Utilize este identificador para referenciar este registo: https://hdl.handle.net/1822/62236

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dc.contributor.authorMarchiq, Ibtissampor
dc.contributor.authorAlbrengues, Jeanpor
dc.contributor.authorGranja, Sara Costapor
dc.contributor.authorGaggioli, Cédricpor
dc.contributor.authorPouysségur, Jacquespor
dc.contributor.authorSimon, Marie-Pierrepor
dc.date.accessioned2019-11-19T15:02:28Z-
dc.date.available2019-11-19T15:02:28Z-
dc.date.issued2015-09-22-
dc.identifier.citationMarchiq, I., Albrengues, J., Granja, S., Gaggioli, C., Pouysségur, J., & Simon, M. P. (2015). Knock out of the BASIGIN/CD147 chaperone of lactate/H+ symporters disproves its pro-tumour action via extracellular matrix metalloproteases (MMPs) induction. Oncotarget, 6(28), 24636.por
dc.identifier.issn1949-2553-
dc.identifier.urihttps://hdl.handle.net/1822/62236-
dc.description.abstractBASIGIN/CD147/EMMPRIN is a multifunctional transmembrane glycoprotein strongly expressed in tumours. BASIGIN controls tumour metabolism, particularly glycolysis by facilitating lactic acid export through the two monocarboxylate transporters MCT1 and hypoxia-inducible MCT4. However, before being recognized as a co-carrier of MCTs, BASIGIN was described as an inducer of extracellular matrix metalloproteases (MMPs). Early on, a model emerged in which, tumour cells use the extracellular domain of BASIGIN to recognize and stimulate neighbouring fibroblasts to produce MMPs. However, this model has remained hypothetical since a direct link between BASIGIN and MMPs production has not yet been clearly established. To validate the BASIGIN/MMP hypothesis, we developed BASIGIN knockouts in three human tumour cell lines derived from glioma, colon, and lung adenocarcinoma. By using co-culture experiments of either human or mouse fibroblasts and tumour cell lines we showed, contrary to what has been abundantly published, that the disruption of BASIGIN in tumour cells and in MEFs has no action on the production of MMPs. Our findings do not support the notion that the pro-tumoural action of BASIGIN is mediated via induction of MMPs. Therefore, we propose that to date, the strongest pro-tumoural action of BASIGIN is mediated through the control of fermentative glycolysis.por
dc.description.sponsorshipThe team was funded from Ligue Nationale Contre le Cancer (Equipe labellisée LNCC), Fondation ARC, INCa, ANR, the EU-FP7 “METOXIA”, SERVIER-CNRS, and Centre Lacassagnepor
dc.language.isoengpor
dc.publisherImpact Journalspor
dc.rightsopenAccesspor
dc.subjectAnimalspor
dc.subjectBasiginpor
dc.subjectCell Line, Tumorpor
dc.subjectCoculture Techniquespor
dc.subjectCulture Media, Conditionedpor
dc.subjectDown-Regulationpor
dc.subjectEndonucleasespor
dc.subjectFibroblastspor
dc.subjectGene Expression Regulation, Neoplasticpor
dc.subjectHumanspor
dc.subjectMatrix Metalloproteinasespor
dc.subjectMicepor
dc.subjectMonocarboxylic Acid Transporterspor
dc.subjectMuscle Proteinspor
dc.subjectNeoplasmspor
dc.subjectParacrine Communicationpor
dc.subjectSignal Transductionpor
dc.subjectSymporterspor
dc.subjectTransfectionpor
dc.subjectZinc Fingerspor
dc.subjectGene Knockout Techniquespor
dc.subjectcancer biologypor
dc.subjectmembrane transportpor
dc.subjectMCTpor
dc.subjectlactic acidpor
dc.subjectglycolysispor
dc.titleKnock out of the BASIGIN/CD147 chaperone of lactate/H+ symporters disproves its pro-tumour action via extracellular matrix metalloproteases (MMPs) inductionpor
dc.typearticlepor
dc.peerreviewedyespor
dc.relation.publisherversionwww.oncotarget.com/index.php?journal=oncotarget&page=article&op=view&path[]=4323&path[]=9656por
oaire.citationStartPage24636por
oaire.citationEndPage24648por
oaire.citationIssue28por
oaire.citationVolume6por
dc.identifier.doi10.18632/oncotarget.4323por
dc.identifier.pmid26284589por
dc.subject.fosCiências Médicas::Medicina Básicapor
dc.subject.wosScience & Technologypor
sdum.journalOncotargetpor
Aparece nas coleções:ICVS - Artigos em revistas internacionais / Papers in international journals

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