Binding Affinity of PRTR Chemicals to Various Human Nuclear Receptors

  • INOUE Daisuke
    Division of Sustainable Energy and Environmental Engineering, Graduate School of Engineering, Osaka University
  • MATSUI Hisae
    Division of Sustainable Energy and Environmental Engineering, Graduate School of Engineering, Osaka University
  • SEI Kazunari
    Division of Sustainable Energy and Environmental Engineering, Graduate School of Engineering, Osaka University
  • YANG Min
    State Key Lab of Environmental Aquatic Chemistry, Research Center for Eco-Environmental Sciences, Chinese Academy of Sciences
  • HU Jianying
    College of Environmental Science, Peking University
  • ARAGANE Jun
    Advanced Technology R&D Center, Mitsubishi Electric Co.
  • HIROTSUJI Junji
    Advanced Technology R&D Center, Mitsubishi Electric Co.
  • NISHIKAWA Jun-ichi
    Department of Environmental Biochemistry, Graduate School of Pharmaceutical Sciences, Osaka University
  • IKE Michihiko
    Division of Sustainable Energy and Environmental Engineering, Graduate School of Engineering, Osaka University

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Other Title
  • PRTR化学物質の各種核内受容体に対する結合性
  • PRTR カガク ブッシツ ノ カクシュ カクナイ ジュヨウタイ ニタイスル ケツゴウセイ

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Abstract

Since the 1990s, population decreases, reproductive anomalies and malformations of highly aquatic animals have been increasingly reported. One possible cause is considered to be endocrine disruptive effects induced by environmental contaminants through a direct interaction with nuclear receptors, not only with steroid hormone receptors but also with other ones. In this study, we examined the binding affinities of 20 chemicals, which are registered in the Japanese Pollutant Release and Transfer Register (PRTR) and have been abundantly discharged into aquatic environments to eight human nuclear receptors and assessed their potential endocrine disruptive effects. Of the 20 PRTR chemicals tested, nonylphenol diethoxylate, telephthalic acid (TPA), and linear dodecyl-benzensulfonate (DBS) bound to at least two receptors at high concentrations. TPA and DBS enhanced the activities of both retinoic acid receptor (RAR) γ and vitamin D receptor (VDR) in a dose-dependent manner. This suggests that TPA and DBS may disturb the vitamin D endocrine functions mediated by a VDR-VDR homodimer or a VDR-RAR heterodimer. Also, our results indicate that endocrine disruptors unsuspected under the current assessment criteria could potentially bind to various nuclear receptors and disrupt endocrine systems mediated by such receptors.

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