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Blood, 15 March 2006, Vol. 107, No. 6, pp. 2330-2338.
Prepublished online as a Blood First Edition Paper on December 1, 2005; DOI 10.1182/blood-2005-04-1655.
 Previous Article | Table of Contents | Next Article 
HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY
The soluble extracellular domain of EphB4 (sEphB4) antagonizes EphB4-EphrinB2 interaction, modulates angiogenesis, and inhibits tumor growth
Nathalie Kertesz,
Valery Krasnoperov,
Ramachandra Reddy,
Lucy Leshanski,
S. Ram Kumar,
Sergey Zozulya, and
Parkash S. Gill
From Vasgene Therapeutics, Inc, and the Departments of Pathology, Surgery, and Medicine, Keck School of Medicine of the University of Southern California, Los Angeles, CA.
The receptor tyrosine kinase EphB4 and its ligand EphrinB2 play a crucial role in vascular development during embryogenesis. The soluble monomeric derivative of the extracellular domain of EphB4 (sEphB4) was designed as an antagonist of EphB4/EphrinB2 signaling. sEphB4 blocks activation of EphB4 and EphrinB2; suppresses endothelial cell migration, adhesion, and tube formation in vitro; and inhibits the angiogenic effects of various growth factors (VEGF and bFGF) in vivo. sEphB4 also inhibits tumor growth in murine tumor xenograft models. sEphB4 is thus a therapeutic candidate for vascular proliferative diseases and cancer.
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