Please use this identifier to cite or link to this item: http://hdl.handle.net/11452/30221
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dc.contributor.authorChesney, Jason A.-
dc.date.accessioned2023-01-02T10:56:08Z-
dc.date.available2023-01-02T10:56:08Z-
dc.date.issued2017-01-31-
dc.identifier.citationYalçın, A. vd. (2017). ''6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase-3 is required for transforming growth factor β1-enhanced invasion of Panc1 cells in vitro''. Biochemical and Biophysical Research Communications, 484(3), 687-693.en_US
dc.identifier.issn0006-291X-
dc.identifier.urihttps://doi.org/10.1016/j.bbrc.2017.01.178-
dc.identifier.urihttps://www.sciencedirect.com/science/article/pii/S0006291X17302462-
dc.identifier.uri1090-2104-
dc.identifier.urihttp://hdl.handle.net/11452/30221-
dc.description.abstractTransforming growth factor [31 (TGF beta 1) is a well -established inducer of the epithelial-mesenchymal transition (EMT) that is essential for the acquisition of malignant properties, such as invasion, in tumor cells. Although recent studies suggest that the EMT in tumor cells is associated with reprogramming of energy metabolism and TGF beta 1 has been shown to stimulate glycolysis in multiple primary cell lines, little is known about TGF beta l 's effect on glycolysis and glycolytic regulators in transformed cells. Given the known regulatory role of 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase-3 (PFKFB3) in glycolysis and association of glycolytic activity with malignant features such as invasion, we sought to investigate whether TGF beta 1 regulates PFKFB3 expression and if PFKFB3 is involved in the TGF beta l -mediated increase in the invasive ability of the Panc1 cell cline a well -established model of TGF beta 1 -initiated EMT. Herein we demonstrate that TGF beta 1 induces PFKFB3 expression and stimulates glycolysis in Panci cells. We also show that s1RNA silencing of PFKFB3 prevents the stimulation of glycolysis and in vitro invasive ability of Panci cells by TGF beta 1. Furthermore, PFKFB3 silencing suppresses the TGFfil -mediated induction of the Snail protein, suggesting that PFKFB3 is required for the regulation of Snail expression by TGFfil. Taken together, our study identifies PFKFB3 as a key TGF beta 1 effector protein that mediates TGF beta 1's effect on Snail expression, invasion, and glycolysis.en_US
dc.language.isoenen_US
dc.publisherElsevieren_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectBiochemistry & molecular biologyen_US
dc.subjectBiophysicsen_US
dc.subjectGlycolysisen_US
dc.subjectPFKFB3en_US
dc.subjectSnailen_US
dc.subjectTransforming growth factor β1en_US
dc.subjectEpithelial-mesenchymal transitionen_US
dc.subjectFactor-betaen_US
dc.subjectTgf-betaen_US
dc.subjectTumor-growthen_US
dc.subjectGlucose-metabolismen_US
dc.subjectLactate productionen_US
dc.subjectCanceren_US
dc.subjectPfkfb3en_US
dc.subjectSnailen_US
dc.subjectInhibitionen_US
dc.subject.meshCell line, tumoren_US
dc.subject.meshCell movementen_US
dc.subject.meshGene expression regulation, enzymologicen_US
dc.subject.meshGene expression regulation, neoplasticen_US
dc.subject.meshGlucoseen_US
dc.subject.meshNeoplasm invasivenessen_US
dc.subject.meshPancreatic neoplasmsen_US
dc.subject.meshPeptide fragmentsen_US
dc.subject.meshPhosphofructokinase-2en_US
dc.subject.meshSignal transductionen_US
dc.subject.meshSnail family transcription factorsen_US
dc.subject.meshTransforming growth factor beta1en_US
dc.subject.meshHumansen_US
dc.title6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase-3 is required for transforming growth factor β1-enhanced invasion of Panc1 cells in vitroen_US
dc.typeArticletr_TR
dc.identifier.wos000395963900034tr_TR
dc.identifier.scopus2-s2.0-85011263952tr_TR
dc.relation.tubitak113Z776tr_TR
