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Vol. 11, Issue 9, 2885-2900, September 2000
3
1 Integrin
Modulates Endothelial Cell Responses to Thrombospondin-1
and
*Laboratory of Pathology, National Cancer Institute, National
Institutes of Health, Bethesda, Maryland 20892; and
Thrombospondin-1 (TSP1) can inhibit angiogenesis by interacting
with endothelial cell CD36 or proteoglycan receptors. We have now
identified Molecular Biology Institute, University of California Los
Angeles, Los Angeles, California 90025
3
1 integrin as an additional receptor for TSP1 that modulates angiogenesis and the in vitro behavior of endothelial cells. Recognition of TSP1 and an 31 integrin-binding
peptide from TSP1 by normal endothelial cells is induced after loss of cell-cell contact or ligation of CD98. Although confluent endothelial cells do not spread on a TSP1 substrate, 31 integrin
mediates efficient spreading on TSP1 substrates of endothelial cells
deprived of cell-cell contact or vascular endothelial cadherin
signaling. Activation of this integrin is independent of
proliferation, but ligation of the 31 integrin modulates
endothelial cell proliferation. In solution, both intact TSP1 and the
31 integrin-binding peptide from TSP1 inhibit
proliferation of sparse endothelial cell cultures independent of their
CD36 expression. However, TSP1 or the same peptide immobilized on the
substratum promotes their proliferation. The TSP1 peptide, when added
in solution, specifically inhibits endothelial cell migration and
inhibits angiogenesis in the chick chorioallantoic membrane, whereas a
fragment of TSP1 containing this sequence stimulates angiogenesis.
Therefore, recognition of immobilized TSP1 by 31 integrin
may stimulate endothelial cell proliferation and angiogenesis. Peptides
that inhibit this interaction are a novel class of angiogenesis inhibitors.
Corresponding author. E-mail address:
droberts{at}helix.nih.gov.
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