Journal
JOURNAL OF BIOMEDICAL MATERIALS RESEARCH PART A
Volume 86A, Issue 2, Pages 535-543Publisher
WILEY
DOI: 10.1002/jbm.a.31658
Keywords
adhesion; integrins; monocyte; macrophage; fusion; biomedical polymers
Funding
- NIBIB NIH HHS [EB 000275, R01 EB000275, R37 EB000275] Funding Source: Medline
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An in vitro system of interleukin (IL)-4-induced foreign body giant cell (FBGC) formation was utilized to define the adhesion protein substrate(s) that promotes this aspect of the foreign body reaction on biomedical polymers. Human monocytes were cultured on cell culture polystyrene surfaces that had been pre-adsorbed with a synthetic arginine-glycine-aspartate peptide previously found to support optimal FBGC formation, or with various concentrations of potential physiological protein substrates, i.e. complement C3bi, collagen types I or IV, fibrinogen, plasma fibronectin, fibroblast fibronectin, laminin, thrombospondin, vitronectin, or von Willebrand factor. Cultures were evaluated on days 0 (1.5 h), 3, and 7 by May-Griinwald/Giemsa staining. Initial monocyte adhesion occurred on all adsorbed proteins. However, by day 7 of culture, only vitronectin was striking in its ability to support significant macrophage adhesion, development, and fusion leading to FBGC formation. Vitronectin supported high degrees of FBGC formation at an absorption concentration between 5 and 25 mu g/mL. These findings suggest that adsorbed vitronectin is critical in the cotlective events that support and promote FBGC formation on biomedical polymers, and that the propensity for vitronectin adsorption may underlie the material surface chemistry dependency of FBGC formation. (C) 2007 Wiley Periodicals, Inc.
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