Vitronectin is a critical protein adhesion substrate for IL-4-induced foreign body giant cell formation - PubMed (original) (raw)

Vitronectin is a critical protein adhesion substrate for IL-4-induced foreign body giant cell formation

Amy K McNally et al. J Biomed Mater Res A. 2008 Aug.

Abstract

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-Grünwald/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 microg/mL. These findings suggest that adsorbed vitronectin is critical in the collective 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.

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Figures

Fig 1

Fig 1

Monocyte/macrophage adhesion, morphology, and FBGC formation on RGD-modified polystyrene. RGD peptide was adsorbed at 25 μg per ml. Monocytes were plated and cultured for 1.5 hr (day 0), or until days 3 or 7. FBGC formation was induced with IL-4 on day 3. May-Grünwald/Giemsa. 20X

Fig. 2

Fig. 2

Adhesion to protein- or RGD-adsorbed polystyrene. Proteins or RGD peptide were adsorbed at a concentration of 25 μg per ml. Following removal of unadsorbed proteins by washing, monocytes were plated and cultured for 1.5 hr (day 0), or until days 3 or 7 and stained with May-Grünwald/Giemsa. FBGC formation was induced with IL-4 on day 3. Adhesion was determined as described in Methods. Results represent mean adherent cell number ± SEM, n = 3 different monocyte donors. *Significantly different from other adsorbed proteins (P<0.05).

Fig. 3

Fig. 3

Monocyte-to-macrophage development and FBGC formation on adsorbed proteins. CN I, C3bi, FG, FN, or VN were adsorbed at a concentration of 25 μg per ml. Monocytes were plated and cultured for 1.5 hr (day 0), or until days 3 or 7, and stained with May-Grünwald/Giemsa. FBGC formation was induced with IL-4 on day 3. 20X

Fig. 4

Fig. 4

Macrophage fusion protein- or RGD-adsorbed polystyrene. Proteins or RGD peptide were adsorbed at a concentration of 25 μg per ml. Monocytes were plated and cultured for 7 days as described in Methods with the IL-4-induction of macrophage fusion on day 3. Following May-Grünwald/Giemsa staining, percent macrophage fusion was determined. Results represent mean % fusion ± SEM, n = 3 different monocyte donors. *Significantly different from other adsorbed proteins (P<0.05).

Fig. 5

Fig. 5

VN-supported IL-4-induced FBGC formation: Concentration dependence. VN was not adsorbed or adsorbed at 2.5, 5, or 25 μg per ml, and monocytes were plated and cultured for 7 days as described in Methods with the IL-4-induction of macrophage fusion on day 3. May-Grünwald/Giemsa. 20X

Fig. 6

Fig. 6

VN-supported IL-4-induced macrophage fusion: Concentration dependence. VN was not adsorbed or adsorbed at the indicated concentrations, and monocytes were plated and cultured for 7 days as described in Methods with the IL-4-induction of macrophage fusion on day 3. Following May-Grünwald/Giemsa staining, percent macrophage fusion was determined. Results represent mean % fusion ± SEM, n = 3 different monocyte donors.

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