Lebectin and lebecetin, two C-type lectins from snake venom, inhibit alpha5beta1 and alphaV-containing integrins.

Abstract : Integrins are essential protagonists in the complex multistep process of cancer progression and metastasis. We recently reported that lebectin, a novel C-type lectin from Macrovipera lebetina venom, displays an anti-integrin activity. In this study, we extend this observation to lebecetin, a second C-type lectin isolated from the same venom and previously reported as a potent inhibitor of platelet aggregation. Both venom lectins appear to exert their effect on cell adhesion, migration, invasion and proliferation by inhibiting alpha5beta1 and alphav-containing integrins. Moreover, the inhibition of alpha5beta1 and alphav integrins is likely due to the binding of venom peptides, as both lebectin and lebecetin co-immunoprecipitate with these integrins. Lebectin and lebecetin are thus the first examples of venom C-type lectins inhibiting an integrin other than the collagen receptor alpha2beta1.
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Matrix Biology, Elsevier, 2007, 26 (4), pp.306-13. 〈10.1016/j.matbio.2007.01.001〉
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Contributeur : Institut Pasteur Tunis <>
Soumis le : mercredi 5 avril 2017 - 12:31:08
Dernière modification le : jeudi 20 septembre 2018 - 14:30:02

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Sameh Sarray, Estelle Delamarre, Jacques Marvaldi, Mohamed El Ayeb, Naziha Marrakchi, et al.. Lebectin and lebecetin, two C-type lectins from snake venom, inhibit alpha5beta1 and alphaV-containing integrins.. Matrix Biology, Elsevier, 2007, 26 (4), pp.306-13. 〈10.1016/j.matbio.2007.01.001〉. 〈pasteur-01375227〉

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