Cell cycle arrest evidence, parasiticidal and bactericidal properties induced by L-amino acid oxidase from Bothrops atrox snake venom
Main Author: | |
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Publication Date: | 2011 |
Other Authors: | , , , , , , , , , , |
Format: | Article |
Language: | eng |
Source: | Repositório Institucional da UNESP |
Download full: | http://dx.doi.org/10.1016/j.biochi.2011.01.009 http://hdl.handle.net/11449/7510 |
Summary: | The present article describes an L-amino acid oxidase from Bothrops atrox snake venom as with antiprotozoal activities in Trypanosoma cruzi and in different species of Leishmania (Leishmania braziliensis, Leishmania donovani and Leishmania major). Leishmanicidal effects were inhibited by catalase, suggesting that they are mediated by H2O2 production. Leishmania spp. cause a spectrum of diseases, ranging from self-healing ulcers 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 mu g/mL and 50 mu 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. (C) 2011 Elsevier Masson SAS. All rights reserved. |
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Cell cycle arrest evidence, parasiticidal and bactericidal properties induced by L-amino acid oxidase from Bothrops atrox snake venomL-amino acid oxidaseCell cycleParasiticidal and bactericidal effectsThe present article describes an L-amino acid oxidase from Bothrops atrox snake venom as with antiprotozoal activities in Trypanosoma cruzi and in different species of Leishmania (Leishmania braziliensis, Leishmania donovani and Leishmania major). Leishmanicidal effects were inhibited by catalase, suggesting that they are mediated by H2O2 production. Leishmania spp. cause a spectrum of diseases, ranging from self-healing ulcers 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 mu g/mL and 50 mu 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. (C) 2011 Elsevier Masson SAS. All rights reserved.Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)Univ São Paulo, Fac Ciencias Farmaceut Ribeirao Preto, Dept Anal Clin Toxicol & Bromatol, BR-14040903 Ribeirao Preto, BrazilUniv Estadual Paulista, Dept Ciencias Biol, Fac Ciencias Farmaceut Araraquara, São Paulo, BrazilUniv Estadual Paulista, Dept Farmacos & Med, Fac Ciencias Farmaceut Araraquara, São Paulo, BrazilUniv São Paulo, Hematol Lab, Hosp Clin, Fac Med Ribeirao Preto, BR-14040903 Ribeirao Preto, BrazilUniv Franca, Grp Pesquisa Prod Nat, GPNUF Lab Pesquisa Microbiol Aplicada, LaPeMA, Franca, SP, BrazilUniv Estadual Paulista, Dept Ciencias Biol, Fac Ciencias Farmaceut Araraquara, São Paulo, BrazilUniv Estadual Paulista, Dept Farmacos & Med, Fac Ciencias Farmaceut Araraquara, São Paulo, BrazilElsevier France-editions Scientifiques Medicales ElsevierUniversidade de São Paulo (USP)Universidade Estadual Paulista (Unesp)Univ FrancaAlves Paiva, Raquel de MeloFigueiredo, Raquel de Freitas [UNESP]Antonucci, Gilmara AusechPaiva, Helder HenriquePires Bianchi, Maria de LourdesRodrigues, Kelly C.Lucarini, RodrigoCaetano, Renato CesarLinhari Rodrigues Pietro, Rosemeire Cristina [UNESP]Comes Martins, Carlos Henriquede Albuquerque, SergioSampaio, Suely Vilela2014-05-20T13:24:20Z2014-05-20T13:24:20Z2011-05-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article941-947application/pdfhttp://dx.doi.org/10.1016/j.biochi.2011.01.009Biochimie. Paris: Elsevier France-editions Scientifiques Medicales Elsevier, v. 93, n. 5, p. 941-947, 2011.0300-9084http://hdl.handle.net/11449/751010.1016/j.biochi.2011.01.009WOS:000290366500015WOS000290366500015.pdfWeb of Sciencereponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengBiochimie3.1881,554info:eu-repo/semantics/openAccess2025-03-29T05:25:44Zoai:repositorio.unesp.br:11449/7510Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestrepositoriounesp@unesp.bropendoar:29462025-03-29T05:25:44Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false |
dc.title.none.fl_str_mv |
Cell cycle arrest evidence, parasiticidal and bactericidal properties induced by L-amino acid oxidase from Bothrops atrox snake venom |
title |
Cell cycle arrest evidence, parasiticidal and bactericidal properties induced by L-amino acid oxidase from Bothrops atrox snake venom |
spellingShingle |
Cell cycle arrest evidence, parasiticidal and bactericidal properties induced by L-amino acid oxidase from Bothrops atrox snake venom Alves Paiva, Raquel de Melo L-amino acid oxidase Cell cycle Parasiticidal and bactericidal effects |
title_short |
