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Adsorption characteristics of human plasma fibronectin in relationship to cell adhesion. | LitMetric

AI Article Synopsis

  • The study examines the adsorption of human plasma fibronectin (FN) on both sulfonated and nonsulfonated polymer surfaces, utilizing ELISA to measure FN concentration.
  • It was found that FN binding reaches saturation between 5-10 microg/mL, with implications for FN structure and self-assembly on the surfaces.
  • Moreover, cell adhesion experiments demonstrated that sulfonated surfaces enhanced cell attachment via the alpha(5)beta(1)-integrin pathway, while nonsulfonated surfaces showed low cell adhesion independent of this integrin.

Article Abstract

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 microg/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 nonsulfonated 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.

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Source
http://dx.doi.org/10.1002/jbm.10151DOI Listing

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