Cell adhesion to tropoelastin is mediated via the C-terminal GRKRK motif and integrin alphaVbeta3

J Biol Chem. 2009 Oct 16;284(42):28616-23. doi: 10.1074/jbc.M109.017525. Epub 2009 Jul 18.


Elastin fibers are predominantly composed of the secreted monomer tropoelastin. This protein assembly confers elasticity to all vertebrate elastic tissues including arteries, lung, skin, vocal folds, and elastic cartilage. In this study we examined the mechanism of cell interactions with recombinant human tropoelastin. Cell adhesion to human tropoelastin was divalent cation-dependent, and the inhibitory anti-integrin alpha(V)beta(3) antibody LM609 inhibited cell spreading on tropoelastin, identifying integrin alpha(V)beta(3) as the major fibroblast cell surface receptor for human tropoelastin. Cell adhesion was unaffected by lactose and heparin sulfate, indicating that the elastin-binding protein and cell surface glycosaminoglycans are not involved. The C-terminal GRKRK motif of tropoelastin can bind to cells in a divalent cation-dependent manner, identifying this as an integrin binding motif required for cell adhesion.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Motifs
  • Animals
  • Cattle
  • Cell Adhesion
  • Dose-Response Relationship, Drug
  • Elastin / chemistry
  • Extracellular Matrix / metabolism
  • Fibroblasts / metabolism
  • Humans
  • Integrin alphaVbeta3 / chemistry*
  • Models, Biological
  • Protein Structure, Tertiary
  • Receptors, Cell Surface / chemistry
  • Skin / cytology
  • Tropoelastin / chemistry
  • Tropoelastin / metabolism*


  • Integrin alphaVbeta3
  • Receptors, Cell Surface
  • Tropoelastin
  • elastin-binding proteins
  • Elastin