Screening data for the endocrine disrupting activities of 583 chemicals using the yeast two-hybrid assay

Screening data for the endocrine disrupting activities of 583 chemicals using the yeast two-hybrid assay

Data in Brief ∎ (∎∎∎∎) ∎∎∎–∎∎∎ 1 Contents lists available at ScienceDirect 2 3 4 5 6 journal homepage: www.elsevier.com/locate/dib 7 8 9 Data Article...

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1 Contents lists available at ScienceDirect 2 3 4 5 6 journal homepage: www.elsevier.com/locate/dib 7 8 9 Data Article 10 11 12 Q1 13 14 15 16 17 Fujio Shiraishi a, Ryo Kamata b, Masanori Terasaki c, 18 Hidetaka Takigami a, Yoshitaka Imaizumi a, Mayuko Yagishita a, 19 Daisuke Nakajima a 20 21 Q2 a National Institute for Environmental Studies, 16-2 Onogawa, Tsukuba, Ibaraki 305-8506, Japan b Kitasato University, 23-35-1 Higashi, Towada, Aomori 034-8628, Japan 22 c Iwate University, 3-18-8 Ueda, Morioka, Iwate 020-8550, Japan 23 24 25 a r t i c l e i n f o abstract 26 27 Article history: We screened 583 chemicals for receptor binding activity to the 28 Received 15 October 2018 human estrogen receptor (hER), the Japanese medaka estrogen 29 Received in revised form receptor (medER), and the aryl hydrocarbon receptor (AhR) using 30 5 November 2018 the yeast two-hybrid assay. The substances tested included subAccepted 14 November 2018 31 stances that could potentially be produced unintentionally by 32 industrial processes, such as halogenated steroids and phenols. 33 Antagonistic effects on hER and the androgen receptor were also 34 screened. The test chemicals were selected for screening on the basis of chemical structure associated with possible estrogen 35 receptor binding activity. The current study presents the report on 36 the screening of 583 chemicals for different kinds of endocrine 37 disrupting activity. 38 & 2018 Published by Elsevier Inc. This is an open access article 39 under the CC BY-NC-ND license 40 (http://creativecommons.org/licenses/by-nc-nd/4.0/). 41 42 43 44 45 46 47 48 49 50 E-mail address: [email protected] (M. Yagishita). 51 52 https://doi.org/10.1016/j.dib.2018.11.071 53 2352-3409/& 2018 Published by Elsevier Inc. This is an open access article under the CC BY-NC-ND license 54 (http://creativecommons.org/licenses/by-nc-nd/4.0/).

Data in Brief

Screening data for the endocrine disrupting activities of 583 chemicals using the yeast two-hybrid assay

Please cite this article as: F. Shiraishi, et al., Screening data for the endocrine disrupting activities of 583 chemicals using the yeast two-hybrid assay, Data in Brief (2018), https://doi.org/10.1016/j. dib.2018.11.071i

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Specifications table Subject area More specific subject area Type of data How data was acquired Data format Experimental factors

Biology Toxicology Table Yeast two-hybrid assay. Luminescence was read on a 96-well plate luminometer (Luminescencer JNR AB2100; Atto Corp., Tokyo, Japan) Raw data 583 chemicals of receptor binding activities, yeast toxicities, and photobacterium toxicities were tested. Each positive control was 17β-estradiol (hER-, medER-agonistic, β-naphthoflavone (AhR-agonistic)), 4-hydroxytamoxygen (ER-antagonistic), and 1-nitropyrene (AR-antagonistic).

Experimental features

Data source location Data accessibility Related research article

The hERα-, medERα-, and AhR-agonist activities and hERα- and AR-antagonist activities of the 583 test chemicals were measured using a yeast two-hybrid assay system. The hERα, medERα, or human AhR and the coactivator TIF2 were introduced into each yeast cell (Saccharomyces cerevisiae strain Y190) in accordance with the method by Nishikawa [1]. Tsukuba, Ibaraki, Japan All data are presented in this article. Kamata R., Shiraishi F., Nishikawa J., Yonemoto J. and Shiraishi H., 2008. Screening and detection of the in vitro agonistic activity of xenobiotics on the retinoic acid receptor. Toxicol. in vitro. 22, 1050–1061 [2] Kamata R., Nakajima D., and Shiraishi F., 2018. Agonistic effects of diverse xenobiotics on the constitutive androstane receptor as detected in a recombinant yeast-cell assay. Toxicol. in vitro. 46, 335–349 [3]

Value of the data

 Screening for endocrine disrupting activity of 583 chemicals was conducted by yeast-two hybrid assay.

