Inhibition of secreted phospholipases A2 by annexin V.: Competition for anionic phospholipid interfaces allows an assessment of the relative interfacial affinities of secreted phospholipases A2
Inhibition of secreted phospholipases A2 by annexin V.: Competition for anionic phospholipid interfaces allows an assessment of the relative interfacial affinities of secreted phospholipases A2
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DOI：
10.1016/s0005-2760(98)00026-5
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发表时间：
1998-04-22
期刊：
影响因子：
--
通讯作者：
Wilton, DC
中科院分区：
文献类型：
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作者：
Buckland, AG;Wilton, DC
膜联蛋白，特别是膜联蛋白1（脂皮质素1）抑制磷脂酶A（2）（PLA（2））的能力是众所周知的，底物消耗机制现在被广泛接受为大多数抑制研究的解释。在这项研究中，我们使用多种磷脂底物和分泌的PLA（2）（sPLA（2））检测了膜联蛋白V的底物消耗机制。结果表明，界面竞争一词最好地描述了膜联蛋白V的抑制作用，尽管总体抑制过程仍然是膜联蛋白对底物的封存过程之一。我们利用酶和膜联蛋白V对磷脂界面相互作用的竞争性质，作为定量sPLA（2）对阴离子磷脂囊泡的相对亲和力的手段。结果突出了人非胰腺sPLA（2）对这种囊泡的非常高的亲和力（K-d
The ability of annexins, particularly annexin 1 (lipocortin 1), to inhibit phospholipase A(2) (PLA(2)) is well known and a substrate depletion mechanism is now widely accepted as the explanation for most inhibitory studies. In this investigation we have examined the substrate depletion mechanism of annexin V using a variety of phospholipid substrates and secreted PLA(2)'s (sPLA(2)). The results suggest that the term interfacial competition best describes the inhibitory effect of annexin V although the overall inhibitory process remains one of substrate sequestration by the annexin. We have utilised the competitive nature of the interaction of enzyme and annexin V for a phospholipid interface as a means of quantifying the relative affinity of sPLA(2)'s for anionic phospholipid vesicles. The results highlight the very high affinity of the human non-pancreatic sPLA(2) for such vesicles (K-d