Mostrar el registro sencillo del ítem

Role of Glycanation and Convertase Maturation of Soluble Glypican-3 in Inhibiting Proliferation of Hepatocellular Carcinoma Cells

dc.rights.licenseopenen_US
dc.contributor.authorSAAD, Ahmad
dc.contributor.authorLIET, Benjamin
dc.contributor.authorJOUCLA, Gilles
dc.contributor.authorSANTARELLI, Xavier
hal.structure.identifierINSERM U1035, Université de Bordeaux, UFR Sciences de la Vie et de la Santé, 33000 Bordeaux
dc.contributor.authorCHARPENTIER, Justine
hal.structure.identifierUniv Bordeaux, Ctr Genom Fonct, Plateforme Protéome
dc.contributor.authorCLAVEROL, Stephane
hal.structure.identifierINSERM U1035, Université de Bordeaux, UFR Sciences de la Vie et de la Santé, 33000 Bordeaux
dc.contributor.authorGROSSET, Christophe F.
dc.contributor.authorTREZEGUET, Veronique
dc.date.accessioned2020-03-25T15:09:09Z
dc.date.available2020-03-25T15:09:09Z
dc.date.issued2018
dc.identifier.issn1520-4995en_US
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/3940
dc.description.abstractEnGlypican 3 (GPC3) is a complex heparan sulfate proteoglycan associated with the outer surface of the plasma membrane by a glycosylphosphatidylinositol (GPI) anchor. It is also N-glycosylated and processed by a furin-like convertase. GPC3 has numerous biological functions. Although GPC3 is undetectable in normal liver tissue, it is abnormally and highly overexpressed in hepatocellular carcinoma (HCC). Interestingly, proliferation of HCC cells such as HepG2 and HuH7 is inhibited when they express a soluble form of GPC3 after lentiviral transduction. To obtain more insight into the role of some of its post-translational modifications, we designed a mutant GPC3, sGPC3m, without its GPI anchor, convertase cleavage site, and glycosaminoglycan chains. The highly pure sGPC3m protein strongly inhibited HuH7 and HepG2 cell proliferation in vitro and induced a significant increase in their cell doubling time. It changed the morphology of HuH7 cells but not that of HepG2. It induced the enlargement of HuH7 cell nuclear area and the restructuration of adherent cell junctions. Unexpectedly, for both cell types, the levels of apoptosis, cell division, and beta-catenin were not altered by sGPC3m, although growth inhibition was very efficient. Overall, our data show that glycanation and convertase maturation are not required for sGPC3m to inhibit HCC cell proliferation.
dc.language.isoENen_US
dc.subject.enCells
dc.subject.enInhibition
dc.subject.enCancer
dc.subject.enPeptides and proteins Cell physiology
dc.title.enRole of Glycanation and Convertase Maturation of Soluble Glypican-3 in Inhibiting Proliferation of Hepatocellular Carcinoma Cells
dc.typeArticle de revueen_US
dc.identifier.doi10.1021/acs.biochem.7b01208
dc.subject.halChimie/Matériauxen_US
bordeaux.journalBiochemistryen_US
bordeaux.page1201-1211en_US
bordeaux.volume57en_US
bordeaux.hal.laboratoriesInstitut de Chimie & de Biologie des Membranes & des Nano-objets (CBMN) - UMR 5248
bordeaux.issue7en_US
bordeaux.institutionBordeaux INPen_US
bordeaux.institutionUniversité de Bordeauxen_US
bordeaux.peerReviewedouien_US
bordeaux.inpressnonen_US
hal.identifierhal-03184413
hal.version1
hal.date.transferred2021-03-29T12:29:01Z
hal.exportfalse
bordeaux.COinSctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Biochemistry&rft.date=2018&rft.volume=57&rft.issue=7&rft.spage=1201-1211&rft.epage=1201-1211&rft.eissn=1520-4995&rft.issn=1520-4995&rft.au=SAAD,%20Ahmad&LIET,%20Benjamin&JOUCLA,%20Gilles&SANTARELLI,%20Xavier&CHARPENTIER,%20Justine&rft.genre=article


Archivos en el ítem

ArchivosTamañoFormatoVer

No hay archivos asociados a este ítem.

Este ítem aparece en la(s) siguiente(s) colección(ones)

Mostrar el registro sencillo del ítem