期刊
JOURNAL OF BIOMEDICAL MATERIALS RESEARCH
卷 61, 期 2, 页码 260-269出版社
JOHN WILEY & SONS INC
DOI: 10.1002/jbm.10151
关键词
fibronectin adsorption on polymer surfaces; cell adhesion to fibronectin; alpha(5)beta(1)-integrin; surface sulfonic groups
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.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据