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergitr_TR
dc.contributor.departmentUludağ Üniversitesi/Veteriner Fakültesi/Biyokimya Anabilim Dalı.tr_TR
dc.contributor.departmentUludağ Üniversitesi/Veteriner Fakültesi/Histoloji ve Embriyoloji Anabilim Dalı.tr_TR
dc.contributor.departmentUludağ Üniversitesi/Fen-Edebiyat Fakültesi/Biyoloji Bölümü.tr_TR
dc.relation.bapOUAP(V)-2015/27tr_TR
dc.contributor.orcid0000-0001-8519-8375tr_TR
dc.contributor.orcid0000-0003-1733-4288tr_TR
dc.contributor.orcid0000-0003-0796-5000tr_TR
dc.contributor.orcid0000-0002-4177-3478tr_TR
dc.contributor.orcid0000-0002-7698-0872tr_TR
dc.identifier.startpage687tr_TR
dc.identifier.endpage693tr_TR
dc.identifier.volume484tr_TR
dc.identifier.issue3tr_TR
dc.relation.journalBiochemical and Biophysical Research Communicationsen_US
dc.contributor.buuauthorYalçın, Abdullah-
dc.contributor.buuauthorSolakoğlu, Tuğba H.-
dc.contributor.buuauthorÖzcan, Selahattin C.-
dc.contributor.buuauthorGüzel, Saime-
dc.contributor.buuauthorPeker, Sabire-
dc.contributor.buuauthorÇelikler, Serap-
dc.contributor.buuauthorBalaban, Başak D.-
dc.contributor.buuauthorSevinç, Elif-
dc.contributor.buuauthorGürpınar, Yunus-
dc.contributor.researcheridABI-4164-2020tr_TR
dc.contributor.researcheridAAA-6938-2022tr_TR
dc.contributor.researcheridAAH-4275-2021tr_TR
dc.contributor.researcheridAAH-2767-2021tr_TR
dc.relation.collaborationYurt dışıtr_TR
dc.identifier.pubmed28161638tr_TR
dc.subject.wosBiochemistry & molecular biologyen_US
dc.subject.wosBiophysicsen_US
dc.indexed.wosSCIEen_US
dc.indexed.scopusScopusen_US
dc.indexed.pubmedPubMeden_US
dc.wos.quartileQ3 (Biochemistry & molecular biology)en_US
dc.wos.quartileQ2 (Biophysics)en_US
dc.contributor.scopusid36857831000tr_TR
dc.contributor.scopusid57193156208tr_TR
dc.contributor.scopusid22835997800tr_TR
dc.contributor.scopusid55460886200tr_TR
dc.contributor.scopusid55109615900tr_TR
dc.contributor.scopusid8234554800tr_TR
dc.contributor.scopusid6604052452tr_TR
dc.contributor.scopusid56508326500tr_TR
dc.contributor.scopusid57193160752tr_TR
dc.subject.scopusPhosphofructokinase-2; Apoptosis; Glycolysisen_US
dc.subject.emtree6 phosphofructo 2 kinaseen_US
dc.subject.emtree6 phosphofructo 2 kinase fructose 2,6 bisphosphatase 3en_US
dc.subject.emtreeSmall interfering RNAen_US
dc.subject.emtreeTransforming growth factor beta1en_US
dc.subject.emtreeUnclassified drugen_US
dc.subject.emtreeUvomorulinen_US
dc.subject.emtree6 phosphofructo 2 kinaseen_US
dc.subject.emtreeGlucoseen_US
dc.subject.emtreePeptide fragmenten_US
dc.subject.emtreePFKFB3 protein, humanen_US
dc.subject.emtreeTranscription factor Snailen_US
dc.subject.emtreeTransforming growth factor beta1en_US
dc.subject.emtreeTransforming growth factor beta1 (41-65)en_US
dc.subject.emtreeTranscription factor snailen_US
dc.subject.emtreeArticleen_US
dc.subject.emtreeCell invasionen_US
dc.subject.emtreeCell proliferationen_US
dc.subject.emtreeCell structureen_US
dc.subject.emtreeCell viabilityen_US
dc.subject.emtreeControlled studyen_US
dc.subject.emtreeEpithelial mesenchymal transitionen_US
dc.subject.emtreeGene expressionen_US
dc.subject.emtreeGene silencingen_US
dc.subject.emtreeGlucose metabolismen_US
dc.subject.emtreeGlycolysisen_US
dc.subject.emtreeHumanen_US
dc.subject.emtreeHuman cellen_US
dc.subject.emtreeIn vitro studyen_US
dc.subject.emtreePancreas adenocarcinomaen_US
dc.subject.emtreePriority journalen_US
dc.subject.emtreeProtein expressionen_US
dc.subject.emtreeSignal transductionen_US
dc.subject.emtreeTransformed cellen_US
dc.subject.emtreeCell motionen_US
dc.subject.emtreeGene expression regulationen_US
dc.subject.emtreeMetabolismen_US
dc.subject.emtreePancreas tumoren_US
dc.subject.emtreePathologyen_US
dc.subject.emtreeTumor cell lineen_US
dc.subject.emtreeTumor invasionen_US
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