Cell cycle arrest evidence, parasiticidal and bactericidal properties induced by XXXX oxidase from Bothrops atrox snake venom.

@entity274 @entity1527 @entity1066 @entity3667 @entity14890 @entity3911
The present article describes an @entity14890 oxidase from Bothrops atrox snake venom as with antiprotozoal activities in @entity1527 and in different species of @entity3667 ( @entity3667 braziliensis, @entity3911 and @entity3667 ). Leishmanicidal effects were inhibited by catalase, suggesting that they are mediated by @entity274 production. @entity3667 spp. cause a spectrum of diseases, ranging from self-healing @entity1066 to disseminated and often fatal infections, depending on the species involved and the host's immune response. BatroxLAAO also displays bactericidal activity against both Gram-positive and Gram-negative bacteria. The apoptosis induced by BatroxLAAO on HL-60 cell lines and PBMC cells was determined by morphological cell evaluation using a mix of fluorescent dyes. As revealed by flow cytometry analysis, suppression of cell proliferation with BatroxLAAO was accompanied by the significant accumulation of cells in the G0/G1 phase boundary in HL-60 cells. BatroxLAAO at 25   g/mL and 50   g/mL blocked G0-G1 transition, resulting in G0/G1 phase cell cycle arrest, thereby delaying the progression of cells through S and G2/M phase in HL-60 cells. This was shown by an accentuated decrease in the proportion of cells in S phase, and the almost absence of G2/M phase cell population. BatroxLAAO is an interesting enzyme that provides a better understanding of the ophidian envenomation mechanism, and has biotechnological potential as a model for therapeutic agents.
