Full metadata record

DC Field Value Language
dc.contributor.authorPark, Hae-Min-
dc.contributor.authorHwang, Mintai Peter-
dc.contributor.authorKim, Yoon-Woo-
dc.contributor.authorKim, Kyoung-Jin-
dc.contributor.authorJin, Jang Mi-
dc.contributor.authorKim, Young Hwan-
dc.contributor.authorYang, Yung-Hun-
dc.contributor.authorLee, Kwan Hyi-
dc.contributor.authorKim, Yun-Gon-
dc.date.accessioned2024-01-20T06:04:09Z-
dc.date.available2024-01-20T06:04:09Z-
dc.date.created2021-09-04-
dc.date.issued2015-09-02-
dc.identifier.issn0008-6215-
dc.identifier.urihttps://pubs.kist.re.kr/handle/201004/125033-
dc.description.abstractThe aberrant glycosylation profile on the surface of cancer cells has been recognized for its potential diagnostic value towards assessing tumor progression. In this study, we initially investigate N-glycan profiles on the surface of normal (HPDE) and cancerous (Capan-1, Panc-1, and MIA PaCa-2) pancreatic cell lines, which are from different sites of pancreatic tumor. The enzymatically deglycosylated total N-glycans are permethylated via a quantitative solid-phase method and then analyzed by using MALDI-TOF MS and MALDI-QIT-TOF MS. We demonstrate that the level of high-mannose type glycans is higher among Capan-1 cells-pancreatic cancer cells that have metastasized to the liver-than that observed among Panc-1 and MIA PaCa-2 cells-pancreatic cancer cells from the pancreas duct head and tail regions, respectively. Furthermore, the relative abundance of highly-branched sialyted N-glycans is significantly up-regulated on Panc-1 and MIA PaCa-2 pancreatic cancer cells compared to that of normal HPDE pancreas cells. Taken together, these results indicate that specific N-glycosylation profile changes in pancreatic cancer cells can be used to not only distinguish between normal and cancerous cells but also provide more information on their location and metastatic potential. (C) 2015 Elsevier Ltd. All rights reserved.-
dc.languageEnglish-
dc.publisherELSEVIER SCI LTD-
dc.subjectACETYLGLUCOSAMINYLTRANSFERASE V-
dc.subjectALTERED GLYCOSYLATION-
dc.subjectGLYCANS-
dc.subjectSERUM-
dc.subjectGLYCOPROTEINS-
dc.subjectHAPTOGLOBIN-
dc.subjectOLIGOSACCHARIDES-
dc.subjectFUCOSYLATION-
dc.subjectCELLS-
dc.titleMass spectrometry-based N-linked glycomic profiling as a means for tracking pancreatic cancer metastasis-
dc.typeArticle-
dc.identifier.doi10.1016/j.carres.2015.04.019-
dc.description.journalClass1-
dc.identifier.bibliographicCitationCARBOHYDRATE RESEARCH, v.413, pp.5 - 11-
dc.citation.titleCARBOHYDRATE RESEARCH-
dc.citation.volume413-
dc.citation.startPage5-
dc.citation.endPage11-
dc.description.journalRegisteredClassscie-
dc.description.journalRegisteredClassscopus-
dc.identifier.wosid000359202300002-
dc.identifier.scopusid2-s2.0-84937409236-
dc.relation.journalWebOfScienceCategoryBiochemistry & Molecular Biology-
dc.relation.journalWebOfScienceCategoryChemistry, Applied-
dc.relation.journalWebOfScienceCategoryChemistry, Organic-
dc.relation.journalResearchAreaBiochemistry & Molecular Biology-
dc.relation.journalResearchAreaChemistry-
dc.type.docTypeArticle-
dc.subject.keywordPlusACETYLGLUCOSAMINYLTRANSFERASE V-
dc.subject.keywordPlusALTERED GLYCOSYLATION-
dc.subject.keywordPlusGLYCANS-
dc.subject.keywordPlusSERUM-
dc.subject.keywordPlusGLYCOPROTEINS-
dc.subject.keywordPlusHAPTOGLOBIN-
dc.subject.keywordPlusOLIGOSACCHARIDES-
dc.subject.keywordPlusFUCOSYLATION-
dc.subject.keywordPlusCELLS-
dc.subject.keywordAuthorPancreatic cells-
dc.subject.keywordAuthorN-glycans-
dc.subject.keywordAuthorQualitative and quantitative analysis-
dc.subject.keywordAuthorMALDI-TOF MS-
Appears in Collections:
KIST Article > 2015
Files in This Item:
There are no files associated with this item.
Export
RIS (EndNote)
XLS (Excel)
XML

qrcode

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

BROWSE