Cell adhesion and integrin binding to recombinant human fibrillin-1

FEBS Lett. 1996 Apr 22;384(3):247-50. doi: 10.1016/0014-5793(96)00325-0.


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 alphaVbeta3. Integrins alphaIIbbeta3, alpha5beta1, alpha2beta1 and alpha1beta1 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 alphaVbeta3.

MeSH terms

  • Amino Acid Sequence
  • Binding Sites
  • Cell Adhesion
  • Cell Line
  • Fibrillin-1
  • Fibrillins
  • Fibrinogen / metabolism
  • Fibroblasts / cytology
  • Humans
  • Integrins / metabolism*
  • Microfilament Proteins / chemistry
  • Microfilament Proteins / isolation & purification
  • Microfilament Proteins / metabolism*
  • Molecular Sequence Data
  • Peptide Fragments / chemistry
  • Peptide Fragments / metabolism
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / isolation & purification
  • Recombinant Proteins / metabolism*
  • Sensitivity and Specificity
  • Tumor Cells, Cultured
  • Vitronectin / metabolism


  • FBN1 protein, human
  • Fibrillin-1
  • Fibrillins
  • Integrins
  • Microfilament Proteins
  • Peptide Fragments
  • Recombinant Proteins
  • Vitronectin
  • Fibrinogen