Rubens F, Brash J, Weitz J, Kinlough-Rathbone R
Department of Pathology, McMaster University, Hamilton, Ontario, Canada.
J Biomed Mater Res. 1992 Dec;26(12):1651-63. doi: 10.1002/jbm.820261209.
During the investigation of fibrin deposition onto hydrophobic polymers in contact with human blood, a model was developed in which fibrinogen was denatured and irreversibly coated onto a polyethylene surface by heating to 70 degrees C for 10 min. The denatured fibrinogen-polyethylene surface is resistant to fluid wall shear rates of up to 550 s-1 and the fibrinogen does not desorb in the presence of plasma proteins. Compared to uncoated polyethylene, little albumin or fibrinogen adsorbs to heat-denatured fibrinogen. Thrombin binds to the denatured fibrinogen-coated polyethylene with low affinity and also acts on the surface-bound denatured fibrinogen and cleaves fibrinopeptide A (FPA) quantitatively. Washed, 51Cr-labeled platelets do not adhere to the thermally denatured fibrinogen at either low or high shear rates compared to surfaces coated with undenatured fibrinogen (p < 0.01). These observations support the role of the D domain of fibrinogen in platelet adhesion because this is the region that is denatured by heating. In contrast, the E domain of fibrinogen is not altered by heating to 70 degrees C and hence remains susceptible to thrombin and/or plasmin cleavage. The characteristics of this surface are such that it can be used to develop fibrin-coated surfaces for use in studies of thrombus formation on artificial surfaces.
在研究纤维蛋白在与人体血液接触的疏水性聚合物上的沉积过程中，开发了一种模型，即通过加热至70摄氏度10分钟，使纤维蛋白原变性并不可逆地包被在聚乙烯表面。变性纤维蛋白原 - 聚乙烯表面能抵抗高达550 s-1的流体壁剪切速率，并且在血浆蛋白存在的情况下纤维蛋白原不会解吸。与未包被的聚乙烯相比，很少有白蛋白或纤维蛋白原吸附到热变性的纤维蛋白原上。凝血酶以低亲和力结合到变性纤维蛋白原包被的聚乙烯上，并且也作用于表面结合的变性纤维蛋白原并定量切割纤维蛋白肽A（FPA）。与用未变性纤维蛋白原包被的表面相比，洗涤后的51Cr标记血小板在低剪切速率或高剪切速率下均不粘附于热变性的纤维蛋白原（p <0.01）。这些观察结果支持纤维蛋白原的D结构域在血小板粘附中的作用，因为这是加热会变性的区域。相比之下，纤维蛋白原的E结构域在加热至70摄氏度时不会改变，因此仍然易受凝血酶和/或纤溶酶的切割。该表面的特性使其可用于开发纤维蛋白包被的表面，用于人工表面上血栓形成的研究。
