Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/2028
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dc.contributor.CRUESPUNIVERSIDADE ESTADUAL DE CAMPINASpt_BR
dc.typeArtigo de periódicopt_BR
dc.titleNatural intracellular peptides can modulate the interactions of mouse brain proteins and thimet oligopeptidase with 14-3-3e and calmodulinpt_BR
dc.contributor.authorRusso, Lilian C.pt_BR
dc.contributor.authorAsega, Amanda F.pt_BR
dc.contributor.authorCastro, Leandro M.pt_BR
dc.contributor.authorNegraes, Priscilla D.pt_BR
dc.contributor.authorCruz, Lilianpt_BR
dc.contributor.authorGozzo, Fabio C.pt_BR
dc.contributor.authorUlrich, Henningpt_BR
dc.contributor.authorCamargo, Antonio C. M.pt_BR
dc.contributor.authorRioli, Vanessapt_BR
dc.contributor.authorFerro, Emer S.pt_BR
unicamp.authorGozzo, Fabio C.pt_BR
unicamp.author.externalRusso, Lilian C.pt
unicamp.author.externalAsega, Amanda F.pt
unicamp.author.externalCastro, Leandro M.pt
unicamp.author.externalNegraes, Priscilla D.pt
unicamp.author.externalCruz, Lilianpt
unicamp.author.externalUlrich, Henningpt
unicamp.author.externalCamargo, Antonio C. M.pt
unicamp.author.externalRioli, Vanessapt
unicamp.author.externalFerro, Emer S.pt
dc.subjectBiomedicinept_BR
dc.subjectCalciumpt_BR
dc.subjectInteractomept_BR
dc.subjectIntracellular peptidespt_BR
dc.subjectPeptide-protein interactionpt_BR
dc.subjectProtein targetpt_BR
dc.subject.wosANGIOTENSIN-CONVERTING ENZYMEpt_BR
dc.subject.wosINTERACTION NETWORKSpt_BR
dc.subject.wosENDOPEPTIDASE 24.15pt_BR
dc.subject.wosHUMAN-DISEASEpt_BR
dc.subject.wosKINASE-Cpt_BR
dc.subject.wosRECEPTORSpt_BR
dc.subject.wosBINDINGpt_BR
dc.subject.wosCELLSpt_BR
dc.subject.wosSPECIFICITYpt_BR
dc.subject.wosASSOCIATIONpt_BR
dc.description.abstractProtein interactions are crucial for most cellular process. Thus, rationally designed peptides that act as competitive assembly inhibitors of protein interactions by mimicking specific, determined structural elements have been extensively used in clinical and basic research. Recently, mammalian cells have been shown to contain a large number of intracellular peptides of unknown function. Here, we investigate the role of several of these natural intracellular peptides as putative modulators of protein interactions that are related to Ca2+-calmodulin (CaM) and 14-3-3 epsilon, which are proteins that are related to the spatial organization of signal transduction within cells. At concentrations of 1-50 mu M, most of the peptides that are investigated in this study modulate the interactions of CaM and 14-3-3 epsilon with proteins from the mouse brain cytoplasm or recombinant thimet oligopeptidase (EP24.15) in vitro, as measured by surface plasmon resonance. One of these peptides (VFDVELL; VFD-7) increases the cytosolic Ca2+ concentration in a dose-dependent manner but only if introduced into HEK293 cells, which suggests a wide biological function of this peptide. Therefore, it is exciting to suggest that natural intracellular peptides are novel modulators of protein interactions and have biological functions within cells.pt
dc.relation.ispartofProteomicspt_BR
dc.publisher.cityHobokenpt_BR
dc.publisherWiley-Blackwellpt_BR
dc.date.issued2012pt_BR
dc.identifier.citationProteomics. Wiley-Blackwell, v.12, n.17, p.2641-2655, 2012pt_BR
dc.language.isoengpt_BR
dc.description.volume12pt_BR
dc.description.issuenumber17pt_BR
dc.description.firstpage2641pt_BR
dc.description.lastpage2655pt_BR
dc.rightsfechadopt_BR
dc.sourceWOSpt_BR
dc.identifier.issn1615-9853pt_BR
dc.identifier.wosidWOS:000308098700006pt_BR
dc.identifier.doi10.1002/pmic.201200032pt_BR
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)pt_BR
dc.description.sponsorshipUniversidade de São Paulo (USP)pt_BR
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)pt_BR
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)pt_BR
dc.description.sponsorship1Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)pt_BR
dc.description.sponsorship1Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)pt_BR
dc.date.available2013-09-19T18:06:17Z
dc.date.available2016-07-01T12:55:29Z-
dc.date.accessioned2013-09-19T18:06:17Z
dc.date.accessioned2016-07-01T12:55:29Z-
dc.description.provenanceMade available in DSpace on 2013-09-19T18:06:17Z (GMT). No. of bitstreams: 0 Previous issue date: 2012en
dc.description.provenanceMade available in DSpace on 2016-07-01T12:55:29Z (GMT). No. of bitstreams: 0 Previous issue date: 2012en
dc.identifier.urihttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/2028
dc.identifier.urihttp://repositorio.unicamp.br/jspui/handle/REPOSIP/2028-
dc.contributor.departmentQuímica Orgânica
dc.contributor.unidadeIQpt
Appears in Collections:IQ - Artigos e Outros Documentos

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