Antitumoral Effect On C6 Glioma Cells And Phosphorylation Of Stress Activated Protein Kinases By Canavalia Brasiliensis Lectin (ConBr)
Heckert, B.T.1; Posser, T.1; Pereira, S.F.1; Santos, D.A. 1; Garcez, R.C.2; Alvarez-Silva, M.2; Nascimento, K.S.2; Teixeira, E.H.3; Cavada, B.S.3; Leal, R.B.1
1Depto. Bioquímica, 2Depto. Biologia Celular, CCB - UFSC, Florianópolis, SC, 88040-900; 3BioMol-Lab - UFC, Fortaleza, Ce.
Lectins constitute a structurally heterogeneous group of carbohydrate-binding proteins, comprising distinct families of evolutionarily related proteins. Lectins are ubiquitous in animals, plants and microorganisms where they mediate a wide variety of biological events, such as cell communication, host defense, fertilization, development, inflammation and tumor metastasis. The present study investigated the effects of ConBr lectin, obtained from Canavalia brasiliensis seeds, on C6 glioma cells viability and on modulation of mitogen-activated protein kinases (MAPKs). C6 glioma cells were incubated in the presence of 1-100ug/ml of ConBr lectin by 24-72 hours. The viability was measured by MTT reduction assay. The phosphorylation of MAPKs (ERK1/2, p38MAPK and JNK1/2) was analyzed by western blotting. The results showed a decrease in the viability of C6 glioma cells after 48 and 72 hours of treatment with lectin 100ug/ml. In parallel, there has been a decrease of ERK1 phosphorylation and a significant increase in the state of phosphorylation of the stress activated protein kinases (SAPKs), p38MAPK and JNK1/2. The present data provide a significant effect of ConBr lectin decreasing tumoral lineage viability. Additionally, it suggests a possible involvement of SAPKs pathways in this process.
Supported by: FAPESC, CAPES/PROCAD and CNPq
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