Anti-angiogenic effect of phospholipases A 2 from Scorpio maurus venom glands on Human Umbilical Vein Endothelial Cells


  • Krayem Najeh
  • Abdelkefi-Koubaa Zaineb
  • Marrakchi Naziha
  • Luis José
  • Gargouri Youssef


  • Adhesion
  • Anti-angiogenic effect
  • Heterodimeric phospholipase A2
  • Invasion
  • Migration
  • Scorpion venom glands


In a previous study, we purified Sm-PLGV an heterodimeric phospholipase A2, from the venom glands of the Tunisian scorpion Scorpio maurus. This enzyme contains a Long chain, a penta-peptide insertion, which is cut out during the maturation process, followed by a short chain. A disulfide bridge links the two chains. Three recombinant forms of this enzyme were produced in Escherichia coli: rPLA2(+5) with a penta-peptide insert, rPLA2(-5) without the penta-peptide, and the Long chain alone without the short one. In the present study, we showed that Sm-PLGV, rPLA2(+5) and rPLA2(-5) displayed more potent anti-angiogenic activity in vitro than the recombinant Long chain and the short one obtained by chemical synthesis. These phospholipases A2 inhibited in a dose-dependent manner adhesion, migration and invasion of Human Umbilical Vein Endothelial Cells. Using Matrigel™, we demonstrated that Sm-PLGV, rPLA2(+5) and rPLA2(-5) significantly inhibited tubulogensesis. We also showed a clear dissociation between the anti-angiogenic effect of Sm-PLGV and its catalytic activity.

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