Lebestatin, a disintegrin from Macrovipera venom, inhibits integrin-mediated cell adhesion, migration and angiogenesis.

Olfa Kallech-Ziri 1 Luis José 2 Salma Daoud 1 Amine Bazaa 1 Najet Srairi Abid 1 Nicolas Andreotti 3 Maxime Lehmann 2 Raoudha Zouari 1 Kamel Mabrouk 3 Jacques Marvaldi 2 Jean-Marc Sabatier 3 Mohamed El Ayeb 1 Naziha Marrakchi 1, 4, *
* Corresponding author
1 Laboratoire des Venins et Toxines, Institut Pasteur de Tunis
2 Faculté de Pharmacie
3 CNRS : UMR 6560
4 Faculté de médecine de Tunis
Abstract : Lebestatin, a new member of the lysine-threonine-serine (KTS)-disintegrin family, was purified to homogeneity from Tunisian snake (Macrovipera lebetina) venom. It is a single-chain polypeptide composed of 41 amino acids. The amino-acid sequence of lebestatin shows that it displays a pattern of cysteines similar to other short disintegrins, but contains the sequence KTS rather than RGD in its integrin-binding loop. Lebestatin presents a high homology with obtustatin and viperistatin. Lebestatin interacts specifically with the alpha1beta1 integrin. It was thus able to inhibit both adhesion and migration of PC12 and alpha1beta1 integrin-expressing CHO cells (CHO-alpha1) to type I and IV collagens. This disintegrin also affected adhesion and migration of endothelial cells and exhibited an anti-angiogenic effect in vivo when using the 8-day-old embryo chick chorioallantoic membrane model.
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Submitted on : Thursday, October 17, 2013 - 10:40:12 AM
Last modification on : Tuesday, February 26, 2019 - 12:18:02 PM

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Olfa Kallech-Ziri, Luis José, Salma Daoud, Amine Bazaa, Najet Srairi Abid, et al.. Lebestatin, a disintegrin from Macrovipera venom, inhibits integrin-mediated cell adhesion, migration and angiogenesis.. Laboratory Investigation, Nature Publishing Group, 2005, 85 (12), pp.1507-16. ⟨10.1038/labinvest.3700350⟩. ⟨pasteur-00874069⟩

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