54I-6 |
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M. D. C. VALADEZ VEGA1, A. García Carrancá, M. Cuellar Cruz, G. Alvarez-Manilla Dubón, and E. Contreras L5. (1) Dept. of Biochemistry, Universidad Autónoma del Estado de Hidalgo, Carr. Pachuca-Tulancingo Km. 4.6, Pachuca, 42076, Mexico, (2) Centro de Investigaciones Quimicas, Universidad Autonoma del Estado de Hidalgo, Carr. Pachuca-Tulancingo Km 4.6, Pachuca, Hidalgo. Mexico, 42076 Lectins are naturally occurring constituents that are mainly found in legume seeds and other parts of plants. Lectins are nonenzymatic protein of nonimmune origin that bind carbohydrates reversibly; they possess the activity to agglutinate cells and precipitate glycoconjugates. The lectins can destroy the epithelial cells of the gastrointestinal tract; interfere with cell mitosis; and damage kidney, liver, and heart cells and agglutinate red blood cells. The present work has been designed to establish the bioactive properties of tepary bean lectins. The hemagglutination activity was determined by twofold serial dilution as described by Jaffe. For hemagglutination inhibition assays, a lectin solution was added to haptens, diluted serially, and incubated with erythrocytes. For glycopeptides affinity, the lectins were immobilized and glycopeptides were applied to the column. Mitogenic activity was assayed employing human peripheral blood; the cells were incubated with different concentrations of lectins, and then added with ƒË3HƒÍthymidine and determined CPM. In vitro cytotoxicity was carried out employing 13 human malignant cells lines, the cells were incubated with several lectin concentrations, and the viability was measured by MTT. The result indicated that tepary lectin has high hemagglutination activity. The hapten assay showed that the glycoproteins inhibit the hemagglutination. Mitogenicity assay indicated that tepary lectin had less potential to stimulate cell division than the other lectins assayed. Affinity chromatography using lectin immobilized indicated that some glycopeptides applied were retarded, and the collected fraction showed a larger proportion of N-acetylglucosamine, mannose, and galactose residues in their structures. Viability assay showed that MCF-7 and T-24 cells lines were more sensitive to cytotoxic effect, while MDA, Hep-G2, and C33-A were more resistant to lectin effect. These results suggest that the lectins found in some legumes can be a useful tool for anticancer research and for glycobiology studies as well
Session 54I, Toxicology & Safety Evaluation: General
2005 IFT Annual Meeting, July 15-20 - New Orleans, Louisiana |