Blood plasma contact activation on silicon, titanium and aluminium
Blood plasma contact activation on silicon, titanium and aluminium
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DOI：
10.1016/j.biomaterials.2006.11.005
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发表时间：
2007-03-01
期刊：
影响因子：
14
通讯作者：
Tengvall, Pentti
中科院分区：
文献类型：
--
作者：
Arvidsson, Sara;Askendal, Agneta;Tengvall, Pentti
在本工作中，我们在体外重新研究了自发性空气氧化硅、钛和铝的血浆蛋白沉积。用免疫椭圆偏振法和零椭圆偏振法检测和定量吸附的蛋白质，放射免疫分析法研究预吸附的I-125HSA在缓冲液或血浆中的保留情况，激肽释放酶特异性比色底物S-2302跟踪激肽释放酶的表面生成。结果表明，凝血和补体系统的接触激活通过凝血因子XII连接在硅和钛上，而不是通过凝血因子XII连接在铝上。预吸附的I-125-HSA最容易被硅取代，其次是钛和铝。在短时间和长时间暴露于血浆后，表面呈现不同的抗体结合模式。在血浆中，钛和硅结合抗HMWK 1分钟，而铝不结合。当等离子体孵育时间延长到2℃时，钛表面的抗HMWK结合完全消失，而硅表面的抗HMWK结合减少。在同一时间段，抗C3c结合增加到三种类型的表面。此外，在凝血因子XII缺乏的血浆中孵育或在正常血浆中加入特定的凝血因子XII(FXII)抑制物玉米胰酶抑制物(CTI)后，抗C3c与硅和钛结合的作用消失，但不包括铝。表面接触等离子体切割激肽释放酶专一性试剂S-2302，无论是在单一表面接触后，还是在新鲜血浆中重新孵育表面后。结果表明，Ob和因子XIIa及其降解产物保留在表面。(C)2006爱思唯尔有限公司。保留所有权利。
In the present work, blood plasma protein deposition to spontaneously air oxidized silicon, titanium and aluminium was re-investigated in vitro. Immunological- and null ellipsometry methods were used to detect and quantitate adsorbed proteins, RIA methods to study the retention of preadsorbed I-125-HSA upon exposure to buffer or blood plasma, and kallikrein-specific colorimetric substrate S-2302 to follow the surface generation of kallikrein.The results show that the contact activation of coagulation and complement systems are connected on Si and Ti, but not on Al, via coagulation factor XII. Preadsorbed I-125-HSA was most readily displaced on silicon, followed by titanium and aluminium. The surfaces displayed different antibody binding patterns after short and long-time exposures to plasma. Titanium and silicon bound anti-HMWK after 1 min in plasma, but aluminium did not. When the plasma incubation time was prolonged up to 2 It the anti-HMWK binding disappeared totally on titanium and decreased on silicon. During the same time period, anti-C3c binding increased to the three types of surfaces. Also, the anti-C3c binding onto Si and Ti, but not Al, disappeared after incubation in Factor XII deficient plasma or when a specific coagulation factor XII (Factor XII) inhibitor, corn trypsin inhibitor (CTI) was added to normal plasma. The surface contacted plasmas cleaved the kallikrein-specific reagent S-2302 both after single surface contact, and after reincubation of surfaces in fresh plasma. The results show that Ob and Factor XIIa and their degradation products were retained at the surfaces. (c) 2006 Elsevier Ltd. All rights reserved.