Please use this identifier to cite or link to this item: https://hdl.handle.net/10216/119034
Full metadata record
DC FieldValueLanguage
dc.creatorCampos, D
dc.creatorFreitas, D
dc.creatorGomes, J
dc.creatorReis, CA
dc.date.accessioned2019-02-21T12:16:16Z-
dc.date.available2019-02-21T12:16:16Z-
dc.date.issued2015
dc.identifier.issn1478-9450
dc.identifier.urihttps://hdl.handle.net/10216/119034-
dc.description.abstractGlycosylation is one of the most abundant forms of protein posttranslational modification. O-glycosylation is a major type of protein glycosylation, comprising different types and structures expressed in several physiologic and pathologic conditions. The understanding of protein attachment site and glycan structure is of the utmost importance for the clarification of the role glycosylation plays in normal cells and in pathological conditions. Neoplastic transformation frequently shows the expression of immature truncated O-glycans. These aberrantly expressed O-glycans have been shown to induce oncogenic properties and can be detected in premalignant lesions, meaning that they are an important source of biomarkers. This article addresses the recent application of genetically engineered cancer cell models to produce simplified homogenous O-glycans allowing the characterization of cancer cells O-glycoproteomes, using advanced mass spectrometry methods and the identification of potential cancer-specific O-glycosylation sites. This article will also discuss possible applications of these biomarkers in the cancer field.
dc.description.sponsorshipIPATIMUP integrates the i3S Research Unit, which is partially supported by FCT, the Portuguese Foundation for Science and Technology. The authors were supported by FEDER funds through the Operational Programme for Competitiveness Factors-COMPETE and National Funds through the FCT-Foundation for Science and Technology, under the projects: PEst-C/SAU/LA0003/2013 and PTDC/BBB-EBI/0786/2012. D Campos has received a grant from the FCT (grant number: SFRH/BD/73717/2010). D Freitas has received a grant from the FCT (grant number: PD/BI/105913/2014).
dc.language.isoeng
dc.publisherTaylor & Francis
dc.relationinfo:eu-repo/grantAgreement/FCT/COMPETE/132983/PT
dc.relationinfo:eu-repo/grantAgreement/FCT/COMPETE/125428/PT
dc.relationinfo:eu-repo/grantAgreement/FCT/SFRH/SFRH%2FBD%2F73717%2F2010/PT
dc.relation.ispartofExpert Review of Proteomics, vol.12(4), p. 337-342
dc.rightsopenAccess
dc.subjectBiomarkers
dc.subjectGlycoproteins/metabolism
dc.subjectGlycosylation
dc.subjectMass Spectrometry
dc.subjectModels, Biological
dc.subjectNeoplasms/metabolism
dc.subjectProteome
dc.titleGlycoengineered cell models for the characterization of cancer O-glycoproteome: an innovative strategy for biomarker discovery
dc.typeArtigo em Revista Científica Internacional
dc.contributor.uportoInstituto de Investigação e Inovação em Saúde
dc.identifier.doi10.1586/14789450.2015.1059758
dc.relation.publisherversionhttps://www.tandfonline.com/doi/abs/10.1586/14789450.2015.1059758?journalCode=ieru20
Appears in Collections:I3S - Artigo em Revista Científica Internacional

Files in This Item:
File Description SizeFormat 
Campos D_2015.pdf492.35 kBAdobe PDFThumbnail
View/Open


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