Cell cycle arrest evidence, parasiticidal and bactericidal properties induced by L-amino acid oxidase from Bothrops atrox snake venom |
title_full |
Cell cycle arrest evidence, parasiticidal and bactericidal properties induced by L-amino acid oxidase from Bothrops atrox snake venom |
title_fullStr |
Cell cycle arrest evidence, parasiticidal and bactericidal properties induced by L-amino acid oxidase from Bothrops atrox snake venom |
title_full_unstemmed |
Cell cycle arrest evidence, parasiticidal and bactericidal properties induced by L-amino acid oxidase from Bothrops atrox snake venom |
title_sort |
Cell cycle arrest evidence, parasiticidal and bactericidal properties induced by L-amino acid oxidase from Bothrops atrox snake venom |
author |
Alves Paiva, Raquel de Melo |
author_facet |
Alves Paiva, Raquel de Melo Figueiredo, Raquel de Freitas [UNESP] Antonucci, Gilmara Ausech Paiva, Helder Henrique Pires Bianchi, Maria de Lourdes Rodrigues, Kelly C. Lucarini, Rodrigo Caetano, Renato Cesar Linhari Rodrigues Pietro, Rosemeire Cristina [UNESP] Comes Martins, Carlos Henrique de Albuquerque, Sergio Sampaio, Suely Vilela |
author_role |
author |
author2 |
Figueiredo, Raquel de Freitas [UNESP] Antonucci, Gilmara Ausech Paiva, Helder Henrique Pires Bianchi, Maria de Lourdes Rodrigues, Kelly C. Lucarini, Rodrigo Caetano, Renato Cesar Linhari Rodrigues Pietro, Rosemeire Cristina [UNESP] Comes Martins, Carlos Henrique de Albuquerque, Sergio Sampaio, Suely Vilela |
author2_role |
author author author author author author author author author author author |
dc.contributor.none.fl_str_mv |
Universidade de São Paulo (USP) Universidade Estadual Paulista (Unesp) Univ Franca |
dc.contributor.author.fl_str_mv |
Alves Paiva, Raquel de Melo Figueiredo, Raquel de Freitas [UNESP] Antonucci, Gilmara Ausech Paiva, Helder Henrique Pires Bianchi, Maria de Lourdes Rodrigues, Kelly C. Lucarini, Rodrigo Caetano, Renato Cesar Linhari Rodrigues Pietro, Rosemeire Cristina [UNESP] Comes Martins, Carlos Henrique de Albuquerque, Sergio Sampaio, Suely Vilela |
dc.subject.por.fl_str_mv |
L-amino acid oxidase Cell cycle Parasiticidal and bactericidal effects |
topic |
L-amino acid oxidase Cell cycle Parasiticidal and bactericidal effects |
description |
The present article describes an L-amino acid oxidase from Bothrops atrox snake venom as with antiprotozoal activities in Trypanosoma cruzi and in different species of Leishmania (Leishmania braziliensis, Leishmania donovani and Leishmania major). Leishmanicidal effects were inhibited by catalase, suggesting that they are mediated by H2O2 production. Leishmania spp. cause a spectrum of diseases, ranging from self-healing ulcers 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 mu g/mL and 50 mu 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. (C) 2011 Elsevier Masson SAS. All rights reserved. |
publishDate |
2011 |
dc.date.none.fl_str_mv |
2011-05-01 2014-05-20T13:24:20Z 2014-05-20T13:24:20Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://dx.doi.org/10.1016/j.biochi.2011.01.009 Biochimie. Paris: Elsevier France-editions Scientifiques Medicales Elsevier, v. 93, n. 5, p. 941-947, 2011. 0300-9084 http://hdl.handle.net/11449/7510 10.1016/j.biochi.2011.01.009 WOS:000290366500015 WOS000290366500015.pdf |
url |
http://dx.doi.org/10.1016/j.biochi.2011.01.009 http://hdl.handle.net/11449/7510 |
identifier_str_mv |
Biochimie. Paris: Elsevier France-editions Scientifiques Medicales Elsevier, v. 93, n. 5, p. 941-947, 2011. 0300-9084 10.1016/j.biochi.2011.01.009 WOS:000290366500015 WOS000290366500015.pdf |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Biochimie 3.188 1,554 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
941-947 application/pdf |
dc.publisher.none.fl_str_mv |
Elsevier France-editions Scientifiques Medicales Elsevier |
publisher.none.fl_str_mv |
Elsevier France-editions Scientifiques Medicales Elsevier |
dc.source.none.fl_str_mv |
Web of Science reponame:Repositório Institucional da UNESP instname:Universidade Estadual Paulista (UNESP) instacron:UNESP |
instname_str |
Universidade Estadual Paulista (UNESP) |
instacron_str |
UNESP |
institution |
UNESP |
reponame_str |
Repositório Institucional da UNESP |
collection |
Repositório Institucional da UNESP |
repository.name.fl_str_mv |
Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP) |
repository.mail.fl_str_mv |
repositoriounesp@unesp.br |
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1834482829315014656 |