Mechanisms of serum protein binding and cell anchorage to immobilized serotonin and indole analogs.

Bovine aortal endothelial cells, bovine smooth muscle cells, chick embryo fibroblasts, and baby hamster kidney cells all attached and grew on immobilized tryptamine or L-tryptophan as successfully as on immobilized serotonin. A detailed investigation employing different serum compositions combined with cell blotting and immunoblotting techniques revealed that adhesion of cells to each of the immobilized indole analogs was mediated by vitronectin and fibronectin. Quantitative analyses revealed major differences in the variety of serum proteins adsorbed to each of the immobilized indole analogs and in particular major differences in the amounts of adsorbed vitronectin. However, similar levels of adsorbed fibronectin and fibronectin fragments were found on each of the immobilized indole analogs. The results indicate that (i) different composites of surface-adsorbed proteins may be directed by chemical differences between the immobilized indole analogs and (ii) mammalian cells may still populate chemically different surfaces with equal success despite differences in the surface profiles of adsorbed serum proteins.