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<title lang=en>NHE-1 relocation outside cholesterol-rich membrane microdomains is associated with its benzo[a]pyrene-related apoptotic function.</title>
<creator>Tekpli, Xavier</creator>
<creator>Huc, Laurence</creator>
<creator>Sergent, Odile</creator>
<creator>Dendelé, Béatrice</creator>
<creator>Dimanche-Boitrel, Marie-Thérèse</creator>
<creator>Holme, Jørn, </creator>
<creator>Lagadic-Gossmann, Dominique</creator>
<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>Stress, membrane, signalisation ; 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>Division of Environmental Medicine ; Norwegian Institute of Public Health</contributor>
<contributor>Ligue Nationale contre le Cancer</contributor>
<description>International audience</description>
<source>ISSN: 1015-8987</source>
<source>EISSN: 1421-9778</source>
<source>Cellular Physiology and Biochemistry</source>
<publisher>Karger</publisher>
<identifier>inserm-00871487</identifier>
<identifier>http://www.hal.inserm.fr/inserm-00871487</identifier>
<identifier>http://www.hal.inserm.fr/inserm-00871487/document</identifier>
<identifier>http://www.hal.inserm.fr/inserm-00871487/file/NHE-1_Relocation_Outside_Cholesterol.accepted.pdf</identifier>
<source>http://www.hal.inserm.fr/inserm-00871487</source>
<source>Cellular Physiology and Biochemistry, Karger, 2012, 29 (5-6), pp.657-66. 〈10.1159/000171027〉</source>
<identifier>DOI : 10.1159/000171027</identifier>
<relation>info:eu-repo/semantics/altIdentifier/doi/10.1159/000171027</relation>
<identifier>PUBMED : 22613966</identifier>
<relation>info:eu-repo/semantics/altIdentifier/pmid/22613966</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>BACKGROUND: Polycyclic aromatic hydrocarbons (PAHs), such as benzo[a]pyrene (B[a]P), are ubiquitous toxic environmental pollutants capable of inducing cell death. Intracellular pH plays a key role in the regulation of cell survival and death. Our previous works have demonstrated that intracellular alkalinization mediated by Na(+)/H(+) exchanger 1 (NHE-1) is a critical event involved in B[a]P-induced apoptosis. The aim of this study was to further elucidate the mechanisms of NHE-1 activation upon B[a]P exposure. METHODS: We tested the effects of plasma membrane cholesterol enrichment or depletion on B[a]P-induced NHE-1 activation related to apoptosis. We isolated cholesterol-rich plasma membrane microdomains to assess NHE-1 submembrane location and immunoprecipitated NHE-1 from the different sub-membrane fractions obtained to examine NHE-1 protein interactions during B[a]P-induced apoptosis. RESULTS: We found that NHE-1 is preferentially located in cholesterol-rich microdomains and that B[a]P activates NHE-1 via its relocation and binding of calmodulin outside these specialized plasma membrane microstructures; these events are necessary for the execution of the apoptosis-related intracellular alkalinization. CONCLUSION: Plasma membrane location of NHE-1 affects its protein interactions and apoptotic function.</description>
<date>2012</date>
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