Cell adhesion and integrin binding to recombinant human fibrillin‐1

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Abstract
Fibrillin‐1 is a major constituent of tissue microfibrils 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 fibrillin‐1 polypeptides produced in a mammalian expression system in cell attachment and solid‐phase integrin binding assays. Fibrillin‐1 polypeptides containing the single RGD sequence located in the fourth 8‐cysteine domain, mediated distinct cell adhesion of a variety of cell lines and bound to purified integrin αVβ3. Integrins αIIbβ3, α5β1, α2β1 and α1β1 did not interact with any of the recombinant fibrillin‐1 peptides. Our results indicate a novel role for fibrillin‐1 in cellular interactions mediated via an RGD motif that is appropriately exposed for recognition by integrin αVβ3.