title: Fibroblast adhesion to RGDS shows novel features compared with fibronectin.
abstract: As previously shown by others, the fibroblast attachment and spreading activity of fibronectin is mimicked by a short peptide (RGDS or longer) from the cell binding domain. Normal rat kidney fibroblasts showed similar attachment kinetics on either peptide GRGDSC or bovine plasma fibronectin and binding to either substratum was inhibited by peptide alone. We now demonstrate, however, considerable differences in biological activity between peptide and fibronectin. In particular, cells developed novel adhesion structures on peptide-coated substrata. Interference reflection microscopy showed a predominance of small round dark grey/black patches of adherent membrane ("spots") with relatively few focal adhesions, which occurred only at the outermost cell margins in contrast to their distribution in cells spread on fibronectin. The spots were resistant to detergent extraction and stained less strongly or not at all for vinculin. Electron microscopy in vertical thin section showed that the ventral surface of the cell was characterized by "point-contacts", corresponding in size to the spot structures seen by interference reflection microscopy, and which were only occasionally associated with microfilaments. Cells also required a higher substratum loading of peptide than fibronectin to promote spreading and proceeded to spread less rapidly and to a lesser extent, developing very few and extremely fine actin cables.
mesh_terms: D000199:Actins / Q000032:analysis; D000818:Animals; D001665:Binding Sites; D002448:Cell Adhesion; D002460:Cell Line; D002462:Cell Membrane / Q000648:ultrastructure; D005347:Fibroblasts / Q000378:metabolism* / Q000648:ultrastructure; D005353:Fibronectins / Q000378:metabolism*; D007668:Kidney; D009842:Oligopeptides / Q000378:metabolism*; D011485:Protein Binding; D051381:Rats; D013379:Substrate Specificity
chemical_list: D000199:Actins; D005353:Fibronectins; D009842:Oligopeptides; C046617:arginyl-glycyl-aspartyl-serine