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<title lang=en>Functional characterization of a chimeric soluble Fas ligand polymer with in vivo anti-tumor activity.</title>
<creator>Daburon, Sophie</creator>
<creator>Devaud, Christel</creator>
<creator>Costet, Pierre</creator>
<creator>Morello, Aurore</creator>
<creator>Garrigue-Antar, Laure</creator>
<creator>Maillasson, Mike</creator>
<creator>Hargous, Nathalie</creator>
<creator>Lapaillerie, Delphine</creator>
<creator>Bonneu, Marc</creator>
<creator>Dechanet-Merville, Julie</creator>
<creator>Legembre, Patrick</creator>
<creator>Capone, Myriam</creator>
<creator>Moreau, Jean-François</creator>
<creator>Taupin, Jean-Luc</creator>
<contributor>Composantes innées de la réponse immunitaire et différenciation (CIRID) ; Université Bordeaux Segalen - Bordeaux 2 - Centre National de la Recherche Scientifique (CNRS)</contributor>
<contributor>Animalerie spécialisée ; Université Bordeaux Segalen - Bordeaux 2</contributor>
<contributor>Laboratoire de recherche sur la croissance cellulaire, la réparation et la régénération tissulaires (CRRET) ; Université Paris-Est Créteil Val-de-Marne - Paris 12 (UPEC UP12) - Centre National de la Recherche Scientifique (CNRS)</contributor>
<contributor>Centre de Recherche en Cancérologie / Nantes - Angers (CRCNA) ; CHU Angers - CHU Nantes - Hôtel-Dieu de Nantes - Institut National de la Santé et de la Recherche Médicale (INSERM) - Hôpital Laennec - Centre National de la Recherche Scientifique (CNRS) - Faculté de Médecine d'Angers</contributor>
<contributor>Centre génomique fonctionnelle ; Université Bordeaux Segalen - Bordeaux 2</contributor>
<contributor>Récepteur de mort et échappement tumoral ; Institut de recherche, santé, environnement et travail [Rennes] (Irset) ; Université d'Angers (UA) - Université des Antilles et de la Guyane (UAG) - Université de Rennes 1 (UR1) - École des Hautes Études en Santé Publique [EHESP] (EHESP) - Institut National de la Santé et de la Recherche Médicale (INSERM) - Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique ) - Université d'Angers (UA) - Université des Antilles et de la Guyane (UAG) - Université de Rennes 1 (UR1) - École des Hautes Études en Santé Publique [EHESP] (EHESP) - Institut National de la Santé et de la Recherche Médicale (INSERM) - Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique )</contributor>
<description>International audience</description>
<source>ISSN: 1932-6203</source>
<source>PLoS ONE</source>
<publisher>Public Library of Science</publisher>
<identifier>hal-00873684</identifier>
<identifier>https://hal.archives-ouvertes.fr/hal-00873684</identifier>
<identifier>https://hal.archives-ouvertes.fr/hal-00873684/document</identifier>
<identifier>https://hal.archives-ouvertes.fr/hal-00873684/file/Functional_Characterization-accepted.pdf</identifier>
<source>https://hal.archives-ouvertes.fr/hal-00873684</source>
<source>PLoS ONE, Public Library of Science, 2013, 8 (1), pp.e54000. 〈10.1371/journal.pone.0054000〉</source>
<identifier>DOI : 10.1371/journal.pone.0054000</identifier>
<relation>info:eu-repo/semantics/altIdentifier/doi/10.1371/journal.pone.0054000</relation>
<identifier>PUBMED : 23326557</identifier>
<relation>info:eu-repo/semantics/altIdentifier/pmid/23326557</relation>
<language>en</language>
<subject>[SDV.CAN] Life Sciences [q-bio]/Cancer</subject>
<type>info:eu-repo/semantics/article</type>
<type>Journal articles</type>
<description lang=en>Binding of ligand FasL to its receptor Fas triggers apoptosis via the caspase cascade. FasL itself is homotrimeric, and a productive apoptotic signal requires that FasL be oligomerized beyond the homotrimeric state. We generated a series of FasL chimeras by fusing FasL to domains of the Leukemia Inhibitory Factor receptor gp190 which confer homotypic oligomerization, and analyzed the capacity of these soluble chimeras to trigger cell death. We observed that the most efficient FasL chimera, called pFasL, was also the most polymeric, as it reached the size of a dodecamer. Using a cellular model, we investigated the structure-function relationships of the FasL/Fas interactions for our chimeras, and we demonstrated that the Fas-mediated apoptotic signal did not solely rely on ligand-mediated receptor aggregation, but also required a conformational adaptation of the Fas receptor. When injected into mice, pFasL did not trigger liver injury at a dose which displayed anti-tumor activity in a model of human tumor transplanted to immunodeficient animals, suggesting a potential therapeutic use. Therefore, the optimization of the FasL conformation has to be considered for the development of efficient FasL-derived anti-cancer drugs targeting Fas.</description>
<date>2013</date>
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