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Phospholipases type A 2  (PLA 2 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 A 2  (sPLA 2 ) 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 PLA 2 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 sPLA 2  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.

Antitumoral Potential of Tunisian Snake Venoms Secreted Phospholipases A2

Antitumoral Potential of Tunisian Snake Venoms Secreted Phospholipases A₂