Cell adhesion and integrin binding to recombinant human fibrillin-1

Martin Pfaff, Dieter P. Reinhardt, Lynn Y. Sakai, Rupert Timpl

Research output: Contribution to journalArticlepeer-review

137 Scopus citations


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 aVP3.

Original languageEnglish (US)
Pages (from-to)247-250
Number of pages4
JournalFEBS Letters
Issue number3
StatePublished - Apr 22 1996
Externally publishedYes


  • Cell adhesion
  • Fibrillin-1
  • Integrin
  • RGD

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology


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