 These data are evaluated; because few studies have carried out to evaluate several kinds of endocrine disrupting activities for same assay system and same timing.

 Each endocrine disrupting activity of 583 chemicals are shown with not only positive or negative, but also each activity values.

 This is a first report on estrogen receptor binding activities of Japanese medaka.  Several synthesis chemicals which may be released as unknown chemicals with endocrine disrupting properties by accident are included in 583 chemicals.

1. Data The substances tested included substances that could potentially be produced unintentionally by industrial processes, such as halogenated steroids and phenols. Antagonistic effects on hER and the androgen receptor were also screened. The test chemicals were selected for screening on the basis of chemical structure associated with possible estrogen receptor binding activity. The main positive chemical groups associated with each receptor binding activity were endogenous hormones (for hER or medER), and polycyclic aromatic compounds (AhR), respectively, see Table.

Please cite this article as: F. Shiraishi, et al., Screening data for the endocrine disrupting activities of 583 chemicals using the yeast two-hybrid assay, Data in Brief (2018), https://doi.org/10.1016/j. dib.2018.11.071i

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109 2. Experimental design, materials, and methods 110 111 hERα, medERα, CAR, and AhR agonist activities and hERα and AR antagonist activities of the 583 112 test chemicals were measured with a yeast two-hybrid assay system. Introduced into each yeast cells 113 (Saccharomyces cerevisiae Y190) were the human estrogen receptor (hERα), Japanese medaka 114 estrogen receptor (medERα), human constitutive androstane receptor (CAR), and human aryl 115 hydrocarbon receptor (AhR) and the coactivator TIF2, in accordance with the method of Nishikawa 116 et al. (1999). Expression plasmids for the hormone receptor ligand binding domain and pGAAD24-TIF117 2 were introduced into yeast cells that carried the β-galactosidase reporter gene (Nishikawa et al., 118 1999). The assays adopted the chemiluminescent reporter gene (for β-galactosidase) method 119 employing a 96-well culture plate (Shiraishi et al., 2000). Yeast cells were preincubated for 24 h at 120 30 °C with shaking in modified SD medium (lacking tryptophan and leucine, 0.86% dextrose) and the 121 cell density was adjusted to an absorbance of 1.75–1.85 at 595 nm. The medium (60 μl) was placed in 122 the wells of the first row of a black 96-well culture plate for chemiluminescence measurement. Wells 123 in rows 2–8 were charged with a solution of 2% DMSO in the medium (60 μl). A solution of test 124 compound (1 mM in DMSO, 20 μl) was added to the medium (480 μl) and aliquots of this mixture 125 (60 μl) were also added to the wells of the first row of the plate. The test solution was serially diluted 126 from row 1 to 7 (each 2  ) and then the yeast cell suspension (60 μl) was also added to each well 127 (including those in row 8, which served as the blank control). Thus, the first row contained a 10 μΜ 128 solution of the test chemical, the second row a 5 μM solution, and so on. After the addition of the 129 yeast suspension and vortex mixing, the plates were incubated at 30 °C under high humidity for 4 h. A 130 solution (80 μl) for inducing chemiluminescence from released β-galactosidase, consisting of reaction 131 buffer (30 μl) containing GalactLux substrate (AURORA GAL-XE, ICN Biomedicals, Inc., Irvine, CA) and 132 zymolylase 20T solution for enzymatic digestion (50 μl), was added to each well. The plate was 133 incubated at 37 °C for 1 h and then placed in a 96-well plate luminometer (Luminescencer JNR 134 AB2100, Atto Corp., Tokyo, Japan) and a light emission accelerator solution (AURORA GAL-XE 50 μl) 135 was added to each well using the luminometer pump. The chemiluminescence produced by 136 β-galactosidase in each well was measured. 137 Q3 A “positive” result in the antagonist activity test was judged to have occurred when the maximum 138 suppression of the chemiluminescence of β-galactosidase activity toward E2 was more than 40% 139 lower than that for the solvent control and when dose dependence was observed over at least three 140 consecutive points. For all substances judged to be positive, the corresponding IC50 was calculated. 141 The quality control of the ER- and AR-antagonism tests was performed by defining the concentration 142 range of IC50 in the positive control and retesting if results outside that range were obtained. Each 143 positive control was 17β-estradiol (The highest concentration in test well medium was 4 nM, and 144 7 stages were set with double dilution. The following values are same.): hER-, medER-agonistic), 145 β-naphthoflavone (10 nM: AhR-agonistic, with 600–2000 pM of E2), 4-hydroxy-tamoxygen (50 nM: 146 hER-antagonistic, with 20 nM of hydroxyltestosterone), and 1-nitropyrene (50 nM: AR-antagonistic). 147 The allowable range was as follows: ER-antagonist test, IC50 of 4-hydroxy-tamoxygen was 148 1200–1800 nM; AhR-antagonist test, IC50 of 1-nitropyrene was 100–500 nM. The YTOX test was also 149 conducted separately to clarify that the decrease in luminescence was due not to toxicity of the test 150 chemicals to the yeast but to antagonism. 151 152 153 Q4 Uncited references 154 155 [4–7]. 156 157 158 Acknowledgments 159 160 This research was supported by the Environment Research and Technology Development Fund 161 (5-1552) of the Ministry of Environment, Japan. We thank Ms. Miho Yamasaki for her skillful technical 162 Q5 assistance. The authors would like to acknowledge Prof. Jun-ichi Nishikawa for providing the culture Please cite this article as: F. Shiraishi, et al., Screening data for the endocrine disrupting activities of 583 chemicals using the yeast two-hybrid assay, Data in Brief (2018), https://doi.org/10.1016/j. dib.2018.11.071i

