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Paper Description


Lebectin, a Macrovipera lebetina venom-derived C-type lectin, inhibits angiogenesis both in vitro and in vivo


Authors: PILOGRET, Magali CONESA, Same SARRAY, Jonathan Michaud LEVESQUE, Salma DAOUD, Kwang Sik KIM, Michel Demeule, et al
Abstract: Integrins play an essential role in endothelial cell motility processes during angiogenesis and thus present interesting targets for the
development of new anti-angiogenic agents. Snake venoms naturally contain a variety of proteins that can affect integrin–ligand
interactions. Recently, the C-type lectin proteins (CLPs) have been characterized as efficient modulators of integrin functions. In this
study, we investigated the anti-angiogenic activity of lebectin, a newly discovered CLP from Macrovipera lebetina venom. Human brain
microvascular endothelial cells (HBMEC), used as an in vitro model, express avb3, avb5, and a5b1 integrins, as well as the a2, a3, a6, and
b4 subunits. Our data show that lebectin acts as a very potent inhibitor (IC500.5 nM) of HBMEC adhesion and migration on fibronectin
by blocking the adhesive functions of both the a5b1 and aV integrins. In addition, lebectin strongly inhibits both HBMEC in vitro
tubulogenesis on MatrigelTM (IC50¼0.4 nM) and proliferation. Finally, using both a chicken CAMassay and a MatrigelTM Plug assay in nude
mice, our results show that lebectin displays potent anti-angiogenic activity in vivo. Lebectin thus represents a new C-type lectin with
anti-angiogenic properties with great potential for the treatment of angiogenesis-related diseases.
Published in: J Cell Physiol;211(2):307-315
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