Fibrillin-1 is a major constituent of tissue microfibrfls that occur in most connective tissues, either in close association with or independent of elastin. To test possible cell-adhesive functions of this protein, we used recombinant human fibrlllin-1 polypeptides produced in a mammalian expression system in cell attachment and solid-phase integrin binding assays. necessitates the use of buffers containing denaturing agents and cannot separate fibrillin-1 and fibrillin-2 [18], we chose to use recombinant human fibrillin-1 polypeptides for a study of possible cell-adhesive functions. These human fibrillin-1 peptides were produced in a mammalian expression system and purified under non-denaturing conditions [19]. Extensive characterization indicated correct folding [19]. Using an experimental approach already applied to characterize cell-adhesive and integrin-binding functions of fibulins [20], laminin [21] and collagen VI [22], we demonstrate the ability of cells to adhere to fibrillin-1 via an RGD motif located in the fourth 8-cysteine domain. In addition we identify integrin aV[33 as a major cellular receptor for this site.