Characterization of dual effects induced by antimicrobial peptides: Regulated cell death or membrane disruption

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dc.contributor.author Paredes-Gamero, Edgar Julian [UNIFESP]
dc.contributor.author Martins, Marta Natividade Crizol [UNIFESP]
dc.contributor.author Cappabianco, Fabio Augusto Menocci [UNIFESP]
dc.contributor.author Ide, Jaime Shinsuke [UNIFESP]
dc.contributor.author Miranda, Antonio [UNIFESP]
dc.date.accessioned 2016-01-24T14:27:23Z
dc.date.available 2016-01-24T14:27:23Z
dc.date.issued 2012-07-01
dc.identifier http://dx.doi.org/10.1016/j.bbagen.2012.02.015
dc.identifier.citation Biochimica Et Biophysica Acta-general Subjects. Amsterdam: Elsevier B.V., v. 1820, n. 7, p. 1062-1072, 2012.
dc.identifier.issn 0304-4165
dc.identifier.uri http://repositorio.unifesp.br/handle/11600/35009
dc.description.abstract Background: Some reports describe lysis mechanisms by antimicrobial peptides (AMPs), while others describe the activation of regulated cell death. in this study, we compare the cell death-inducing activities of four beta-hairpin AMPs (gomesin, protegrin, tachyplesin and polyphemusin II) along with their linear analogs in the human erythroleukemia K562 cell line to investigate the relationship between their structure and activity.Methods: K562 cells were exposed to AMPs. Morphological and biochemistry alterations were evaluated using light microscopy, confocal microscopy and flow cytometry.Results: Gomesin and protegrin displayed cytotoxic properties that their linear counterparts did not. Tachyplesin and polyphemusin II and also their linear analogs induced cell death. We were able to distinguish two ways in which these AMPs induced cell death. Lower concentrations of AMPs induced controlled cell death mechanisms. Gomesin, tachyplesin and linear-tachyplesin promoted apoptosis that was characterized by annexin labeling, sensitivity to Z-VAD, and caspase-3 activation, but was also inhibited by necrostatin-1. Gomesin and protegrin induced cell death was dependent on intracellular Ca2+ mechanisms and the participation of free radicals was observed in protegrin induced cell death. Polyphemusin II and its linear analog mainly induced necrosis. Conversely, treatment with higher concentrations of AMPs primarily resulted in cell membrane disruption, but with clearly different patterns of action for each AMP tested.Conclusion: Different actions by beta-hairpin AMPs were observed at low concentrations and at higher concentrations despite the structure similarity.General significance: Controlled intracellular mechanism and direct membrane disruption were clearly distinguished helping to understand the real action of AMPs in mammalian cells. (C) 2012 Elsevier B.V. All rights reserved. en
dc.description.sponsorship Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorship Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.description.sponsorship Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
dc.format.extent 1062-1072
dc.language.iso eng
dc.publisher Elsevier B.V.
dc.relation.ispartof Biochimica Et Biophysica Acta-general Subjects
dc.rights Acesso aberto
dc.subject Antimicrobial peptide en
dc.subject Cell death en
dc.subject Membrane permeabilization en
dc.subject Intracellular mechanism en
dc.title Characterization of dual effects induced by antimicrobial peptides: Regulated cell death or membrane disruption en
dc.type Artigo
dc.rights.license http://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.contributor.institution Universidade Federal de São Paulo (UNIFESP)
dc.description.affiliation Universidade Federal de São Paulo, Dept Bioquim, BR-04044020 São Paulo, Brazil
dc.description.affiliation Universidade Federal de São Paulo, Dept Biofis, BR-04044020 São Paulo, Brazil
dc.description.affiliation Universidade Federal de São Paulo, Dept Ciencia & Tecnol, BR-12231280 Sao Jose Dos Campos, SP, Brazil
dc.description.affiliationUnifesp Universidade Federal de São Paulo, Dept Bioquim, BR-04044020 São Paulo, Brazil
dc.description.affiliationUnifesp Universidade Federal de São Paulo, Dept Biofis, BR-04044020 São Paulo, Brazil
dc.description.affiliationUnifesp Universidade Federal de São Paulo, Dept Ciencia & Tecnol, BR-12231280 Sao Jose Dos Campos, SP, Brazil
dc.description.sponsorshipID FAPESP: 2009/54869-2
dc.description.sponsorshipID FAPESP: 2011/17584-0
dc.identifier.file WOS000305366100033.pdf
dc.identifier.doi 10.1016/j.bbagen.2012.02.015
dc.description.source Web of Science
dc.identifier.wos WOS:000305366100033



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