Inhibition of angiogenesis by thrombospondin-2

Biochem Biophys Res Commun. 1995 Dec 5;217(1):326-32. doi: 10.1006/bbrc.1995.2780.


To assess the ability of proteins of the thrombospondin family to inhibit angiogenesis, recombinant murine thrombospondin-2, bovine thrombospondin-2/CISP and thrombospondin-5/COMP were purified and tested for ability to block the migration of capillary endothelial cells towards a variety of inducers and to inhibit neovascularization induced in the rat cornea. Both preparations of thrombospondin-2 were active inhibitors in vitro and in vivo whereas thrombospondin-5/COMP was inactive. These results define thrombospondin-2 as a newly identified naturally occurring inhibitor of angiogenesis and suggest that the properdin-like type 1 modules that it shares with antiangiogenic thrombospondin-1 and are missing in thrombospondin-5/COMP could contribute to this activity.

Publication types

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

MeSH terms

  • Adrenal Glands / blood supply
  • Adrenal Glands / drug effects
  • Animals
  • Cattle
  • Cell Adhesion Molecules / pharmacology*
  • Cell Adhesion Molecules / physiology
  • Cell Movement / drug effects
  • Corneal Neovascularization / prevention & control
  • Endothelium, Vascular / cytology
  • Endothelium, Vascular / drug effects
  • In Vitro Techniques
  • Membrane Glycoproteins / pharmacology*
  • Membrane Glycoproteins / physiology
  • Mice
  • Neovascularization, Physiologic / drug effects*
  • Rats
  • Recombinant Proteins / pharmacology
  • Thrombospondins


  • Cell Adhesion Molecules
  • Membrane Glycoproteins
  • Recombinant Proteins
  • Thrombospondins