Author: ["Jean-Sébastien Silvestre","Clotilde Théry","Ghislaine Hamard","Jacques Boddaert","Barbara Aguilar","Alain Delcayre","Christophe Houbron","Radia Tamarat","Olivier Blanc-Brude","Sylvia Heeneman","Michel Clergue","Micheline Duriez","Régine Merval","Bernard Lévy","Alain Tedgui","Sebastian Amigorena","Ziad Mallat"]
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Abstract
Vascular endothelial growth factor (VEGF)-induced blood vessel growth is involved in both physiological and pathological angiogenesis and requires integrin-mediated signaling. We now show that an integrin-binding protein initially described in milk-fat globule, MFG-E8 (also known as lactadherin), is expressed in and around blood vessels and has a crucial role in VEGF-dependent neovascularization in the adult mouse. Using neutralizing antibodies and lactadherin-deficient animals, we show that lactadherin interacts with αvβ3 and αvβ5 integrins and alters both VEGF-dependent Akt phosphorylation and neovascularization. In the absence of VEGF, lactadherin administration induced αvβ3- and αvβ5-dependent Akt phosphorylation in endothelial cells in vitro and strongly improved postischemic neovascularization in vivo. These results show a crucial role for lactadherin in VEGF-dependent neovascularization and identify lactadherin as an important target for the modulation of neovascularization.Cite this article
Silvestre, JS., Théry, C., Hamard, G. et al. Lactadherin promotes VEGF-dependent neovascularization. Nat Med 11, 499–506 (2005). https://doi.org/10.1038/nm1233 