Glycosylation changes leading to the increase in size on the common core of N-glycans, required enzymes, and related cancer-associated proteins

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dc.contributor.authorKaraçalı, Sabire
dc.contributor.authorİzzetoğlu, Savaş
dc.contributor.authorDeveci, Remziye
dc.date.accessioned2020-12-01T12:25:33Z
dc.date.available2020-12-01T12:25:33Z
dc.date.issued2014
dc.departmentEge Üniversitesien_US
dc.description.abstractGlycan parts of glycoconjugates on the surfaces of cells regulate many kinds of interactions between the cells and their immediate environments. Alterations in glycosylation on the cancer-associated glycoproteins are responsible for changes in their molecular interactions and biological functions. Glycosylation changes occur in the core and/or at the nonreducing end of the oligosaccharide chains of N-glycans. in this review, we focus on the branching of the common core structure of N-glycans, the responsible enzyme, and the extensions of some of the branches causing size increases on the surface of tumor cells. Abnormal branching, elongation of the branches, and increasing size of the common core of N-glycans are the typical features of these changes and are related with malignant transformations. Seven N-acetylglucosaminyltransferases (GnTs) (GnT-I, GnT-II, GnT-III, GnT-IV, GnT-V, GnT-VI, and GnT-IX) and alpha\1,6-fucosyltransferase (FUT8) initiate the new branches on the core. GnT-IV, GnT-V, and GnT-IX initiate the branches available for poly-LacNAc extensions, which are responsible for tumor progression and metastasis. GnT-III prevents the catalytic activity of GnT-II, GnT-IV, GnT-V, and FUT8 to form branching and elongation of the branches. the contributions of GnT-III and the other enzymes to the cancer progression are in conflict with each other. While GnT-III prevents cancer, the others increase metastasis. the function of FUT8 is related to signal transduction and its activity is higher in tumor tissue than in healthy tissue. the impact of glycosylation changes on some of the cancer-associated proteins (growth factor receptors, adhesion and signal molecules, CD147, TIMP-1, and matriptase) is also summarized.en_US
dc.identifier.endpage771en_US
dc.identifier.issn1300-0152
dc.identifier.issn1303-6092
dc.identifier.issue6en_US
dc.identifier.startpage754en_US
dc.identifier.urihttps://app.trdizin.gov.tr//makale/TVRZek1UVTBOQT09
dc.identifier.urihttps://hdl.handle.net/11454/65324
dc.identifier.volume38en_US
dc.indekslendigikaynakTR-Dizinen_US
dc.language.isoenen_US
dc.relation.ispartofTurkish Journal of Biologyen_US
dc.relation.publicationcategoryMakale - Ulusal Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.subjectBiyolojien_US
dc.titleGlycosylation changes leading to the increase in size on the common core of N-glycans, required enzymes, and related cancer-associated proteinsen_US
dc.typeArticleen_US

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