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Vol. 15, Issue 8, 3580-3590, August 2004
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3
1 Integrin
The Burnham Institute, La Jolla, California 92037
Submitted March 19, 2004;
Revised May 22, 2004;
Accepted May 27, 2004
Monitoring Editor: Martin A. Schwartz
The NG2 proteoglycan is expressed by microvascular pericytes in newly formed blood vessels. We have used in vitro and in vivo models to investigate the role of NG2 in cross-talk between pericytes and endothelial cells (EC). Binding of soluble NG2 to the EC surface induces cell motility and multicellular network formation in vitro and stimulates corneal angiogenesis in vivo. Biochemical data demonstrate the involvement of both galectin-3 and 
3
1 integrin in the EC response to NG2 and show that NG2, galectin-3, and 31 form a complex on the cell surface. Transmembrane signaling via 31 is responsible for EC motility and morphogenesis in this system. Galectin-3–dependent oligomerization may potentiate NG2-mediated activation of 31. In conjunction with recent studies demonstrating the early involvement of pericytes in angiogenesis, these data suggest that pericyte-derived NG2 is an important factor in promoting EC migration and morphogenesis during the early stages of neovascularization.
Abbreviations used: bFGF, basic fibroblast growth factor; EC, endothelial cell(s); HMVEC, human microvascular endothelial cells; MAEC, mouse aortic endothelial cells; MALDI-TOF, matrix-assisted laser desorption ionization-time of flight; NG2/EC, extracellular domain of NG2; PDGF, platelet-derived growth factor.
* Corresponding author. E-mail address: fukushi{at}burnham.org.
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