ADSORPTION OF BABOON FIBRINOGEN AND THE ADHESION OF PLATELETS TO A THIN-FILM POLYMER DEPOSITED BY RADIOFREQUENCY GLOW-DISCHARGE OF ALLYLAMINE
ADSORPTION OF BABOON FIBRINOGEN AND THE ADHESION OF PLATELETS TO A THIN-FILM POLYMER DEPOSITED BY RADIOFREQUENCY GLOW-DISCHARGE OF ALLYLAMINE
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DOI：
10.1016/0142-9612(92)90057-u
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发表时间：
1992-01-01
期刊：
影响因子：
14
通讯作者：
HORBETT, TA
中科院分区：
文献类型：
--
作者：
CHINN, JA;RATNER, BD;HORBETT, TA
血小板粘附在静态和流动条件下，从洗涤后的血小板悬浮液中含有白蛋白的聚合物沉积的烯丙胺蒸汽的射频辉光放电的聚（对苯二甲酸乙二醇酯）基板上进行了测量。用于化学分析的电子能谱被用来表征表面。从一系列稀释的血浆溶液中的纤维蛋白原吸附到射频辉光放电/烯丙胺，使用I-125放射性标记的狒狒纤维蛋白原测量，随着血浆稀释度的降低而增加，其水平远高于先前在聚氨酯上观察到的水平。洗脱十二烷基硫酸钠从稀释血浆中吸附的纤维蛋白原也随着血浆浓度的增加而增加，但纤维蛋白原预吸附从血浆中变得不可洗脱时，表面储存在缓冲液中5天前与十二烷基硫酸钠接触。使用In-111放射性标记的狒狒血小板测定了血小板与稀释血浆预吸附基质的粘附性。粘附大大减少，用于预吸附的血浆浓度增加，表明非特异性血小板结合到裸露的表面时，蛋白质覆盖是不完整的。非特异性血小板结合被抑制到不同程度的预吸附不同的蛋白质的表面。与正常血浆相比，用稀释（1.0%）狒狒和缺乏纤维蛋白原的人血浆（即血清、热脱纤维蛋白原血浆和先天性无纤维蛋白原血浆）预吸附表面的血小板粘附减少。在缺乏的血浆中加入外源性纤维蛋白原可部分恢复血小板粘附至正常水平。粘附表面预吸附人血浆缺乏血管性血友病因子是与观察到的正常血浆。与纤维蛋白原缺乏媒体的血浆预吸附研究表明，吸附的纤维蛋白原是必要的血小板粘附到射频辉光放电/烯丙胺基板在高蛋白覆盖。然而，由于粘附性大大降低时，血浆预吸附基板被存储在缓冲液中血小板接触前，吸附的纤维蛋白原的构象也是重要的介导血小板粘附到射频辉光放电。
Platelet adhesion under static and flow conditions from a washed platelet suspension containing albumin to a polymer deposited by radio-frequency glow discharge of allylamine vapour on a poly(ethylene terephthalate) substrate was measured. Electron spectroscopy for chemical analysis was used to characterize the surface. Fibrinogen adsorption from a series of dilute plasma solutions to radio-frequency glow discharge/allylamine, measured using I-125 radiolabelled baboon fibrinogen, increased with decreasing plasma dilution to a level much higher than that previously observed on polyurethanes. Elutability by sodium dodecyl sulphate of fibrinogen adsorbed from dilute plasma also increased with increasing plasma concentration, but fibrinogen preadsorbed from plasma became non-elutable when surfaces were stored in buffer for 5 d before contact with sodium dodecyl sulphate. Platelet adhesion to substrates which had been pre-adsorbed with dilute plasma was measured using baboon platelets radiolabelled with In-111. Adhesion greatly decreased as the plasma concentration used for preadsorption increased, suggesting that non-specific platelet binding to the bare surface occurs when protein coverage is incomplete. Non-specific platelet binding was inhibited to varying degrees by preadsorption of different proteins to the surface. Platelet adhesion to surfaces preadsorbed with dilute (1.0%) baboon and human plasmas lacking fibrinogen (i.e. serum, heat-defibrinogenated plasma and congenitally afibrinogenemic plasma) was diminished compared with normal plasma. Addition of exogenous fibrinogen to the deficient plasma partially restored platelet adhesion to normal levels. Adhesion to surfaces preadsorbed with human plasma deficient in von Willebrand factor was comparable to that observed with normal plasma. The plasma preadsorption studies with fibrinogen deficient media suggested that adsorbed fibrinogen is necessary for platelet adhesion to the radio-frequency glow discharge/allylamine substrate at high protein coverage. However, since adhesion was greatly reduced when the plasma preadsorbed substrate was stored in buffer before platelet contact, the conformation of adsorbed fibrinogen is also important in mediating platelet adhesion to radio-frequency glow discharge.