Plant lectins are non-enzymic and non-immune origin proteins that specifically recognize and bind to various sugar structures and possess the activity to agglutinate cells and/or precipitate polysaccharides and glycoconjugates. The emerging evidences showed that plant lectins contribute not only to tumour cell recognition but also to cell adhesion and localization, to signal transduction, to mitogenic cytotoxicity and apoptosis. The aim of experiment. Evaluation of antimutagenicity and cytotoxicity of a lectin-enriched protein fraction from Nettle herb. Material and methods. Lectin-enriched protein fraction was obtained from the herb of Urtica dioica L. The antimutagenicity was studied in a bacterial reverse mutation assay (Ames test), both in the absence and presence of an exogenous metabolic activator S9 (the liver postmitochondrial supernatant of rats treated with the mixture phenobarbital/ β-naphthoflavone to induce the hepatic microsomal enzymes). A set of three strains, S. typhimurium TA98 (hisD3052galbiochl1008rfa1001 ΔuvrBpKM101), S. typhimurium TA100 (hisG56galbiochl1005rfa1004ΔuvrB pKM101) and E. coli WP2uvrA (trpE65ΔuvrA), was used. Cytotoxicity was determined by the tetrazolium dye (MTT) colorimetric assay in HepG2 human hepatoblastoma cell line. Results. Lectin-enriched protein fraction did not display any significant reduction in the cell viability of HepG2 cells, neither after 24 h nor after 48 h of treatment. Lectin-enriched protein fraction showed antimutagenic effect against 2AA (2-aminoanthracene), which reached, at the highest concentration tested, the maximal inhibition of 56%, 78% and 61% in TA98, TA100 and WP2uvrA strains, respectively. In contrast, lectin-enriched fraction produced no significant antimutagenic effects (maximal inhibition < 25%) against 2NF (2-nitrofluorene), SA (sodium azide), MMS (methyl methanesulfonate). Conclusions. Lectin-enriched protein fraction did not inhibited the cell proliferation in tumour hepatic HepG2
Antimutagenic activity of proteins (lectins) fraction from herb of Nettle / Vitalone, Annabella; Mazzanti, Gabriela; R., Staršelskytė; N., Savickienė; DI SOTTO, Antonella; J., Bernatoniene; G., Draksiene; A., Savickas. - In: ROSSIJSKIJ BIOTERAPEVTICESKIJ ZURNAL. - ISSN 1726-9784. - STAMPA. - 2:(2013), pp. 96-96. (Intervento presentato al convegno Belarusian-Russian scientific and practical conference with international participation "National anticancer drugs". tenutosi a Minsk nel 23-25 May 2013).
Antimutagenic activity of proteins (lectins) fraction from herb of Nettle.
VITALONE, Annabella;MAZZANTI, Gabriela;DI SOTTO, ANTONELLA;
2013
Abstract
Plant lectins are non-enzymic and non-immune origin proteins that specifically recognize and bind to various sugar structures and possess the activity to agglutinate cells and/or precipitate polysaccharides and glycoconjugates. The emerging evidences showed that plant lectins contribute not only to tumour cell recognition but also to cell adhesion and localization, to signal transduction, to mitogenic cytotoxicity and apoptosis. The aim of experiment. Evaluation of antimutagenicity and cytotoxicity of a lectin-enriched protein fraction from Nettle herb. Material and methods. Lectin-enriched protein fraction was obtained from the herb of Urtica dioica L. The antimutagenicity was studied in a bacterial reverse mutation assay (Ames test), both in the absence and presence of an exogenous metabolic activator S9 (the liver postmitochondrial supernatant of rats treated with the mixture phenobarbital/ β-naphthoflavone to induce the hepatic microsomal enzymes). A set of three strains, S. typhimurium TA98 (hisD3052galbiochl1008rfa1001 ΔuvrBpKM101), S. typhimurium TA100 (hisG56galbiochl1005rfa1004ΔuvrB pKM101) and E. coli WP2uvrA (trpE65ΔuvrA), was used. Cytotoxicity was determined by the tetrazolium dye (MTT) colorimetric assay in HepG2 human hepatoblastoma cell line. Results. Lectin-enriched protein fraction did not display any significant reduction in the cell viability of HepG2 cells, neither after 24 h nor after 48 h of treatment. Lectin-enriched protein fraction showed antimutagenic effect against 2AA (2-aminoanthracene), which reached, at the highest concentration tested, the maximal inhibition of 56%, 78% and 61% in TA98, TA100 and WP2uvrA strains, respectively. In contrast, lectin-enriched fraction produced no significant antimutagenic effects (maximal inhibition < 25%) against 2NF (2-nitrofluorene), SA (sodium azide), MMS (methyl methanesulfonate). Conclusions. Lectin-enriched protein fraction did not inhibited the cell proliferation in tumour hepatic HepG2I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
