To assess the ability of proteins of the thrombospondin family to inhi
bit angiogenesis, recombinant murine thrombospondin-2, bovine thrombos
pondin-2/CISP and thrombospondin-5/COMP were purified and tested for a
bility 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 inhibito
rs in vitro and in vivo whereas thrombospondin-5/COMP was inactive. Th
ese results define thrombospondin-2 as a newly identified naturally oc
curring 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 activit
y. (C) 1995 Academic Press,Inc.