Published online before print December 29, 2003, doi: 10.1161/01.RES.0000115555.05668.93
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Submitted on July 18, 2003
Revised on December 11, 2003
Accepted on December 17, 2003
4
1 Integrin Mediates Selective Endothelial Cell Responses to Thrombospondins 1 and 2 In Vitro and Modulates Angiogenesis In Vivo
Maria J. Calzada ;
From the Laboratory of Pathology (M.J.C., L.Z., J.M.S., J.Z., H.C.K., D.D.R.), National Cancer Institute, National Institutes of Health, Bethesda, Md; Department of Molecular, Cell and Developmental Biology (M.L.I.-A.), UCLA, Los Angeles, Calif; and the Department of Medicine (D.S.A., D.F.M.), University of Wisconsin-Madison, Madison, Wis.
* To whom correspondence should be addressed. E-mail: droberts{at}helix.nih.gov.
We examined the function of 
4
1 integrin in angiogenesis and in mediating endothelial cell responses to the angiogenesis modulators, thrombospondin-1 and thrombospondin-2. 41 supports adhesion of venous endothelial cells but not of microvascular endothelial cells on immobilized thrombospondin-1, vascular cell adhesion molecule-1, or recombinant N-terminal regions of thrombospondin-1 and thrombospondin-2. Chemotactic activities of this region of thrombospondin-1 and thrombospondin-2 are also mediated by 41, whereas antagonism of fibroblast growth factor-2-stimulated chemotaxis is not mediated by this region. Immobilized N-terminal regions of thrombospondin-1 and thrombospondin-2 promote endothelial cell survival and proliferation in an 41-dependent manner. Soluble 41 antagonists inhibit angiogenesis in the chick chorioallantoic membrane and neovascularization of mouse muscle explants. The latter inhibition is thrombospondin-1-dependent and not observed in explants from thrombospondin-1-/- mice. Antagonizing 41 may in part block proangiogenic activities of thrombospondin-1 and thrombospondin-2, because N-terminal regions of thrombospondin-1 and thrombospondin-2 containing the 41 binding sequence stimulate angiogenesis in vivo. Therefore, 41 is an important endothelial cell receptor for mediating motility and proliferative responses to thrombospondins and for modulation of angiogenesis.
Key words: adhesion • proliferation • migration • angiogenesis • peptides
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