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Tytuł oryginału: Adsorption characteristics of human plasma fibronectin in relationship to cell adhesion.
Autorzy: Kowalczyńska Hanna M., Nowak-Wyrzykowska Małgorzata, Dobkowski Jacek, Kołos Robert, Kamiński Jarosław, Makowska-Cynka Alicja, Marciniak Ewa
Źródło: J. Biomed. Mater. Res. 2002: 61 (2) s.260-269, il., tab., bibliogr. 57 poz.
Sygnatura GBL: 305,818

Hasła klasyfikacyjne GBL:
  • hematologia
  • onkologia

    Typ dokumentu:
  • praca doświadczalna
  • praca opublikowana za granicą
  • tytuł obcojęzyczny

    Wskaźnik treści:
  • zwierzęta
  • myszy
  • in vitro

    Streszczenie angielskie: 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 ćg/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 ŕ5á1-integrin blocking by a monoclonal antibody resulted on sulfonated polymer surfaces. This indicates that cell adhesion to FN adsorbed on these surfaces is mostly mediated by the ŕ5á1-integrin. In contrast, in the case of FN adsorbed on nonsulfonated surfaces the cell adhesion was not inhibited by the ŕ5á1-integrin blocking.

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