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Published online 19 March 2001. doi:10.1083/jcb.152.6.1247
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© The Rockefeller University Press, 0021-9525/2001//1247 $5.00
The Journal of Cell Biology, Volume 152, Number 6, , 2001 1247-1254

Original Article

Angiomotin

: An Angiostatin Binding Protein That Regulates Endothelial Cell Migration and Tube Formation



Boris Troyanovskya, Tetyana Levchenkoa, Göran Månssona, Olga Matvijenkoa, and Lars Holmgrena

a Center for Genomics Research and Microbiology and Tumor Biology Center, Karolinska Institutet, S-171 76 Stockholm, Sweden
CCK, R8: 03, Karolinska Hospital, S-171 76 Stockholm, Sweden.(4683) 3-9031(4685) 177-9317

lars.holmgren{at}cck.ki.se

Angiostatin, a circulating inhibitor of angiogenesis, was identified by its ability to maintain dormancy of established metastases in vivo. In vitro, angiostatin inhibits endothelial cell migration, proliferation, and tube formation, and induces apoptosis in a cell type–specific manner. We have used a construct encoding the kringle domains 1–4 of angiostatin to screen a placenta yeast two-hybrid cDNA library for angiostatin-binding peptides. Here we report the identification of angiomotin, a novel protein that mediates angiostatin inhibition of migration and tube formation of endothelial cells. In vivo, angiomotin is expressed in the endothelial cells of capillaries as well as larger vessels of the human placenta. Upon expression of angiomotin in HeLa cells, angiomotin bound and internalized fluorescein-labeled angiostatin. Transfected angiomotin as well as endogenous angiomotin protein were localized to the leading edge of migrating endothelial cells. Expression of angiomotin in endothelial cells resulted in increased cell migration, suggesting a stimulatory role of angiomotin in cell motility. However, treatment with angiostatin inhibited migration and tube formation in angiomotin-expressing cells but not in control cells. These findings indicate that angiostatin inhibits cell migration by interfering with angiomotin activity in endothelial cells.

Key Words: endothelium • neovascularization • migration • plasminogen • receptor

© 2001 The Rockefeller University Press

B. Troyanovsky and T. Levchenko contributed equally to this work.

Abbreviations used in this paper: β-gal, β-galactosidase; bFGF, basic fibroblast growth factor; FAK, focal adhesion kinase; GFP, green fluorescent protein; GST; glutathione S-transferase; HUVEC, human umbilical vein endothelial cell; MAE, mouse aortic endothelial; RT, reverse transcription.


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