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dc.contributor.authorBriggs, MT
dc.contributor.authorCondina, MR
dc.contributor.authorHo, YY
dc.contributor.authorEverest-Dass, AV
dc.contributor.authorMittal, P
dc.contributor.authorKaur, G
dc.contributor.authorOehler, MK
dc.contributor.authorPacker, NH
dc.contributor.authorHoffmann, P
dc.date.accessioned2019-09-09T02:56:36Z
dc.date.available2019-09-09T02:56:36Z
dc.date.issued2019
dc.identifier.issn1615-9853
dc.identifier.doi10.1002/pmic.201800482
dc.identifier.urihttp://hdl.handle.net/10072/387058
dc.description.abstractEpithelial ovarian cancer is one of the most fatal gynecological malignancies in adult women. As studies on protein N‐glycosylation have extensively reported aberrant patterns in the ovarian cancer tumor microenvironment, obtaining spatial information will uncover tumor‐specific N‐glycan alterations in ovarian cancer development and progression. matrix‐assisted laser desorption/ionization (MALDI) mass spectrometry imaging (MSI) is employed to investigate N‐glycan distribution on formalin‐fixed paraffin‐embedded ovarian cancer tissue sections from early‐ and late‐stage patients. Tumor‐specific N‐glycans are identified and structurally characterized by porous graphitized carbon‐liquid chromatography‐electrospray ionization‐tandem mass spectrometry (PGC‐LC‐ESI‐MS/MS), and then assigned to high‐resolution images obtained from MALDI‐MSI. Spatial distribution of 14 N‐glycans is obtained by MALDI‐MSI and 42 N‐glycans (including structural and compositional isomers) identified and structurally characterized by LC‐MS. The spatial distribution of oligomannose, complex neutral, bisecting, and sialylated N‐glycan families are localized to the tumor regions of late‐stage ovarian cancer patients relative to early‐stage patients. Potential N‐glycan diagnostic markers that emerge include the oligomannose structure, (Hex)6 + (Man)3(GlcNAc)2, and the complex neutral structure, (Hex)2 (HexNAc)2 (Deoxyhexose)1 + (Man)3(GlcNAc)2. The distribution of these markers is evaluated using a tissue microarray of early‐ and late‐stage patients.
dc.description.peerreviewedYes
dc.languageEnglish
dc.language.isoeng
dc.publisherWiley
dc.relation.ispartofpagefrome1800482
dc.relation.ispartofjournalProteomics
dc.subject.fieldofresearchBiological Sciences
dc.subject.fieldofresearchInformation and Computing Sciences
dc.subject.fieldofresearchMedical and Health Sciences
dc.subject.fieldofresearchcode06
dc.subject.fieldofresearchcode08
dc.subject.fieldofresearchcode11
dc.subject.keywordsN-glycan
dc.subject.keywordsformalin-fixed paraffin-embedded
dc.subject.keywordsmass spectrometry imaging
dc.subject.keywordsmatrix-assisted laser desorption/ionization
dc.subject.keywordsovarian cancer
dc.titleMALDI Mass Spectrometry Imaging of Early- and Late-Stage Serous Ovarian Cancer Tissue Reveals Stage-Specific N-Glycans
dc.typeJournal article
dc.type.descriptionC1 - Articles
dcterms.bibliographicCitationBriggs, MT; Condina, MR; Ho, YY; Everest-Dass, AV; Mittal, P; Kaur, G; Oehler, MK; Packer, NH; Hoffmann, P, MALDI Mass Spectrometry Imaging of Early- and Late-Stage Serous Ovarian Cancer Tissue Reveals Stage-Specific N-Glycans, Proteomics, 2019, pp. e1800482-
dcterms.licensehttp://creativecommons.org/licenses/by/4.0/
dc.date.updated2019-09-09T02:52:23Z
dc.description.versionVersion of Record (VoR)
gro.description.notepublicThis publication has been entered into Griffith Research Online as an Advanced Online Version.
gro.rights.copyright© 2019 The Authors. Proteomics Published by WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
gro.hasfulltextFull Text
gro.griffith.authorEverest-Dass, Arun
gro.griffith.authorPacker, Nicki


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