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dc.contributor.authorChatterjee, Sayantani
dc.contributor.authorLee, Ling Y
dc.contributor.authorKawahara, Rebeca
dc.contributor.authorAbrahams, Jodie L
dc.contributor.authorAdamczyk, Barbara
dc.contributor.authorAnugraham, Merrina
dc.contributor.authorAshwood, Christopher
dc.contributor.authorSumer-Bayraktar, Zeynep
dc.contributor.authorBriggs, Matthew T
dc.contributor.authorChik, Jenny HL
dc.contributor.authorEverest-Dass, Arun
dc.contributor.authorFoerster, Sarah
dc.contributor.authorHinneburg, Hannes
dc.contributor.authorLeite, Katia RM
dc.contributor.authorLoke, Ian
dc.contributor.authorMoginger, Uwe
dc.contributor.authorMoh, Edward SX
dc.contributor.authorNakano, Miyako
dc.contributor.authorRecuero, Saulo
dc.contributor.authorSethi, Manveen K
dc.contributor.authorSrougi, Miguel
dc.contributor.authorStavenhagen, Kathrin
dc.contributor.authorVenkatakrishnan, Vignesh
dc.contributor.authorWongtrakul-Kish, Katherine
dc.contributor.authorDiestel, Simone
dc.contributor.authorHoffmann, Peter
dc.contributor.authorKarlsson, Niclas G
dc.contributor.authorKolarich, Daniel
dc.contributor.authorMolloy, Mark P
dc.contributor.authorMuders, Michael H
dc.contributor.authorOehler, Martin K
dc.contributor.authorPacker, Nicolle H
dc.contributor.authorPalmisano, Giuseppe
dc.contributor.authorThaysen-Andersen, Morten
dc.date.accessioned2019-10-08T03:00:33Z
dc.date.available2019-10-08T03:00:33Z
dc.date.issued2019
dc.identifier.issn1615-9853
dc.identifier.doi10.1002/pmic.201900010
dc.identifier.urihttp://hdl.handle.net/10072/388125
dc.description.abstractWhile aberrant protein glycosylation is a recognised characteristic of human cancers, advances in glycoanalytics continue to discover new associations between glycoproteins and tumourigenesis. This glycomics‐centric study investigates a possible link between protein paucimannosylation, an under‐studied class of human N‐glycosylation [Man1‐3GlcNAc2Fuc0‐1], and human cancers. The paucimannosidic glycans (PMGs) of 34 cancer cell lines and 133 tissue samples spanning 11 cancer types and matching non‐cancerous specimens were profiled from 467 published and unpublished PGC‐LC‐MS/MS N‐glycome datasets collected over a decade within our laboratories. PMGs, particularly Man2‐3GlcNAc2Fuc1, were prominent features of 29 cancer cell lines, but the PMG level varied dramatically across and within the investigated cancer types (1.0%‐50.2%). Analyses of paired (tumour/non‐tumour) and stage‐stratified tissues demonstrated that PMGs are significantly enriched in tumour tissues from several cancer types including liver cancer (p = 0.0033) and colorectal cancer (p = 0.0017) and is elevated as a result of prostate cancer and chronic lymphocytic leukaemia progression (p<0.05). Surface expression of paucimannosidic epitopes was demonstrated on human glioblastoma cells using immunofluorescence while biosynthetic involvement of N‐acetyl‐β‐hexosaminidase was indicated by quantitative proteomics. This intriguing association between protein paucimannosylation and human cancers warrants further exploration to detail the biosynthesis, cellular location(s), protein carriers and functions of paucimannosylation in tumourigenesis and metastasis.
dc.languageEnglish
dc.publisherWiley
dc.relation.ispartofpagefrom1900010
dc.relation.ispartofpageto1900010
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.titleProtein Paucimannosylation is an Enriched N‐glycosylation Signature of Human Cancers
dc.typeJournal article
dc.type.descriptionC1 - Articles
dcterms.bibliographicCitationChatterjee, S; Lee, LY; Kawahara, R; Abrahams, JL; Adamczyk, B; Anugraham, M; Ashwood, C; Sumer‐Bayraktar, Z; Briggs, MT; Chik, JHL; Everest‐Dass, A; Förster, S; Hinneburg, H; Leite, KRM; Loke, I; Möginger, U; Moh, ESX; Nakano, M; Recuero, S; Sethi, MK; Srougi, M; Stavenhagen, K; Venkatakrishnan, V; Wongtrakul‐Kish, K; Diestel, S; Hoffmann, P; Karlsson, NG; Kolarich, D; Molloy, MP; Muders, MH; Oehler, MK; Packer, NH; Palmisano, G; Thaysen‐Andersen, M, Protein Paucimannosylation is an Enriched N‐glycosylation Signature of Human Cancerss, Proteomics, pp. 1900010-1900010
dc.date.updated2019-10-08T01:32:06Z
dc.description.versionPost-print
gro.description.notepublicThis publication has been entered into Griffith Research Online as an Advanced Online Version.
gro.rights.copyright© 2019 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim. This is the peer reviewed version of the following article: PProtein Paucimannosylation is an Enriched N ‐glycosylation Signature of Human Cancers, Proteomics, which has been published in final form at 10.1002/pmic.201900010. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Self-Archiving (http://olabout.wiley.com/WileyCDA/Section/id-828039.html)
gro.hasfulltextFull Text
gro.griffith.authorEverest-Dass, Arun
gro.griffith.authorKolarich, Daniel
gro.griffith.authorPacker, Nicki
gro.griffith.authorAbrahams, Jodie L.


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