Lebecin, a new C-type lectin like protein from Macrovipera lebetina venom with anti-tumor activity against the breast cancer cell line MDA-MB231.

authors

  • Jebali Jed
  • Fakhfekh Emna
  • Morgen Maram
  • Srairi-Abid Najet
  • Majdoub Hafedh
  • Gargouri Ali
  • El Ayeb Mohamed
  • Luis José
  • Marrakchi Naziha
  • Sarray Sameh

keywords

  • Cell adhesion
  • Snake venom
  • Cell migration
  • Molecular cloning
  • Molecular modeling

document type

ART

abstract

C-type lectins like proteins display various biological activities and are known to affect especially platelet aggregation. Few of them have been reported to have anti-tumor effects. In this study, we have identified and characterized a new C-type lectin like protein, named lebecin. Lebecin is a heterodimeric protein of 30 kDa. The N-terminal amino acid sequences of both subunits were determined by Edman degradation and the entire amino acid sequences were deduced from cDNAs. The precursors of both lebecin subunits contain a 23-amino acid residue signal peptide and the mature α and β subunits are composed of 129 and 131 amino acids, respectively. Lebecin is shown to be a potent inhibitor of MDA-MB231 human breast cancer cells proliferation. Furthermore, lebecin dose-dependently inhibited the integrin-mediated attachment of these cells to different adhesion substrata. This novel C-type lectin also completely blocked MDA-MB231 cells migration towards fibronectin and fibrinogen in haptotaxis assays.

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