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of yeast used in the two-hybrid assay. We also thank Dr. Kunimitsu Kaya for his helpful advice and comments.

Transparency document. Supporting information Transparency data associated with this article can be found in the online version at https://doi.org/ 10.1016/j.dib.2018.11.071.

Appendix A. Supplementary material Supplementary data associated with this article can be found in the online version at https://doi. org/10.1016/j.dib.2018.11.071.

References [1] J. Nishikawa, K. Saito, J. Goto, F. Dakeyama, M. Matsuo, T. Nishihara, New screening methods for chemicals with hormonal activities using interaction of nuclear hormone receptor with coactivator, Toxicol. Appl. Pharm. 154 (1999) 76–83. [2] R. Kamata, F. Shiraishi, J. Nishikawa, J. Yonemoto, H. Shiraishi, Screening and detection of the in vitro agonistic activity of xenobiotics on the retinoic acid receptor, Toxicol. Vitr. 22 (2008) 1050–1061. [3] R. Kamata, D. Nakajima, F. Shiraishi, Agonistic effects of diverse xenobiotics on the constitutive androstane receptor as detected in a recombinant yeast-cell assay, Toxicol. Vitr. 46 (2018) 335–349. [4] T. Nishihara, J. Nishikawa, T. Kanayama, F. Dakeyama, K. Saito, M. Imagawa, S. Takatori, Y. Kitagawa, S. Hori, H. Utsumi, Estrogenic activities of 517 chemicals by yeast two-hybrid assay, J. Health Sci. 46 (2000) 282–298. [5] H. Fukazawa, M. Watanabe, F. Shiraishi, H. Shiraishi, T. Shiozawa, H. Matsushita, Y. Terao, Formation of chlorinated derivatives of bisphenol A in waste paper recycling plants and their estrogenic activities, J. Health Sci. 48 (2002) 242–249. [6] M. Terasaki, F. Shiraishi, T. Nishikawa, J.S. Edmonds, M. Morita, M. Makino, Estrogenic activity of impurities in industrial grade bisphenol A, Environ. Sci. Technol. 39 (2005) 3703–3707. [7] H. Nakamura, T. Shiozawa, Y. Terao, F. Shiraishi, H. Fukazawa, By-products produced by the reaction of estrogens with hypochlorous acid and their estrogen activities, J. Health Sci. 52 (2006) 124–131.

Please cite this article as: F. Shiraishi, et al., Screening data for the endocrine disrupting activities of 583 chemicals using the yeast two-hybrid assay, Data in Brief (2018), https://doi.org/10.1016/j. dib.2018.11.071i