Open Access
CD36: a critical anti-angiogenic receptor
Ronit Simantov1,Roy L Silverstein1
Division of Hematology-Oncology, Weill Medical College of Cornell University, 1300 York Avenue, New York, NY 10021, USA.
DOI: 10.2741/1168 Volume 8 Issue 6, pp.874-882
Published: 01 September 2003
(This article belongs to the Special Issue New insights into angiogenesis)

Thrombospondin-1 (TSP-1) is a potent inhibitor of angiogenesis in vivo and of microvascular endothelial cell responses to angiogenic factors in vitro. CD36 is the cellular receptor for TSP-1 on microvascular endothelium and is necessary for its anti-angiogenic activity. The anti-angiogenic activity of TSP-1 is contained in a structural domain known as the TSP type I repeat (TSR-1). TSR-1 domains occur in many other proteins, some of which have also been shown to have anti-angiogenic activity. Structure-function analyses have determined that binding of TSP-1 to CD36 is mediated by interaction of the TSR-1 domain of TSP with a conserved domain called CLESH-1 in CD36. Histidine rich glycoprotein, a plasma and cellular protein that blocks the binding of thrombospndin-1 to CD36, inhibits the antiangiogenic response to thrombospondin and may serve to modulate the thrombospondin/CD36 anti-angiogenic pathway. Several in vivo models support the role of the TSP/CD36 system in angiogenesis and tumor growth and provide evidence that the CD36 antiangiogenic pathway offers attractive therapeutic targets.

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Ronit Simantov, Roy L Silverstein. CD36: a critical anti-angiogenic receptor. Frontiers in Bioscience-Landmark. 2003. 8(6); 874-882.