Distinct urinary glycoprotein signatures in prostate cancer patients

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dc.contributorSistema FMUSP-HC: Faculdade de Medicina da Universidade de São Paulo (FMUSP) e Hospital das Clínicas da FMUSP
dc.contributor.authorKAWAHARA, R.
dc.contributor.authorORTEGA, F.
dc.contributor.authorROSA-FERNANDES, L.
dc.contributor.authorGUIMARãES, V.
dc.contributor.authorQUINA, D.
dc.contributor.authorNAHAS, W.
dc.contributor.authorSCHWäMMLE, V.
dc.contributor.authorSROUGI, M.
dc.contributor.authorLEITE, K. R. M.
dc.contributor.authorTHAYSEN-ANDERSEN, M.
dc.contributor.authorLARSEN, M. R.
dc.contributor.authorPALMISANO, G.
dc.date.accessioned2019-03-13T17:07:02Z
dc.date.available2019-03-13T17:07:02Z
dc.date.issued2018
dc.description.abstractNovel biomarkers are needed to complement prostate specific antigen (PSA) in prostate cancer (PCa) diagnostic screening programs. Glycoproteins represent a hitherto largely untapped resource with a great potential as specific and sensitive tumor biomarkers due to their abundance in bodily fluids and their dynamic and cancer-associated glycosylation. However, quantitative glycoproteomics strategies to detect potential glycoprotein cancer markers from complex biospecimen are only just emerging. Here, we describe a glycoproteomics strategy for deep quantitative mapping of N- and O-glycoproteins in urine with a view to investigate the diagnostic value of the glycoproteome to discriminate PCa from benign prostatic hyperplasia (BPH), two conditions that remain difficult to clinically stratify. Total protein extracts were obtained, concentrated and digested from urine of six PCa patients (Gleason score 7) and six BPH patients. The resulting peptide mixtures were TMT-labeled and mixed prior to a multi-faceted sample processing including hydrophilic interaction liquid chromatography (HILIC) and titanium dioxide SPE based enrichment, endo-/exoglycosidase treatment and HILIC-HPLC pre-fractionation. The isolated N- and O-glycopeptides were detected and quantified using high resolution mass spectrometry. We accurately quantified 729 N-glycoproteins spanning 1,310 unique N-glycosylation sites and observed 954 and 965 unique intact N- and O-glycopeptides, respectively, across the two disease conditions. Importantly, a panel of 56 intact N-glycopeptides perfectly discriminated PCa and BPH (ROC: AUC = 1). This study has generated a panel of intact glycopeptides that has a potential for PCa detection. © Kawahara et al.eng
dc.description.indexPubMedeng
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo: 2015/02866-0
dc.description.sponsorshipGR11.172.1
dc.description.sponsorshipSyddansk Universitet, SDU
dc.identifier.citationONCOTARGET, v.9, n.69, p.33077-33097, 2018
dc.identifier.doi10.18632/oncotarget.26005
dc.identifier.issn1949-2553
dc.identifier.urihttps://observatorio.fm.usp.br/handle/OPI/31023
dc.language.isoeng
dc.publisherIMPACT JOURNALS LLCeng
dc.relation.ispartofOncotarget
dc.rightsrestrictedAccesseng
dc.rights.holderCopyright IMPACT JOURNALS LLCeng
dc.subjectGlycopeptideeng
dc.subjectGlycoproteomicseng
dc.subjectProstate cancereng
dc.subjectTMT-labelingeng
dc.subjectUrineeng
dc.subject.otherglycoproteineng
dc.subject.otherglycosidaseeng
dc.subject.othertumor markereng
dc.subject.otherarticleeng
dc.subject.otherdiagnostic valueeng
dc.subject.otherdifferential diagnosiseng
dc.subject.otherdisease markereng
dc.subject.othergleason scoreeng
dc.subject.otherglycoproteomicseng
dc.subject.otherhigh performance liquid chromatographyeng
dc.subject.otherhumaneng
dc.subject.otherhydrophilic interaction chromatographyeng
dc.subject.othermass spectrometryeng
dc.subject.otherprostate cancereng
dc.subject.otherprostate hypertrophyeng
dc.subject.otherproteomicseng
dc.subject.otherurineeng
dc.titleDistinct urinary glycoprotein signatures in prostate cancer patientseng
dc.typearticleeng
dc.type.categoryoriginal articleeng
dc.type.versionpublishedVersioneng
dspace.entity.typePublication
hcfmusp.affiliation.countryAustrália
hcfmusp.affiliation.countryDinamarca
hcfmusp.affiliation.countryisodk
hcfmusp.affiliation.countryisoau
hcfmusp.author.externalKAWAHARA, R.:Instituto de Ciências Biomédicas, Departamento de Parasitologia, Universidade de São Paulo, USP, São Paulo, Brazil
hcfmusp.author.externalROSA-FERNANDES, L.:Department of Biochemistry and Molecular Biology, University of Southern Denmark, Odense, Denmark
hcfmusp.author.externalQUINA, D.:Instituto de Ciências Biomédicas, Departamento de Parasitologia, Universidade de São Paulo, USP, São Paulo, Brazil
hcfmusp.author.externalSCHWäMMLE, V.:Department of Biochemistry and Molecular Biology, University of Southern Denmark, Odense, Denmark
hcfmusp.author.externalTHAYSEN-ANDERSEN, M.:Department of Molecular Sciences, Macquarie University, Sydney, NSW, Australia
hcfmusp.author.externalLARSEN, M. R.:Department of Biochemistry and Molecular Biology, University of Southern Denmark, Odense, Denmark
hcfmusp.author.externalPALMISANO, G.:Instituto de Ciências Biomédicas, Departamento de Parasitologia, Universidade de São Paulo, USP, São Paulo, Brazil
hcfmusp.citation.scopus32
hcfmusp.contributor.author-fmusphcFABIO LEME ORTEGA
hcfmusp.contributor.author-fmusphcVANESSA RIBEIRO GUIMARAES SCHREITER
hcfmusp.contributor.author-fmusphcWILLIAM CARLOS NAHAS
hcfmusp.contributor.author-fmusphcMIGUEL SROUGI
hcfmusp.contributor.author-fmusphcKATIA RAMOS MOREIRA LEITE
hcfmusp.description.beginpage33077
hcfmusp.description.endpage33097
hcfmusp.description.issue69
hcfmusp.description.volume9
hcfmusp.origemSCOPUS
hcfmusp.origem.pubmed30237853
hcfmusp.origem.scopus2-s2.0-85052921731
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