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Identification of a human estrogen receptor α tetrapeptidic fragment with dual antiproliferative and anti-nociceptive action

dc.rights.licenseopenen_US
dc.contributor.authorJOUFFRE, Baptiste
dc.contributor.authorACRAMEL, Alexandre
dc.contributor.authorBELNOU, Mathilde
dc.contributor.authorSANTOLLA, Maria Francesca
dc.contributor.authorTALIA, Marianna
dc.contributor.authorLAPPANO, Rosamaria
dc.contributor.authorNEMATI, Fariba
dc.contributor.authorDECAUDIN, Didier
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorKHEMTEMOURIAN, Lucie
dc.contributor.authorLIU, Wang-Qing
dc.contributor.authorMAGGIOLINI, Marcello
dc.contributor.authorESCHALIER, Alain
dc.contributor.authorMALLET, Christophe
dc.contributor.authorJACQUOT, Yves
dc.date.accessioned2024-04-24T13:43:22Z
dc.date.available2024-04-24T13:43:22Z
dc.date.issued2023-01-24
dc.identifier.issn2045-2322en_US
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/199322
dc.description.abstractEnThe synthetic peptide ERα17p (sequence: PLMIKRSKKNSLALSLT), which corresponds to the 295–311 region of the human estrogen receptor α (ERα), induces apoptosis in breast cancer cells. In mice and at low doses, it promotes not only the decrease of the size of xenografted triple-negative human breast tumors, but also anti-inflammatory and anti-nociceptive effects. Recently, we have shown that these effects were due to its interaction with the seven-transmembrane G protein-coupled estrogen receptor GPER. Following modeling studies, the C-terminus of this peptide (sequence: NSLALSLT) remains compacted at the entrance of the GPER ligand-binding pocket, whereas its N-terminus (sequence: PLMI) engulfs in the depth of the same pocket. Thus, we have hypothesized that the PLMI motif could support the pharmacological actions of ERα17p. Here, we show that the PLMI peptide is, indeed, responsible for the GPER-dependent antiproliferative and anti-nociceptive effects of ERα17p. By using different biophysical approaches, we demonstrate that the NSLALSLT part of ERα17p is responsible for aggregation. Overall, the tetrapeptide PLMI, which supports the action of the parent peptide ERα17p, should be considered as a hit for the synthesis of new GPER modulators with dual antiproliferative and anti-nociceptive actions. This study highlights also the interest to modulate GPER for the control of pain.
dc.language.isoENen_US
dc.rights.urihttp://creativecommons.org/licenses/by/
dc.title.enIdentification of a human estrogen receptor α tetrapeptidic fragment with dual antiproliferative and anti-nociceptive action
dc.typeArticle de revueen_US
dc.identifier.doi10.1038/s41598-023-28062-9en_US
dc.subject.halSciences du Vivant [q-bio]en_US
bordeaux.journalScientific Reportsen_US
bordeaux.page1326en_US
bordeaux.volume13en_US
bordeaux.hal.laboratoriesCBMN : Chimie & de Biologie des Membranes & des Nano-objets - UMR 5248en_US
bordeaux.issue1en_US
bordeaux.institutionUniversité de Bordeauxen_US
bordeaux.institutionBordeaux INPen_US
bordeaux.institutionCNRSen_US
bordeaux.peerReviewedouien_US
bordeaux.inpressnonen_US
bordeaux.import.sourcehal
hal.identifierhal-04087799
hal.version1
hal.popularnonen_US
hal.audienceInternationaleen_US
hal.exportfalse
workflow.import.sourcehal
dc.rights.ccPas de Licence CCen_US
bordeaux.COinSctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Scientific%20Reports&rft.date=2023-01-24&rft.volume=13&rft.issue=1&rft.spage=1326&rft.epage=1326&rft.eissn=2045-2322&rft.issn=2045-2322&rft.au=JOUFFRE,%20Baptiste&ACRAMEL,%20Alexandre&BELNOU,%20Mathilde&SANTOLLA,%20Maria%20Francesca&TALIA,%20Marianna&rft.genre=article


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