Angiopoietin-1 induces endothelial cell sprouting through the activation of focal adhesion kinase and plasmin secretion.

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Angiopoietin-1 (Ang1) is a strong inducer of endothelial cell sprouting, which is a first step in both angiogenesis and neovascularization. We examined the mechanisms underlying Ang1-induced cell sprouting using porcine pulmonary artery endothelial cells. Ang1 induced the nondirectional and directional migration of endothelial cells mediated through the Tie2 but not the Tie1 receptor. Ang1 induced tyrosine phosphorylation of p125(FAK), and this phosphorylation was dependent on phosphatidylinositol (PI) 3'-kinase activity. Ang1 induced the secretion of plasmin and matrix metalloproteinase-2 (MMP-2), which is inhibited by PI 3'-kinase inhibitors. Ang 1 also induced the secretion of small amounts of proMMP-3 and proMMP-9 but not proMMP-1. Ang1 suppressed the secretion of tissue inhibitor of metalloproteinase-2 (TIMP-2), but not of TIMP-1. Addition of alpha(2)-antiplasmin, a combination of TIMP-1 and TIMP-2, or PI 3'-kinase inhibitors inhibited Ang1-induced sprouting activity. Therefore, Ang1-induced sprouting activity in endothelial cells may be accomplished by cytoskeletal changes and secretion of proteinases and may be largely mediated through intracellular PI 3'-kinase activation.
Publisher
LIPPINCOTT WILLIAMS WILKINS
Issue Date
2000-05
Language
English
Article Type
Article
Keywords

MATRIX METALLOPROTEINASES; TIE2 RECEPTOR; IN-VITRO; ANGIOGENESIS; MIGRATION; GROWTH; MORPHOGENESIS; MECHANISMS; EXPRESSION; SURVIVAL

Citation

CIRCULATION RESEARCH, v.86, no.9, pp.952 - 959

ISSN
0009-7330
URI
http://hdl.handle.net/10203/77493
Appears in Collection
MSE-Journal Papers(저널논문)
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