Localization of matrix metalloproteinase MMP-2 to the surface of invasive cells by interaction with integrin alpha v beta 3

Cell. 1996 May 31;85(5):683-93. doi: 10.1016/s0092-8674(00)81235-0.


Cellular invasion depends on cooperation between adhesive and proteolytic mechanisms. Evidence is provided that the matrix metalloproteinase MMP-2 can be localized in a proteolytically active form on the surface of invasive cells, based on its ability to bind directly integrin alpha v beta 3. MMP-2 and alpha v beta 3 were specifically colocalized on angiogenic blood vessels and melanoma cells in vivo. Expression of alpha v beta 3 on cultured melanoma cells enabled their binding to MMP-2 in a proteolytically active form, facilitating cell-mediated collagen degradation. In vitro, these proteins formed an SDS-stable complex that depended on the noncatalytic C-terminus of MMP-2, since a truncation mutant lost the ability to bind alpha v beta 3. These findings define a single cell-surface receptor that regulates both matrix degradation and motility, thereby facilitating directed cellular invasion.

Publication types

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

MeSH terms

  • Animals
  • Cell Adhesion
  • Cell Membrane / metabolism
  • Chick Embryo
  • Cricetinae
  • Gelatinases / metabolism*
  • Humans
  • Matrix Metalloproteinase 2
  • Melanoma, Experimental / metabolism
  • Melanoma, Experimental / pathology
  • Melanoma, Experimental / secondary
  • Metalloendopeptidases / metabolism*
  • Neoplasm Invasiveness
  • Neovascularization, Pathologic
  • Receptors, Vitronectin / metabolism*
  • Solubility
  • Tumor Cells, Cultured
  • Vitronectin / metabolism


  • Receptors, Vitronectin
  • Vitronectin
  • Gelatinases
  • Metalloendopeptidases
  • Matrix Metalloproteinase 2