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<title lang=en>Impact of biochemical design on estrogen receptor/estrogen response element interaction by surface plasmon resonance technology</title>
<creator>Habauzit, Denis</creator>
<creator>Bayle, Sandrine</creator>
<creator>Benimelis, David</creator>
<creator>Chopineau, Joel</creator>
<creator>Roig, Benoît</creator>
<contributor>TREC : Transcription, Environment and Cancer ; 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>
<contributor>IMT - Mines Alès Ecole Mines Télécom (IMT - MINES ALES)</contributor>
<contributor>Université de Nîmes (UNIMES)</contributor>
<contributor>Institut Charles Gerhardt Montpellier - Institut de Chimie Moléculaire et des Matériaux de Montpellier (ICGM ICMMM) ; Université Montpellier 1 (UM1) - Université Montpellier 2 - Sciences et Techniques (UM2) - Ecole Nationale Supérieure de Chimie de Montpellier (ENSCM) - Université de Montpellier (UM) - Centre National de la Recherche Scientifique (CNRS)</contributor>
<contributor>Laboratoire d'étude et de recherche en environnement et santé (LERES) ; École des Hautes Études en Santé Publique [EHESP] (EHESP)</contributor>
<description>International audience</description>
<source>ISSN: 0003-9861</source>
<source>EISSN: 1096-0384</source>
<source>Archives of Biochemistry and Biophysics</source>
<publisher>Elsevier</publisher>
<identifier>hal-00936061</identifier>
<identifier>https://hal.archives-ouvertes.fr/hal-00936061</identifier>
<identifier>https://hal.archives-ouvertes.fr/hal-00936061/document</identifier>
<identifier>https://hal.archives-ouvertes.fr/hal-00936061/file/Impactsur biochemical_design_on_estrogen_receptor_estrogen_response_element_interaction_by_surface_plasmon_resonance_technology-accepted.pdf</identifier>
<source>https://hal.archives-ouvertes.fr/hal-00936061</source>
<source>Archives of Biochemistry and Biophysics, Elsevier, 2014, 541, pp.61-66. 〈10.1016/j.abb.2013.11.006〉</source>
<identifier>DOI : 10.1016/j.abb.2013.11.006</identifier>
<relation>info:eu-repo/semantics/altIdentifier/doi/10.1016/j.abb.2013.11.006</relation>
<identifier>PUBMED : 24280273</identifier>
<relation>info:eu-repo/semantics/altIdentifier/pmid/24280273</relation>
<language>en</language>
<subject lang=es>Temperature</subject>
<subject lang=es>Surface plasmon resonance</subject>
<subject lang=es>Estrogen</subject>
<subject lang=es>Estrogen receptor</subject>
<subject lang=es>Dimerization</subject>
<subject lang=es>Solvent</subject>
<subject>[CHIM.MATE] Chemical Sciences/Material chemistry</subject>
<subject>[SDV.BBM.BC] Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM]</subject>
<subject>[SDV.BBM.BP] Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biophysics</subject>
<type>info:eu-repo/semantics/article</type>
<type>Journal articles</type>
<description lang=en>The estrogen receptor (ER) is a transcription factor that binds under 17-b-estradiol (E2) stimulation as homodimer to a short DNA consensus sequence named estrogen response element (ERE). The ER/ERE interaction has been assessed by several research groups through different methodologies notably by surface plasmon resonance (SPR) techniques. The biochemical parameters and conditions (solvent, ER concentration, salt, time and temperature) used to prepare samples before analysis were very different from one study to another. But no studies have aimed to compare the effect of these modifications on ER/ERE interaction. Therefore the main objective of the present paper was to assess the influence of biochemical parameters onto the ER/ERE interaction with the final aim to improve the comprehension of this interaction. Our results highlighted that parameters like solvent, ER concentration, salt and surfactant concentration, temperature and time deeply modify ER/ERE interaction. Nevertheless, the dimer formation under E2 stimulation occurred with all tested conditions. Altogether, incubation parameters of ER with E2, deeply modify its binding level onto ERE. These data constitute an important key point to consider for the improvement of ER/ERE detection method depending upon the aim of the study (interaction measurement, environmental detection, development of new technologies or devices).</description>
<date>2014-01-01</date>
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