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dc.contributor.authorTHIEBAUD, P.
dc.contributor.authorGARBAY, B.
dc.contributor.authorAUGUSTE, P.
dc.contributor.authorLE SENECHAL, C.
dc.contributor.authorMACIEJEWSKA, Z.
dc.contributor.authorFEDOU, S.
dc.contributor.authorGAUTHEREAU, X.
dc.contributor.authorCOSTAGLIOLI, Patricia
dc.contributor.authorTHEZE, N.
dc.date.accessioned2020-09-03T07:56:24Z
dc.date.available2020-09-03T07:56:24Z
dc.date.issued2016
dc.identifier.issn0196-9781
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/10894
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.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/Matériaux
bordeaux.journalPeptides
bordeaux.page21-28
bordeaux.volume83
bordeaux.hal.laboratoriesInstitut de Chimie & de Biologie des Membranes & des Nano-objets (CBMN) - UMR 5248*
bordeaux.hal.laboratoriesInstitut de Chimie & de Biologie des Membranes & des Nano-objets (CBMN, UMR 5248)
bordeaux.institutionUniversité de Bordeaux
bordeaux.institutionBordeaux INP
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