Antitumoral Potential of Tunisian Snake Venoms Secreted Phospholipases A2. (31st January 2013)

• Record Type: Journal Article
• Authors: Zouari-Kessentini, Raoudha; Srairi-Abid, Najet; Bazaa, Amine; El Ayeb, Mohamed; Luis, Jose; Marrakchi, Naziha
• Other Names: Ponce Soto Luis A. Academic Editor.
• Is Part Of: BioMed research international. Volume 2013(2013)
• Publication Date: 2013-01-31
• Subjects: Medicine -- Periodicals; Biology -- Periodicals; Biotechnology -- Periodicals; Life sciences -- Periodicals; 610.5
• DOI: 10.1155/2013/391389
• Languages: English
• ISSNs: 2314-6133

Abstract

Abstract : Phospholipases type A2 (PLA2 s) are the most abundant proteins found in Viperidae snake venom. They are quite fascinating from both a biological and structural point of view. Despite similarity in their structures and common catalytic properties, they exhibit a wide spectrum of pharmacological activities. Besides being hydrolases, secreted phospholipases A2 (sPLA2 ) are an important group of toxins, whose action at the molecular level is still a matter of debate. These proteins can display toxic effects by different mechanisms. In addition to neurotoxicity, myotoxicity, hemolytic activity, antibacterial, anticoagulant, and antiplatelet effects, some venom PLA2 s show antitumor and antiangiogenic activities by mechanisms independent of their enzymatic activity. This paper aims to discuss original finding against anti-tumor and anti-angiogenic activities of sPLA2 isolated from Tunisian vipers: Cerastes cerastes and Macrovipera lebetina, representing new tools to target specific integrins, mainly, α 5 β 1 and α v integrins.