Effect of L-amino acid oxidase from Calloselasma rhodosthoma snake venom on human neutrophils
| Autor: | Anderson M. Kayano, Andreimar M. Soares, Neriane Monteiro Nery, Caroline V. Xavier, Rodrigo G. Stábeli, Adriana Silva Pontes, Weverson Luciano Pires, Onassis Boeri de Castro, Fabianne Lacouth-Silva, Juliana P. Zuliani, Sulamita da Silva Setúbal, Silvana D. da Silva, Leonardo A. Calderon |
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| Rok vydání: | 2013 |
| Předmět: |
Adult
Adolescent Cell Survival Neutrophils Viper Venoms Biology Toxicology L-amino-acid oxidase L-Amino Acid Oxidase Proinflammatory cytokine chemistry.chemical_compound Young Adult Viperidae Animals Humans chemistry.chemical_classification Reactive oxygen species Oxidase test Superoxide Tumor Necrosis Factor-alpha Interleukin-8 Hydrogen Peroxide In vitro chemistry Biochemistry Snake venom Liberation Reactive Oxygen Species |
| Zdroj: | Toxicon : official journal of the International Society on Toxinology. 80 |
| ISSN: | 1879-3150 |
| Popis: | The in vitro effects of LAAO, an L-amino acid oxidase isolated from Calloselasma rhodosthoma snake venom, on isolated human neutrophil function were investigated. LAAO showed no toxicity on neutrophils. At non-cytotoxic concentrations, LAAO induced the superoxide anion production by isolated human neutrophil. This toxin, in its native form, is also able to stimulate the production of hydrogen peroxide in neutrophils, suggesting that its primary structure is essential for stimulation the cell. Moreover, the incubation of LAAO and phenol red medium did not induce the production of hydrogen peroxide. Furthermore, LAAO was able to stimulate neutrophils to release proinflammatory mediators such as IL-8 and TNF-a as well as NETs liberation. Together, the data showed that the LAAO triggers relevant proinflammatory events. Particular regions of the molecule distinct from the LAAO catalytic site may be involved in the onset of inflammatory events. |
| Databáze: | OpenAIRE |
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