Lebectin and lebecetin, two C-type lectins from snake venom, inhibit alpha5beta1 and alphaV-containing integrins.
Integrins are essential protagonists in the complex multistep process of cancer progression and metastasis. We recently reported that lebectin, a novel C-type lectin from Macrovipera lebetina venom, displays an anti-integrin activity. In this study, we extend this observation to lebecetin, a second C-type lectin isolated from the same venom and previously reported as a potent inhibitor of platelet aggregation. Both venom lectins appear to exert their effect on cell adhesion, migration, invasion and proliferation by inhibiting alpha5beta1 and alphav-containing integrins. Moreover, the inhibition of alpha5beta1 and alphav integrins is likely due to the binding of venom peptides, as both lebectin and lebecetin co-immunoprecipitate with these integrins. Lebectin and lebecetin are thus the first examples of venom C-type lectins inhibiting an integrin other than the collagen receptor alpha2beta1.
Sarray
Sameh
S
Institut Pasteur de Tunis, Tunis, Tunisia.
Delamarre
Estelle
E
Marvaldi
Jacques
J
El Ayeb
Mohamed
M
Marrakchi
Naziha
N
Luis
José
J
D000818:Animals; D002448:Cell Adhesion; D045744:Cell Line, Tumor; D002462:Cell Membrane / Q000378:metabolism; D002465:Cell Movement; D015972:Gene Expression Regulation, Neoplastic / Q000187:drug effects; D006801:Humans; D047468:Immunoprecipitation; D039081:Integrin alpha5beta1 / Q000037:antagonists & inhibitors / Q000378:metabolism*; D039564:Integrin alphaV / Q000378:metabolism*; D037102:Lectins / Q000737:chemistry*; D037181:Lectins, C-Type / Q000378:metabolism*; D009361:Neoplasm Invasiveness; D012910:Snake Venoms / Q000378:metabolism*; D014757:Viper Venoms / Q000378:metabolism* / Q000633:toxicity
D039081:Integrin alpha5beta1; D039564:Integrin alphaV; D037102:Lectins; D037181:Lectins, C-Type; D012910:Snake Venoms; D014757:Viper Venoms; C478765:lebecetin protein, Macrovipera lebetina; C519594:lebectin protein, Macrovipera lebetina