Protein disulfide isomerase plasma levels in healthy humans reveal proteomic signatures involved in contrasting endothelial phenotypes

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dc.contributorLab. Fisiopatologiapt_BR
dc.contributor.authorOliveira, Percíllia Victória Santos dept_BR
dc.contributor.authorGarcia-Rosa, Sheilapt_BR
dc.contributor.authorSachetto, Ana Teresa Azevedopt_BR
dc.contributor.authorMoretti, Ana Iochabel Soarespt_BR
dc.contributor.authorDebbas, Victorpt_BR
dc.contributor.authorDe Bessa, Tiphany Coraliept_BR
dc.contributor.authorSilva, Nathalia Tenguanpt_BR
dc.contributor.authorPereira, Alexandre da Costapt_BR
dc.contributor.authorMartins-de-Souza, Danielpt_BR
dc.contributor.authorSantoro, Marcelo Laramipt_BR
dc.contributor.authorLaurindo, Francisco Rafael Martinspt_BR
dc.date.accessioned2020-07-09T21:23:11Z-
dc.date.available2020-07-09T21:23:11Z-
dc.date.issued2019pt_BR
dc.identifier.citationOliveira PVS, Garcia-Rosa S, Sachetto ATA, Moretti AIS, Debbas V, De Bessa TC, et al. Protein disulfide isomerase plasma levels in healthy humans reveal proteomic signatures involved in contrasting endothelial phenotypes. Redox Biol. 2019 Apr;22:101142. doi:10.1016/j.redox.2019.101142.pt_BR
dc.identifier.urihttps://repositorio.butantan.gov.br/handle/butantan/2691-
dc.description.abstractRedox-related plasma proteins are candidate reporters of protein signatures associated with endothelial struc-ture/function. Thiol-proteins from protein disulfide isomerase (PDI) family are unexplored in this context. Here,we investigate the occurrence and physiological significance of a circulating pool of PDI in healthy humans. Wevalidated an assay for detecting PDI in plasma of healthy individuals. Our results indicate high inter-individual(median = 330 pg/mL) but low intra-individual variability over time and repeated measurements. Remarkably,plasma PDI levels could discriminate between distinct plasma proteome signatures, with PDI-rich (> median)plasma differentially expressing proteins related to cell differentiation, protein processing, housekeeping func-tions and others, while PDI-poor plasma differentially displayed proteins associated with coagulation, in-flammatory responses and immunoactivation. Platelet function was similar among individuals with PDI-rich vs.PDI-poor plasma. Remarkably, such protein signatures closely correlated with endothelial function and phe-notype, since cultured endothelial cells incubated with PDI-poor or PDI-rich plasma recapitulated gene ex-pression and secretome patterns in line with their corresponding plasma signatures. Furthermore, such sig-natures translated into functional responses, with PDI-poor plasma promoting impairment of endothelialadhesion to fibronectin and a disturbed pattern of wound-associated migration and recovery area. Patients withcardiovascular events had lower PDI levels vs. healthy individuals. This is the first study describing PDI levels asreporters of specific plasma proteome signatures directly promoting contrasting endothelial phenotypes andfunctional responses.pt_BR
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)pt_BR
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)pt_BR
dc.description.sponsorshipFundação Butantanpt_BR
dc.description.sponsorshipCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)pt_BR
dc.format.extent101142pt_BR
dc.language.isoEnglishpt_BR
dc.relation.ispartofRedox biologypt_BR
dc.rightsOpen Accesspt_BR
dc.titleProtein disulfide isomerase plasma levels in healthy humans reveal proteomic signatures involved in contrasting endothelial phenotypespt_BR
dc.typeArticlept_BR
dc.identifier.doi10.1016/j.redox.2019.101142pt_BR
dc.identifier.urlhttp://dx.doi.org/10.1016/j.redox.2019.101142pt_BR
dc.contributor.externalUniversidade de São Paulo (USP)¦¦Brasilpt_BR
dc.contributor.externalUniversidade Estadual de Campinas (UNICAMP)¦¦Brasilpt_BR
dc.contributor.externalInstituto Nacional de Biomarcadores em Neuropsiquiatria (INBioN)¦¦Brasilpt_BR
dc.identifier.citationvolume22pt_BR
dc.subject.keywordProtein disulfide isomerasept_BR
dc.subject.keywordPlasma proteomept_BR
dc.subject.keywordEndothelial cellspt_BR
dc.subject.keywordPlasma protein signaturespt_BR
dc.subject.keywordThiol proteinspt_BR
dc.relation.ispartofabbreviatedRedox Biolpt_BR
dc.identifier.citationabntv. 22, 101142, abr. 2019pt_BR
dc.identifier.citationvancouver2019 Apr;22:101142pt_BR
dc.contributor.butantanSachetto, Ana Teresa Azevedo|:Aluno|:Lab. Fisiopatologia|:pt_BR
dc.contributor.butantanSantoro, Marcelo Larami|:Pesquisador|:Lab. Fisiopatologia|:pt_BR
dc.sponsorship.butantanConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)¦¦305245/2015-5pt_BR
dc.sponsorship.butantanCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)¦¦154529pt_BR
dc.sponsorship.butantanFundação Butantan¦¦pt_BR
dc.sponsorship.butantanFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)¦¦2013/07937-8pt_BR
dc.sponsorship.butantanFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)¦¦2014/20595-1pt_BR
dc.sponsorship.butantanFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)¦¦2017/19866-9pt_BR
dc.sponsorship.butantanFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)¦¦2018/07511-4pt_BR
dc.sponsorship.butantanFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)¦¦2013/25177-0pt_BR
dc.sponsorship.butantanFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)¦¦2013/08711-3pt_BR
dc.sponsorship.butantanFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)¦¦2014/10068-4pt_BR
dc.sponsorship.butantanFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)¦¦2017/25588-1pt_BR
dc.identifier.bvsccBR78.1pt_BR
dc.identifier.bvsdbIBProdpt_BR
dc.description.dbindexedYespt_BR
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