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dc.contributor.authorLaurino, CCFC
dc.contributor.authorFritzler, M. J.
dc.contributor.authorMortara, Renato Arruda [UNIFESP]
dc.contributor.authorSilva, N. P.
dc.contributor.authorAlmeida, I. C.
dc.contributor.authorAndrade, LEC
dc.date.accessioned2016-01-24T12:40:59Z
dc.date.available2016-01-24T12:40:59Z
dc.date.issued2006-03-01
dc.identifierhttp://dx.doi.org/10.1111/j.1365-2249.2006.03024.x
dc.identifier.citationClinical and Experimental Immunology. Oxford: Blackwell Publishing, v. 143, n. 3, p. 572-584, 2006.
dc.identifier.issn0009-9104
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/28755
dc.description.abstractThe aim of this study was to characterize a novel human autoantibody-autoantigen system represented as cytoplasmic discrete speckles (CDS) in indirect immunofluorescence (IIF). A distinct CDS IIF pattern represented by 3-20 discrete speckles dispersed throughout the cytoplasm was identified among other cytoplasmic speckled IIF patterns. the cytoplasmic domains labelled by human anti-CDS-1 antibodies did not co-localize with endosome/lysosome markers EEA1 and LAMP-2, but showed partial co-localization with glycine-tryptophan bodies (GWB). CDS-1 sera did not react with several cellular extracts in immunoblotting and did not immunoprecipitate recombinant GW182 or EEA1 proteins. the typical CDS-1 IIF labelling pattern was abolished after delipidation of HEp-2 cells. Moreover, CDS-1 sera reacted strongly with a lipid component co-migrating with phosphatidylethanolamine (PE) in high performance thin-layer chromatography (HPTLC)-immunostaining of HEp-2 cell total lipid extracts. the CDS-1 major molecular targets were established by electrospray ionization-mass spectrometry (ESI-MS), HPTLC-immunostaining and chemiluminescent enzyme-linked immunosorbent assay as diacyl-PE species, containing preferentially a cis-C18 : 1 fatty acid chain at C-2 of the glycerol moiety, namely 1,2-cis-C18 : 1-PE and 1-C16 : 0-2-cis-C18 : 1-PE. the clinical association of CDS-1 sera included a variety of systemic and organ-specific autoimmune diseases but they were also observed in patients with no evidence of autoimmune disease.en
dc.format.extent572-584
dc.language.isoeng
dc.publisherBlackwell Publishing
dc.relation.ispartofClinical and Experimental Immunology
dc.rightsAcesso aberto
dc.subjectautoantibodiesen
dc.subjectautoantigenen
dc.subjectepitope analysisen
dc.subjectcytoplasmic domainsen
dc.subjectphospholipidsen
dc.subjectGW bodiesen
dc.titleHuman autoantibodies to diacyl-phosphatidylethanolamine recognize a specific set of discrete cytoplasmic domainsen
dc.typeArtigo
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.contributor.institutionUniv Calgary
dc.contributor.institutionUniv Texas
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.description.affiliationUniversidade Federal de São Paulo, Div Rheumatol, Escola Paulista Med, BR-04023062 São Paulo, Brazil
dc.description.affiliationUniv Calgary, Dept Biochem & Mol Biol, Calgary, AB, Canada
dc.description.affiliationUNIFESP, EPM, Dept Microbiol Imunol & Parasitol, São Paulo, Brazil
dc.description.affiliationUniv Texas, Dept Biol Sci, El Paso, TX 79968 USA
dc.description.affiliationUniv São Paulo, ICB, Dept Parasitol, São Paulo, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Div Rheumatol, Escola Paulista Med, BR-04023062 São Paulo, Brazil
dc.description.affiliationUnifespUNIFESP, EPM, Dept Microbiol Imunol & Parasitol, São Paulo, Brazil
dc.identifier.doi10.1111/j.1365-2249.2006.03024.x
dc.description.sourceWeb of Science
dc.identifier.wosWOS:000235370200022


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