Adsorption characteristics of human plasma fibronectin in relationship to cell adhesion
Adsorption characteristics of human plasma fibronectin in relationship to cell adhesion
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DOI：
10.1002/jbm.10151
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发表时间：
2002-08-01
期刊：
影响因子：
--
通讯作者：
Marciniak, E
中科院分区：
文献类型：
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作者：
Kowalczynska, HM;Nowak-Wyrzykowska, M;Marciniak, E
用多克隆抗血清和ELISA方法研究了人血浆纤维连接蛋白（FN）在非磺化和磺化聚合物表面的吸附。将ELISA信号记录为溶液中FN浓度的函数。FN结合的浓度依赖性显示在5-10 μ g/mL范围内的饱和效应。ELISA数据进行了讨论，在自组装单层和不同构象的FN分子。L1210细胞的早期粘附聚合物表面后，预先吸附FN在这些表面上进行了研究，在静态条件下。在FN吸附在磺化表面上的情况下，粘附细胞的相对数量随着界面表面张力的增加而增加（即，细胞粘附取决于磺酸基的表面密度）。然而，在FN吸附在非磺化表面上的情况下，粘附细胞的相对数量是低的，并且与界面表面张力无关。α（5）β（1）-整联蛋白的单克隆抗体阻断导致细胞粘附到吸附在磺化聚合物表面的FN的强烈抑制。这表明细胞粘附到吸附在这些表面上的FN主要是由α（5）β（1）-整联蛋白介导的。相反，在FN吸附在非磺化表面的情况下，细胞粘附不受α（5）β（1）-整联蛋白阻断的抑制。(C)2002 Wiley Periodicals，Inc.
Adsorption of human plasma fibronectin (FN) on nonsulfonated and sulfonated polymer surfaces was studied, by using a polyclonal antiserum to FN and the ELISA method. ELISA signal was recorded as a function of FN concentration in solutions. The concentration dependence of FN binding shows the saturation effect in the range 5-10 mug/mL. ELISA data are discussed in the terms of a self-assembled monolayer and different conformations of the FN molecule.The early adhesion of L1210 cells to polymer surfaces after prior adsorption of FN on these surfaces was studied under static conditions. In the case of FN adsorbed on sulfonated surfaces, the relative number of adhering cells increased with the increase of the interfacial surface tension (i.e., the cell adhesion depends on the surface density of sulfonic groups). However, in the case of FN adsorbed on nonsultonated surfaces, the relative number of adhering cells was low and independent on the interfacial surface tension.The alpha(5)beta(1)-integrin blocking by a monoclonal antibody resulted in a strong inhibition of the cell adhesion to FN adsorbed on sulfonated polymer surfaces. This indicates that cell adhesion to FN adsorbed on these surfaces is mostly mediated by the alpha(5)beta(1)-integrin. In contrast, in the case of FN adsorbed on nonsulfonated surfaces the cell adhesion was not inhibited by the alpha(5)beta(1)-integrin blocking. (C) 2002 Wiley Periodicals, Inc.