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

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dc.contributor.authorParedes-Gamero, Edgar Julian [UNIFESP]
dc.contributor.authorMartins, Marta Natividade Crizol [UNIFESP]
dc.contributor.authorCappabianco, Fabio Augusto Menocci [UNIFESP]
dc.contributor.authorIde, Jaime Shinsuke [UNIFESP]
dc.contributor.authorMiranda, Antonio [UNIFESP]
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.date.accessioned2016-01-24T14:27:23Z
dc.date.available2016-01-24T14:27:23Z
dc.date.issued2012-07-01
dc.description.abstractBackground: 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.affiliationUniversidade Federal de São Paulo, Dept Bioquim, BR-04044020 São Paulo, Brazil
dc.description.affiliationUniversidade Federal de São Paulo, Dept Biofis, BR-04044020 São Paulo, Brazil
dc.description.affiliationUniversidade Federal de São Paulo, Dept Ciencia & Tecnol, BR-12231280 Sao Jose Dos Campos, SP, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Dept Bioquim, BR-04044020 São Paulo, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Dept Biofis, BR-04044020 São Paulo, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Dept Ciencia & Tecnol, BR-12231280 Sao Jose Dos Campos, SP, Brazil
dc.description.sourceWeb of Science
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.description.sponsorshipCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
dc.description.sponsorshipIDFAPESP: 2009/54869-2
dc.description.sponsorshipIDFAPESP: 2011/17584-0
dc.format.extent1062-1072
dc.identifierhttp://dx.doi.org/10.1016/j.bbagen.2012.02.015
dc.identifier.citationBiochimica Et Biophysica Acta-general Subjects. Amsterdam: Elsevier B.V., v. 1820, n. 7, p. 1062-1072, 2012.
dc.identifier.doi10.1016/j.bbagen.2012.02.015
dc.identifier.fileWOS000305366100033.pdf
dc.identifier.issn0304-4165
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/35009
dc.identifier.wosWOS:000305366100033
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofBiochimica Et Biophysica Acta-general Subjects
dc.rightsinfo:eu-repo/semantics/openAccess
dc.rights.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.subjectAntimicrobial peptideen
dc.subjectCell deathen
dc.subjectMembrane permeabilizationen
dc.subjectIntracellular mechanismen
dc.titleCharacterization of dual effects induced by antimicrobial peptides: Regulated cell death or membrane disruptionen
dc.typeinfo:eu-repo/semantics/article
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