Mechanism of the cytotoxic effect of l-amino acid oxidase isolated from Bothrops alternatus snake venom
Ribeiro, P.íc.H.; Zuliani, J.P.; Fernandes, C.F.C.; Calderon, L.A.; Stábeli, R.G.; Nomizo, A.; Soares, A.M.
International Journal of Biological Macromolecules 92: 329-337
2016
ISSN/ISBN: 1879-0003
PMID: 27394649
DOI: 10.1016/j.ijbiomac.2016.07.022
Accession: 058282813
BaltLAAO-I, an L-amino acid oxidase isolated from Bothrops alternatus, is a glycoprotein enzyme with a pI-5.3, 15% sugar and a related molecular mass of 66,000Da in its monomeric form, and 123,000Da in its dimeric form. The objective of this study is to describe the cytotoxicity activity induced by BaltLAAO-I isolated from Bothrops alternatus venom and its possible mechanism of action on tumor cells. Our results clearly depict that BaltLAAO-I has a strong selective cytotoxic activity on tumor cell lines (JURKAT, SK-BR-3 and B16F10). On the other hand, the results show low cytotoxicity on human peripheral blood mononuclear cells. Furthermore, our findings demonstrate that BaltLAAO-I induces the apoptosis of tumor cell lines through a cytotoxic activity exerted by a generation of reactive oxygen intermediates. All in all, the data indicate that LAAOs exert a selective cytotoxic role on tumor cells, demonstrating a great potential for future use in clinical therapy.