| Literature DB >> 24814013 |
Jed Jebali1, Emna Fakhfekh2, Maram Morgen2, Najet Srairi-Abid2, Hafedh Majdoub3, Ali Gargouri4, Mohamed El Ayeb2, José Luis5, Naziha Marrakchi2, Sameh Sarray6.
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.Entities:
Keywords: Cell adhesion; Cell migration; Molecular cloning; Molecular modeling; Snake venom
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Year: 2014 PMID: 24814013 DOI: 10.1016/j.toxicon.2014.04.010
Source DB: PubMed Journal: Toxicon ISSN: 0041-0101 Impact factor: 3.033