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<datestamp>2018-01-11</datestamp>
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<publisher>HAL CCSD</publisher>
<title lang=en>Activation of EGFR by small compounds through coupling the generation of hydrogen peroxide to stable dimerization of Cu/Zn SOD1</title>
<creator>Sakanyan, Vehary</creator>
<creator>Hulin, Philippe</creator>
<creator>Sousa, Rodolphe, </creator>
<creator>Silva, Viviane A. O.</creator>
<creator>Hambardzumyan, Artur</creator>
<creator>Nedellec, Steven</creator>
<creator>Tomasoni, Christophe</creator>
<creator>Logé, Cédric</creator>
<creator>Pineau, Charles</creator>
<creator>Roussakis, Christos</creator>
<creator>Fleury, Fabrice</creator>
<creator>Artaud, Isabelle</creator>
<contributor>IICiMed - EA 1155 ; Université de Nantes (UN) - UFR Sciences et Techniques - UFR des Sciences Pharmaceutiques</contributor>
<contributor>Institut Fédératif de Recherche 26 (IFR26) ; Université de Nantes (UN)</contributor>
<contributor>Plateforme MicroPicel ; Université de Nantes</contributor>
<contributor>Laboratoire de Chimie et de Biochimie Pharmacologiques et Toxicologiques (LCBPT - UMR 8601) ; Université Paris Descartes - Paris 5 (UPD5) - Centre National de la Recherche Scientifique (CNRS)</contributor>
<contributor>UMR 6286 Biotechnologie, Biocatalyse & Biorégulation (U3B) ; Centre National de la Recherche Scientifique (CNRS)</contributor>
<contributor>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 )</contributor>
<contributor>FRE 3478 ; Université de Nantes (UN) - Centre National de la Recherche Scientifique (CNRS)</contributor>
<description>International audience</description>
<source>ISSN: 2045-2322</source>
<source>EISSN: 2045-2322</source>
<source>Scientific Reports</source>
<publisher>Nature Publishing Group</publisher>
<identifier>hal-01279094</identifier>
<identifier>https://hal-univ-rennes1.archives-ouvertes.fr/hal-01279094</identifier>
<source>https://hal-univ-rennes1.archives-ouvertes.fr/hal-01279094</source>
<source>Scientific Reports, Nature Publishing Group, 2016, 6, pp.21088. 〈10.1038/srep21088〉</source>
<identifier>DOI : 10.1038/srep21088</identifier>
<relation>info:eu-repo/semantics/altIdentifier/doi/10.1038/srep21088</relation>
<identifier>PUBMED : 26883293</identifier>
<relation>info:eu-repo/semantics/altIdentifier/pmid/26883293</relation>
<language>en</language>
<subject>[SDV] Life Sciences [q-bio]</subject>
<type>info:eu-repo/semantics/article</type>
<type>Journal articles</type>
<description lang=en>Activation of cell signaling by reactive chemicals and pollutants is an important issue for human health. It has been shown that lipophilic nitro-benzoxadiazole (NBD) compounds rapidly move across the plasma membrane and enhance Epidermal Growth Factor Receptor (EGFR) tyrosine phosphorylation in cancer cells. Unlike ligand-dependent activation, the mechanism of this induction relies on the generation of hydrogen peroxide, which is involved in the activation of the catalytic site of the receptor and the inactivation of protein tyrosine phosphatase PTP-1B. Production of H2O2 during redox transformation of NBD compounds is associated with the transition of a monomeric form of Cu/Zn superoxide dismutase 1 (SOD1) to stable dimers. The highly stable and functionally active SOD1 dimer, in the absence of adequate activities in downstream reactions, promotes the disproportionate production and accumulation of intracellular hydrogen peroxide shortly after exposure to NBD compounds. The intrinsic fluorescence of small compounds was used to demonstrate their binding to SOD1. Our data indicate that H2O2 and concomitantly generated electrophilic intermediates behave as independent entities, but all contribute to the biological reactivity of NBD compounds. This study opens a promising path to identify new biomarkers of oxidative/electrophilic stress in the progression of cancer and other diseases</description>
<date>2016</date>
</dc>
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