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

@article{Bazaa2009MVLPLA2AP,
  title={MVL-PLA2, a phospholipase A2 from Macrovipera lebetina transmediterranea venom, inhibits tumor cells adhesion and migration.},
  author={Amine Bazaa and Jose Luis and Najet Srairi-Abid and Olfa Kallech-Ziri and Raoudha Kessentini-Zouari and C{\'e}line D{\'e}filles and J. C. Lissitzky and Mohamed El Ayeb and Naziha Marrakchi},
  journal={Matrix biology : journal of the International Society for Matrix Biology},
  year={2009},
  volume={28 4},
  pages={188-93}
}
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… CONTINUE READING