Lebecetin, a C-lectin protein from the venom of Macrovipera lebetina that inhibits platelet aggregation and adhesion of cancerous cells

Haemostasis
S SarrayN Marrakchi

Abstract

A novel C-lectin protein, lebecetin, was purified and characterized from the venom of Macrovipera lebetina. It is a disulfide-linked heterodimer of 15 and 16 kD. The subunits are homologous to each other and to the other snake venom proteins of the C-type (Ca(2+)-dependent) lectin superfamily. Lebecetin shows a potent inhibitory effect on whole blood and washed platelets induced by different agonists. It inhibits the agglutination of human fixed platelets in the presence of ristocetin. Lebecetin also interferes with the adhesion of IGR39 melanoma and HT29D4 adenocarcinoma cells. These two lines adhere to lebecetin used as matrix. Lebecetin is also able to strongly reduce IGR39 and HT29D4 cell adhesion to fibrinogen and laminin, but not to fibronectin and collagen types I and IV, respectively. Adhesion properties of lebecetin may thus involve integrin receptors.

Citations

Apr 1, 2014·BioMed Research International·Leonardo A CalderonAndreimar M Soares
May 7, 2005·Toxicon : Official Journal of the International Society on Toxinology·Qiumin LuKenneth J Clemetson
Dec 25, 2012·Matrix Biology : Journal of the International Society for Matrix Biology·Maram MorjenNaziha Marrakchi
May 13, 2014·Toxicon : Official Journal of the International Society on Toxinology·Jed JebaliSameh Sarray
Mar 23, 2018·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·Marius Alexandru MogaLiana Pleş
Oct 27, 2018·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·Mohamad RimaZiad Fajloun

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