainio,* Jorma A. Virtanen, Paavo K. J. Kinnunen,* John C. Voyta, Louis C. Smith, Antonio M. Gotto, Jr., James T. Sparrow, Franc Pattus, and Robert Verger abstract: Action of lipoprotein lipase and its activation by apolipoprotein C-II (apoC-II) were studied with monomolecular films of l, 2-didodecanoyl-5 «-glycero-3-phosphoglycerol as a substrate. The enzyme velocity and the specific activity of the interface-bound enzyme show a bell-shaped curve as a function of lipid packing, both in the presence and absence of apoC-II. Above critical surface pressure of 20 dyn cm" 1, lipoprotein lipasealone is no longer able to hydrolyze a monolayer of l, 2-didodecanoyl-j-«-glycero-3-phosphoglycerol. However, lipoprotein lipase readily penetrates into the phos-pholipid interface upto surface pressures exceeding 40 dyn cm" 1, without any effect by apoC-II. Activation of lipoprotein lipase by apoC-II can be assigned to be due to two specific effects. Below the critical surface pressure of 20 dyn cm" 1, apoC-II merely increases the turnover number of lipoproteinIjipoprotein lipase (EC 3.1. 1.34) is a triacylglycerol hy-drolase located at the capillary endothelium in peripheral tissues such as heart, muscle, and adipose tissue [for reviews, see Smith et al.(1978) and Kinnunen et al.(1983)]. Its action appears to be the rate-limiting step in the removal of circu-