Journal
LABORATORY INVESTIGATION
Volume 85, Issue 12, Pages 1507-1516Publisher
SPRINGERNATURE
DOI: 10.1038/labinvest.3700350
Keywords
venom; disintegrin; KTS motif; CAM model; alpha 1 beta 1 collagen receptor
Categories
Ask authors/readers for more resources
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 alpha 1 beta 1 integrin. It was thus able to inhibit both adhesion and migration of PC12 and alpha 1 beta 1 integrin-expressing CHO cells (CHO-alpha 1) 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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available