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MVL-PLA2, a phospholipase A2 from Macrovipera lebetina transmediterranea venom, inhibits tumor cells adhesion and migration.

Abstract : Here, we report the purification and characterization of an acidic Asp49 phospholipase A2, named MVL-PLA2, with a molecular mass of 13,626.64 Da. The complete MVL-PLA2 cDNA was cloned from Macrovipera lebetina transmediterranea venom gland cDNA library. MVL-PLA2 possesses 122 amino acid residues, including 14 cysteines, and belongs to group II snake venom phospholipase A2 enzymes. MVL-PLA2 was not cytotoxic up to 2 muM and completely abolished cell adhesion and migration of various human tumor cells. Chemical modification with p-bromophenacyl bromide abolished the enzymatic activity of MVL-PLA2 without affecting its anti-tumor effect, suggesting the presence of 'pharmacological sites' distinct from the catalytic site in snake venom phospholipase A2. We demonstrated for the first time that the anti-tumor effect of MVL-PLA2 was mediated by alpha5beta1 and alphav-containing integrins. This finding may serve as starting point for structure-function relationship studies leading to design a new generation of specific anti-cancer drugs.
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https://hal-riip.archives-ouvertes.fr/pasteur-00612541
Contributor : Institut Pasteur Tunis <>
Submitted on : Friday, July 29, 2011 - 11:33:03 AM
Last modification on : Saturday, October 24, 2020 - 3:10:40 AM

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Amine Bazaa, José Luis, Najet Srairi-Abid, Olfa Kallech-Ziri, Raoudha Kessentini-Zouari, et al.. MVL-PLA2, a phospholipase A2 from Macrovipera lebetina transmediterranea venom, inhibits tumor cells adhesion and migration.. Matrix Biology, Elsevier, 2009, 28 (4), pp.188-93. ⟨10.1016/j.matbio.2009.03.007⟩. ⟨pasteur-00612541⟩

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