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-l and are missing in thrombospondin-5/COMP could contribute to this activity.
|Original language||English (US)|
|Number of pages||7|
|Journal||Biochemical and Biophysical Research Communications|
|State||Published - Jan 1 1995|
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology