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Am J Physiol Heart Circ Physiol (May 19, 2006). doi:10.1152/ajpheart.01318.2005
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Submitted on December 14, 2005
Accepted on May 10, 2006

Signaling and regulation of endothelial cell survival by angiopoietin-2

Rania Harfouche1 and Sabah N. A. Hussain1*

1 Medicine, McGill University, Montreal, Canada

* To whom correspondence should be addressed. E-mail: sabah.hussain{at}muhc.mcgill.ca.

Angiopoietins are ligands for endothelial cell-specific Tie-2 receptors. While angiopoietin-1 (Ang-1) activates these receptors and promotes cell survival, migration and sprouting, little information is available regarding how angiopoietin-2 (Ang-2) influences these cells. In this study, we evaluated signaling pathways and biological effects of physiological concentrations of Ang-2 in cultured human umbilical vein endothelial cells. Ang-2 at 150 and 300 ng/ml elicited a transient (reaching peak values within 15 min of exposure) increase in the phosphorylation of Tie-2 receptors, protein kinase B (AKT), Erk1/2 and p38 members of the mitogen activated protein kinases. However, unlike Ang-1, Ang-2 significantly inhibited JNK/SAPK phosphorylation. When vascular endothelial growth factor (VEGF) was present along with Ang-2, Erk1/2 phosphorylation was inhibited whereas augmentation of Ang-1-induced Erk1/2 phosphorylation was triggered by VEGF. Ang-2 treatment had no effect on cell migration and in-vitro wound healing but significantly attenuated serum-deprivation-induced apoptosis and promoted survival. These effects were completely reversed by PI-3 kinase and Erk1/2 inhibitors but were augmented by an inhibitor of the p38 pathway. These results suggest that Ang-2 promotes endothelial cell survival through the Erk1/2 and PI-3 kinase pathways and that this angiopoietin is not a strong promoter of endothelial cell migration. We also conclude that the nature of interactions in terms of Erk1/2 activation between Ang-2 and VEGF is different from that of Ang-1 and VEGF.




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