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dc.contributor.authorChatterjee, S
dc.contributor.authorUgonotti, J
dc.contributor.authorLee, LY
dc.contributor.authorEverest-Dass, A
dc.contributor.authorKawahara, R
dc.contributor.authorThaysen-Andersen, M
dc.date.accessioned2021-11-25T07:55:44Z
dc.date.available2021-11-25T07:55:44Z
dc.date.issued2021
dc.identifier.issn1949-2553en_US
dc.identifier.doi10.18632/ONCOTARGET.28064en_US
dc.identifier.urihttp://hdl.handle.net/10072/410362
dc.description.abstractAberrant protein glycosylation is a prominent cancer feature. While many tumour-associated glycoepitopes have been reported, advances in glycoanalytics continue to uncover new associations between glycosylation and cancer. Guided by a comprehensive literature survey suggesting that oligomannosylation (Man5-9 GlcNAc2) is a widespread and often regulated glycosignature in human cancers, we here revisit a valuable compilation of nearly 500 porous graphitized carbon LC-MS/ MS N-glycomics datasets acquired across 11 human cancer types to systematically test for oligomannose-cancer associations. Firstly, the quantitative glycomics data obtained across 34 cancerous cell lines demonstrated that oligomannosylation is a pan-cancer feature spanning in a wide abundance range. In keeping with literature, our quantitative glycomics data of tumour and matching control tissues and new MALDI-MS imaging data of tissue microarrays showed a strong cancer-associated elevation of oligomannosylation in both basal cell (p = 1.78 × 10-12) and squamous cell (p = 1.23 × 10-11) skin cancer and colorectal cancer (p = 8.0 × 10-4). The glycomics data also indicated that some cancer types including gastric and liver cancer exhibit unchanged or reduced oligomannose levels, observations also supported by literature and MALDI-MS imaging data. Finally, expression data from public cancer repositories indicated that several α1,2-mannosidases are regulated in tumour tissues suggesting that these glycan-processing enzymes may contribute to the cancer-associated modulation of oligomannosylation. This omics-centric study has compiled robust glycomics and enzyme expression data revealing interesting molecular trends that open avenues to better understand the role of oligomannosylation in human cancers.en_US
dc.description.peerreviewedYesen_US
dc.languageenen_US
dc.publisherImpact Journals, LLCen_US
dc.relation.ispartofpagefrom2188en_US
dc.relation.ispartofpageto2205en_US
dc.relation.ispartofissue21en_US
dc.relation.ispartofjournalOncotargeten_US
dc.relation.ispartofvolume12en_US
dc.subject.fieldofresearchOncology and carcinogenesisen_US
dc.subject.fieldofresearchcode3211en_US
dc.titleTrends in oligomannosylation and α1,2-mannosidase expression in human cancersen_US
dc.typeJournal articleen_US
dc.type.descriptionC1 - Articlesen_US
dcterms.bibliographicCitationChatterjee, S; Ugonotti, J; Lee, LY; Everest-Dass, A; Kawahara, R; Thaysen-Andersen, M, Trends in oligomannosylation and α1,2-mannosidase expression in human cancers, Oncotarget, 2021, 12 (21), pp. 2188-2205en_US
dcterms.licensehttp://creativecommons.org/licenses/by/3.0en_US
dc.date.updated2021-11-24T00:36:48Z
dc.description.versionVersion of Record (VoR)en_US
gro.rights.copyright© 2021 Chatterjee et al. This is an open access article distributed under the terms of the Creative Commons Attribution License (CC BY 3.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.en_US
gro.hasfulltextFull Text
gro.griffith.authorEverest-Dass, Arun


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