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首页> 外文期刊>Biochemistry >Competition of annexin V and anticardiolipin antibodies for binding to phosphatidylserine containing membranes.
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Competition of annexin V and anticardiolipin antibodies for binding to phosphatidylserine containing membranes.

机译：膜联蛋白V和抗心磷脂抗体竞争与含磷脂酰丝氨酸的膜结合。

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Annexin V, an intracellular protein with a calcium-dependent high affinity for anionic phospholipid membranes, acts as an inhibitor of lipid-dependent reactions of the blood coagulation. Antiphospholipid antibodies found in the plasma of patients with antiphospholipid syndrome generally do not interact with phospholipid membranes directly, but recognize (plasma) proteins associated with lipid membranes, mostly prothrombin or beta(2)-glycoprotein I (beta(2)GPI). Previously, it has been proposed that antiphospholipid antibodies may cause thrombosis by displacing annexin V from procoagulant cell surfaces. We used ellipsometry to study the binding of annexin V and of complexes of beta(2)GPI with patient-derived IgG antibodies to beta(2)GPI, commonly referred to as anticardiolipin antibodies (ACA), to phospholipid bilayers composed of phosphatidylcholine (PC) and 20% phosphatidylserine (PS). More specifically, we investigated the competition of these proteins for the binding sites at these bilayers. We show that ACA-beta(2)GPI complexes, adsorbed to PSPC bilayers, are displaced for more than 70% by annexin V and that annexin V binding is unaffected by the presence of ACA-beta(2)GPI complexes. Conversely, annexin V preadsorbed to these bilayers completely prevents adsorption of ACA-beta(2)GPI complexes, and none of the preadsorbed annexin V is displaced by ACA-beta(2)GPI complexes. Using ellipsometry, we also studied the effect of ACA-beta(2)GPI complexes on the interaction of annexin V with the membranes of ionophore-activated blood platelets as a more physiological relevant model of cell membranes. The experiments with blood platelets confirm the high-affinity binding of annexin V to these membranes and unequivocally show that annexin V binding is unaffected by the presence of ACA-beta(2)GPI. In conclusion, our data unambiguously show that ACA-beta(2)GPI complexes are unable to displace annexin V from procoagulant membranes to any significant extent, whereas annexin V does displace the majority of preadsorbed ACA-beta(2)GPI complexes from these membranes.
机译：膜联蛋白V是一种对阴离子磷脂膜具有钙依赖性高亲和力的细胞内蛋白，可作为血凝的脂质依赖性反应的抑制剂。在患有抗磷脂综合征的患者血浆中发现的抗磷脂抗体通常不直接与磷脂膜相互作用，但会识别与脂质膜相关的（血浆）蛋白，主要是凝血酶原或β（2）-糖蛋白I（beta（2）GPI）。以前，已经提出抗磷脂抗体可以通过从促凝细胞表面置换膜联蛋白V来引起血栓形成。我们使用椭偏仪研究了膜联蛋白V和β（2）GPI与患者衍生的IgG抗体对β（2）GPI的复合物（通常称为抗心磷脂抗体（ACA））与由磷脂酰胆碱（PC）组成的磷脂双层的结合）和20％的磷脂酰丝氨酸（PS）。更具体地说，我们研究了这些蛋白质对这些双层结合位点的竞争。我们显示，吸附到PSPC双层的ACA-beta（2）GPI复合物被膜联蛋白V置换超过70％，而膜联蛋白V的结合不受ACA-beta（2）GPI复合物的存在的影响。相反，膜联蛋白V预吸附到这些双层完全阻止了ACA-beta（2）GPI复合物的吸附，并且没有一个预吸附的膜联蛋白V被ACA-beta（2）GPI复合物取代。使用椭偏光度法，我们还研究了ACA-beta（2）GPI复合物对膜联蛋白V与离子载体激活的血小板膜相互作用的影响，这是一种更生理相关的细胞膜模型。用血小板进行的实验证实了膜联蛋白V与这些膜的高亲和力结合，并明确表明，膜联蛋白V的结合不受ACA-beta（2）GPI的存在的影响。总之，我们的数据清楚地表明，ACA-β（2）GPI复合物无法在很大程度上取代促凝膜上的膜联蛋白V，而膜联蛋白V确实能从这些膜上替代大多数预吸附的ACA-β（2）GPI复合物。

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