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dc.contributor.authorSethi, Manveen K.
dc.contributor.authorKim, Hoguen
dc.contributor.authorPark, Cheol Keun
dc.contributor.authorBaker, Mark S.
dc.contributor.authorPaik, Young-Ki
dc.contributor.authorPacker, Nicolle H.
dc.contributor.authorHancock, William S.
dc.contributor.authorFanayan, Susan
dc.contributor.authorThaysen-Andersen, Morten
dc.date.accessioned2017-10-31T12:31:39Z
dc.date.available2017-10-31T12:31:39Z
dc.date.issued2015
dc.identifier.issn0959-6658
dc.identifier.doi10.1093/glycob/cwv042
dc.identifier.urihttp://hdl.handle.net/10072/336514
dc.description.abstractGlycomics may assist in uncovering the structure–function relationships of protein glycosylation and identify glycoprotein markers in colorectal cancer (CRC) research. Herein, we performed label-free quantitative glycomics on a carbon-liquid chromatography–tandem mass spectrometry-based analytical platform to accurately profile the N-glycosylation changes associated with CRC malignancy. N-Glycome profiling was performed on isolated membrane proteomes of paired tumorigenic and adjacent non-tumorigenic colon tissues from a cohort of five males (62.6 ± 13.1 y.o.) suffering from colorectal adenocarcinoma. The CRC tissues were typed according to their epidermal growth factor receptor (EGFR) status by western blotting and immunohistochemistry. Detailed N-glycan characterization and relative quantitation identified an extensive structural heterogeneity with a total of 91 N-glycans. CRC-specific N-glycosylation phenotypes were observed including an overrepresentation of high mannose, hybrid and paucimannosidic type N-glycans and an under-representation of complex N-glycans (P < 0.05). Sialylation, in particular α2,6-sialylation, was significantly higher in CRC tumors relative to non-tumorigenic tissues, whereas α2,3-sialylation was down-regulated (P < 0.05). CRC stage-specific N-glycosylation was detected by high α2,3-sialylation and low bisecting β1,4-GlcNAcylation and Lewis-type fucosylation in mid-late relative to early stage CRC. Interestingly, a novel link between the EGFR status and the N-glycosylation was identified using hierarchical clustering of the N-glycome profiles. EGFR-specific N-glycan signatures included high bisecting β1,4-GlcNAcylation and low α2,3-sialylation (both P < 0.05) relative to EGFR-negative CRC tissues. This is the first study to correlate CRC stage and EGFR status with specific N-glycan features, thus advancing our understanding of the mechanisms causing the biomolecular deregulation associated with CRC.
dc.description.peerreviewedYes
dc.languageEnglish
dc.language.isoeng
dc.publisherOxford University Press
dc.relation.ispartofpagefrom1064
dc.relation.ispartofpageto1078
dc.relation.ispartofissue10
dc.relation.ispartofjournalGlycobiology
dc.relation.ispartofvolume25
dc.subject.fieldofresearchBiochemistry and Cell Biology not elsewhere classified
dc.subject.fieldofresearchBiological Sciences
dc.subject.fieldofresearchMedical and Health Sciences
dc.subject.fieldofresearchcode060199
dc.subject.fieldofresearchcode06
dc.subject.fieldofresearchcode11
dc.titleIn-depth N-glycome profiling of paired colorectal cancer and non-tumorigenic tissues reveals cancer-, stage- and EGFR-specific protein N-glycosylation
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
gro.hasfulltextNo Full Text
gro.griffith.authorPacker, Nicki


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