Regulation of integrin function by the urokinase receptor

Science. 1996 Sep 13;273(5281):1551-5. doi: 10.1126/science.273.5281.1551.


Integrin function is central to inflammation, immunity, and tumor progression. The urokinase-type plasminogen activator receptor (uPAR) and integrins formed stable complexes that both inhibited native integrin adhesive function and promoted adhesion to vitronectin via a ligand binding site on uPAR. Interaction of soluble uPAR with the active conformer of integrins mimicked the inhibitory effects of membrane uPAR. Both uPAR-mediated adhesion and altered integrin function were blocked by a peptide that bound to uPAR and disrupted complexes. These data provide a paradigm for regulation of integrins in which a nonintegrin membrane receptor interacts with and modifies the function of activated integrins.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • CD18 Antigens / metabolism
  • Cell Adhesion*
  • Cell Line
  • Fibronectins / metabolism
  • Glycosylphosphatidylinositols / metabolism
  • Humans
  • Integrin beta1 / metabolism
  • Integrins / metabolism
  • Integrins / physiology*
  • Ligands
  • Molecular Sequence Data
  • Receptors, Cell Surface / metabolism*
  • Receptors, Cytoadhesin / metabolism*
  • Receptors, Urokinase Plasminogen Activator
  • Recombinant Fusion Proteins / metabolism
  • Transfection
  • Urokinase-Type Plasminogen Activator / metabolism
  • Vitronectin / metabolism


  • CD18 Antigens
  • Fibronectins
  • Glycosylphosphatidylinositols
  • Integrin beta1
  • Integrins
  • Ligands
  • PLAUR protein, human
  • Receptors, Cell Surface
  • Receptors, Cytoadhesin
  • Receptors, Urokinase Plasminogen Activator
  • Recombinant Fusion Proteins
  • Vitronectin
  • Urokinase-Type Plasminogen Activator