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hal.structure.identifierInserm U1035, Biotherapies des Maladies Genetiques et Cancers, Univ Bordeaux, CHU de Bordeaux, Pole de Biologie et Pathologie
dc.contributor.authorTHIÉBAUD, Pierre
hal.structure.identifierBiotechnologie des protéines recombinantes à visée santé
hal.structure.identifierLaboratoire de Chimie des Polymères Organiques [LCPO]
hal.structure.identifierTeam 3 LCPO : Polymer Self-Assembly & Life Sciences
dc.contributor.authorGARBAY, Bertrand
IDREF: 033777551
hal.structure.identifierInserm U1035, Biotherapies des Maladies Genetiques et Cancers, Univ Bordeaux, CHU de Bordeaux, Pole de Biologie et Pathologie
dc.contributor.authorAUGUSTE, Patrick
hal.structure.identifierBiotechnologie des protéines recombinantes à visée santé
dc.contributor.authorLE SENECHAL, Caroline
hal.structure.identifierInserm U1035, Biotherapies des Maladies Genetiques et Cancers, Univ Bordeaux, CHU de Bordeaux, Pole de Biologie et Pathologie
dc.contributor.authorMACIEJEWSKA, Zuzanna
hal.structure.identifierInserm U1035, Biotherapies des Maladies Genetiques et Cancers, Univ Bordeaux, CHU de Bordeaux, Pole de Biologie et Pathologie
dc.contributor.authorFÉDOU, Sandrine
hal.structure.identifierInserm U1035, Biotherapies des Maladies Genetiques et Cancers, Univ Bordeaux, CHU de Bordeaux, Pole de Biologie et Pathologie
dc.contributor.authorGAUTHEREAU, Xavier
hal.structure.identifierBiotechnologie des protéines recombinantes à visée santé
dc.contributor.authorCOSTAGLIOLI, Patricia
hal.structure.identifierInserm U1035, Biotherapies des Maladies Genetiques et Cancers, Univ Bordeaux, CHU de Bordeaux, Pole de Biologie et Pathologie
dc.contributor.authorTHEZE, Nadine
dc.date.accessioned2020
dc.date.available2020
dc.date.issued2016
dc.identifier.issn0196-9781
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/20190
dc.description.abstractEnBesides its widely described function in the innate immune response, no other clear physiological function has been attributed so far to the Liver-Expressed-Antimicrobial-Peptide 2 (LEAP2). We used the Xenopus embryo model to investigate potentially new functions for this peptide. We identified the amphibian leap2 gene which is highly related to its mammalian orthologues at both structural and sequence levels. The gene is expressed in the embryo mostly in the endoderm-derived tissues. Accordingly it is induced in pluripotent animal cap cells by FGF, activin or a combination of vegT/beta-catenin. Modulating leap2 expression level by gain-of-function strategy impaired normal embryonic development. When over-expressed in pluripotent embryonic cells derived from blastula animal cap explant, leap2 stimulated FGF while it reduced the activin response. Finally, we demonstrate that LEAP2 blocks FGF-induced migration of HUman Vascular Endothelial Cells (HUVEC). Altogether these findings suggest a model in which LEAP2 could act at the extracellular level as a modulator of FGF and activin signals, thus opening new avenues to explore it in relation with cellular processes such as cell differentiation and migration. (C) 2016 Elsevier Inc. All rights reserved.
dc.language.isoen
dc.publisherElsevier
dc.subject.enLIVER
dc.subject.enFUNCTIONAL-ANALYSIS
dc.subject.enMESODERM INDUCTION
dc.subject.enLeap2
dc.subject.enXenopus laevis
dc.subject.enEmbryo
dc.subject.enFGF
dc.subject.enActivin
dc.subject.enCell migration
dc.subject.enHUVEC
dc.subject.enPEPTIDE 2 LEAP-2
dc.subject.enEXPRESSED ANTIMICROBIAL PEPTIDE-2
dc.subject.enMOLECULAR CHARACTERIZATION
dc.subject.enGENES
dc.subject.enLAEVIS
dc.subject.enCELLS
dc.subject.enEVOLUTION
dc.title.enOverexpression of Leap2 impairs Xenopus embryonic development and modulates FGF and activin signals
dc.typeArticle de revue
dc.identifier.doi10.1016/j.peptides.2016.06.008
dc.subject.halChimie/Polymères
bordeaux.journalPeptides
bordeaux.page21-28
bordeaux.volume83
bordeaux.hal.laboratoriesLaboratoire de Chimie des Polymères Organiques (LCPO) - UMR 5629*
bordeaux.institutionBordeaux INP
bordeaux.institutionUniversité de Bordeaux
bordeaux.peerReviewedoui
hal.identifierhal-01373224
hal.version1
hal.origin.linkhttps://hal.archives-ouvertes.fr//hal-01373224v1
bordeaux.COinSctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Peptides&rft.date=2016&rft.volume=83&rft.spage=21-28&rft.epage=21-28&rft.eissn=0196-9781&rft.issn=0196-9781&rft.au=THI%C3%89BAUD,%20Pierre&GARBAY,%20Bertrand&AUGUSTE,%20Patrick&LE%20SENECHAL,%20Caroline&MACIEJEWSKA,%20Zuzanna&rft.genre=article


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