IMMUNOLOCALIZATION OF FIBRONECTIN AND VITRONECTIN RECEPTORS IN HUMAN GINGIVAL FIBROBLASTS SPREADING ON TITANIUM SURFACES

The adhesion and spreading of human gingival fibroblasts on glass and differently processed titanium surfaces was studied by immunolocalization of vinculin and the alpha and beta subunits of the fibronectin (alpha(5) beta(1)) and vitronectin (alpha(v) beta 3) receptors. Vinculin-containing focal contacts were present both at 4 and 24 h of spreading in cells grown on glass or electropolished or etched titanium surfaces but not in cells spreading on sandblasted titanium surfaces. Immunostaining for the alpha 5 and beta 1 subunits of the fibronectin receptor showed only a diffuse membrane fluorescence after 4 h of cell spreading irrespective of the growth surface. The alpha(v) and beta(3) subunits of the vitronectin receptor were at this stage detected in focal contacts in cells spreading on glass or electropolished or etched titanium surfaces. In cells spreading on sandblasted titanium surfaces, however, the vitronectin receptor had only a diffuse distribution. In cells that had been allowed to spread for 24 h on glass or electropolished or etched titanium surfaces the alpha(5) and beta(1) integrin subunits were either diffusely distributed or showed a localization typical of extracellular matrix contacts. The alpha(v) and beta(3) integrin subunits were, as earlier, localized to typical focal contacts in cells grown on glass or electropolished or etched titanium surfaces. Cells attached to sandblasted titanium surfaces still expressed all the integrin subunits only diffusely. The results show that the surface texture of the substratum can affect the expression of integrin subunits in human gingival fibroblasts. As evidenced by the recruitment of integrin subunits to focal and extracellular matrix contacts, smooth or finely grooved titanium surfaces appear to be optimal in supporting the attachment of human gingival fibroblasts.