Cell cycle arrest evidence, parasiticidal and bactericidal properties induced by L-amino acid oxidase from Bothrops atrox snake venom

Bibliographic Details
Main Author: Alves Paiva, Raquel de Melo
Publication Date: 2011
Other Authors: 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
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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spelling 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
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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)
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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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