[Snake venom disintegrins: classification and therapeutic potential].
Biochemistry and pharmacology of snake venoms reveal structural and functional polymorphisms of proteins they contain. These lead their effects by their enzymatic activities (proteases, phospholipases A2, L-amino acid oxydases...) or by binding to membrane receptors. Disintegrin from snake venoms play a role as antagonists of cell adhesion and migration by binding integrins and blocking their function. Characterization of integrin antagonists from snake venom allows us understanding the function of some integrins providing new information to develop new therapeutic agents. In this review, we report classification and therapeutic implications of disintegrins. In particular the structural and the functional characteristics of lebestatin; a short disintegrin isolated from Tunisian Macrovipera lebetina snake venom.
Kallech-Ziri
O
O
Laboratoire des Venins et Toxines, Institut Pasteur de Tunis, 13 Place Pasteur, 1002 Tunis Belvédère, Tunisie.
Luis
J
J
El Ayeb
M
M
Marrakchi
N
N
D000818:Animals; D002448:Cell Adhesion; D019483:Disintegrins / Q000737:chemistry / Q000145:classification* / Q000494:pharmacology / Q000627:therapeutic use*; D016023:Integrins / Q000037:antagonists & inhibitors; D008956:Models, Chemical; D008958:Models, Molecular; D009362:Neoplasm Metastasis / Q000188:drug therapy; D009389:Neovascularization, Pathologic / Q000188:drug therapy; D010974:Platelet Aggregation / Q000187:drug effects; D010975:Platelet Aggregation Inhibitors / Q000737:chemistry / Q000145:classification* / Q000494:pharmacology / Q000627:therapeutic use*; D012910:Snake Venoms / Q000737:chemistry*; D014416:Tunisia
D019483:Disintegrins; D016023:Integrins; D010975:Platelet Aggregation Inhibitors; D012910:Snake Venoms