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Protein paucimannosylation is an enriched N-Glycosylation signature of human cancers

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dc.contributor.authorChatterjee, S.
dc.contributor.authorLee, L.Y.
dc.contributor.authorKawahara, R.
dc.contributor.authorAbrahams, J.L.
dc.contributor.authorBriggs, M.T.
dc.contributor.authorHoffman, P.
dc.contributor.authorThaysen Andersen, M.
dc.date.issued2019
dc.description.abstractWhile aberrant protein glycosylation is a recognized characteristic of human cancers, advances in glycoanalytics continue to discover new associations between glycoproteins and tumorigenesis. This glycomics-centric study investigates a possible link between protein paucimannosylation, an under-studied class of human N-glycosylation [Man1-3GlcNAc2Fuc0-1],and cancer. The paucimannosidic glycans (PMGs) of 34 cancer cell lines and 133 tissue samples spanning 11 cancer types and matching non-cancerous specimens are profiled from 467 published and unpublished PGC-LC-MS/MS N-glycome datasets collected over a decade. PMGs, particularly Man2-3GlcNAc2Fuc1, are prominent features of 29 cancer cell lines,but the PMG level varies dramatically across and within the cancer types (1.0–50.2%). Analyses of paired (tumor/nontumor) and stage-stratified tissues demonstrate that PMGs are significantly enriched in tumor 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 is demonstrated on human glioblastoma cells using immunofluorescence while biosynthetic involvement of N-acetyl-β-hexosaminidase is indicated by quantitative proteomics. This intriguing association between protein paucimannosylationand human cancers warrants further exploration to detail the biosynthesis, cellular location(s), protein carriers, andfunctions of paucimannosylation in tumorigenesis and metastasis.
dc.identifier.citationProteomics, 2019; 19(21-22, article no. 1900010):1-13
dc.identifier.doi10.1002/pmic.201900010
dc.identifier.issn1615-9861
dc.identifier.issn1615-9861
dc.identifier.orcidBriggs, M.T. [0000-0002-6601-2552]
dc.identifier.urihttps://hdl.handle.net/11541.2/139650
dc.language.isoen
dc.publisherWiley-VCH Verlag GmbH
dc.relation.fundingMacquarie University iMQRES 2017152
dc.relation.fundingFAPESP 2014/06863‐3
dc.relation.fundingFAPESP 2015/02866‐0
dc.relation.fundingFAPESP 2017/03010‐8
dc.relation.fundingFAPESP 2018/15549‐1
dc.relation.fundingCancer Institute NSW ECF181259
dc.relation.fundingGerman Research Foundation DI 1189/6‐1
dc.relation.fundingConselho Nacional de Desenvolvimento Científico e Tecnológico
dc.rightsCopyright 2015 Access Condition Notes: Accepted manuscript available after 1 October 2020
dc.source.urihttps://doi.org/10.1002/pmic.201900010
dc.subjectcancer
dc.subjectglycan
dc.subjectglycomics
dc.subjectpaucimannosidic glycan
dc.subjectprotein paucimannosylation
dc.titleProtein paucimannosylation is an enriched N-Glycosylation signature of human cancers
dc.typeJournal article
pubs.publication-statusPublished
ror.fileinfo12180630930001831 13180630920001831 9916319185801831_AM.pdf
ror.mmsid9916319185801831

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