| Literature DB >> 16200076 |
Kallech-Ziri Olfa1, Luis José, Daoud Salma, Bazaa Amine, Srairi Abid Najet, Andreotti Nicolas, Lehmann Maxime, Zouari Raoudha, Mabrouk Kamel, Marvaldi Jacques, Sabatier Jean-Marc, El Ayeb Mohamed, Marrakchi Naziha.
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.Entities:
Mesh：
Substances：
Year: 2005 PMID： 16200076 DOI： 10.1038/labinvest.3700350
Source DB: PubMed Journal: Lab Invest ISSN： 0023-6837 Impact factor: 5.662