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  • 1.
    Asnake, Solomon
    et al.
    Örebro University, School of Science and Technology.
    Pradhan, Ajay
    Örebro University, School of Science and Technology.
    Banjop-Kharlyngdoh, Joubert
    Örebro University, School of Science and Technology.
    Modig, Carina
    Örebro University, School of Science and Technology.
    Olsson, Per-Erik
    Örebro University, School of Science and Technology.
    1,2-dibromo-4-(1,2 dibromoethyl) cyclohexane (TBECH)-mediated steroid hormone receptor activation and gene regulation in chicken LMH cells2014In: Environmental Toxicology and Chemistry, ISSN 0730-7268, E-ISSN 1552-8618, Vol. 33, no 4, p. 891-899Article in journal (Refereed)
    Abstract [en]

    The incorporation of brominated flame retardants into industrial and household appliances has increased their occurrence in the environment, resulting in deleterious effects on wildlife. With the increasing restraints on available compounds, there has been a shift to using brominated flame retardants that has seen the production of alternative brominated flame retardants such as 1,2-dibromo-4-(1,2 dibromoethyl) cyclohexane (TBECH), which has been detected in the environment. In previous in silico and in vitro studies the authors have shown that TBECH can activate both the human androgen receptor (hAR) and the zebrafish AR (zAR) suggesting that it is a potential endocrine disruptor. The present study was aimed at determining the interaction of TBECH with the chicken AR (cAR). In the present study, TBECH bound to cAR, but in vitro activation assay studies using the chicken LMH cell line showed it had a potency of only 15% compared with testosterone. Sequence difference between ARs from different species may contribute to the different responses to TBECH. Further quantitative reverse-transcriptase polymerase chain reaction (qRT-PCR) analysis showed that TBECH interacted with and altered the expression of both thyroid receptors and estrogen receptors. In addition, the qRT-PCR analysis showed that TBECH altered the transcription pattern of genes involved in inflammatory, apoptotic, proliferative, DNA methylation, and drug-metabolizing pathways. This demonstrates that TBECH, apart from activating cAR, can also influence multiple biological pathways in the chicken.

  • 2.
    Asnake, Solomon
    et al.
    Örebro University, School of Science and Technology.
    Pradhan, Ajay
    Biology, The Life Science Center, School of Science and Technology, Örebro University, Örebro, Sweden.
    Kharlyngdoh, Joubert Banjop
    Örebro University, School of Science and Technology.
    Modig, Carina
    Örebro University, School of Science and Technology.
    Olsson, Per-Erik
    Örebro University, School of Science and Technology.
    The brominated flame retardants TBP-AE and TBP-DBPE antagonize the chicken androgen receptor and act as potential endocrine disrupters in chicken LMH cells2015In: Toxicology in Vitro, ISSN 0887-2333, E-ISSN 1879-3177, Vol. 29, no 8, p. 1993-2000Article in journal (Refereed)
    Abstract [en]

    Increased exposure of birds to endocrine disrupting compounds has resulted in developmental and reproductive dysfunctions. We have recently identified the flame retardants, ally1-2,4,6-tribromophenyl ether (TBP-AE), 2-3-dibromopropy1-2,4,6-tribromophenyl ether (TBP-DBPE) and the TBP-DBPE metabolite 2-bromoallyI-2,4,6-tribromophenyl ether (TBP-BAE) as antagonists to both the human androgen receptor (AR) and the zebrafish AR. In the present study, we aimed at determining whether these compounds also interact with the chicken AR. In silico modeling studies showed that TBP-AE, TBP-BAE and TBP-DBPE were able to dock into to the chicken AR ligand-binding pocket. In vitro transfection assays revealed that all three brominated compounds acted as chicken AR antagonists, inhibiting testosterone induced AR activation. In addition, qRT-PCR studies confirmed that they act as AR antagonists and demonstrated that they also alter gene expression patterns of apoptotic, anti-apoptotic, drug metabolizing and amino acid transporter genes. These studies, using chicken LMH cells, suggest that TBP-AE, TBP-BAE and TBP-DBPE are potential endocrine disrupters in chicken.

  • 3.
    Carvalho, Raquel N.
    et al.
    Institute for Environment and Sustainability, European Commission-DG Joint Research Centre, Ispra, Italy.
    Arukwe, Augustine
    Norwegian University of Science & Technology, Trondheim, Norway.
    Ait-Aissa, Selim
    National Institute for Industrial Environment and Risks, Verneuil en Halatte, France.
    Bado-Nilles, Anne
    National Institute for Industrial Environment and Risks, Verneuil en Halatte, France; Reims University, Reims, France.
    Balzamo, Stefania
    Istituto Superiore per la Protezione e la Ricerca Ambientale (ISPRA), Rome, Italy.
    Baun, Anders
    Department of Environmental Engineering,Technical University of Denmark, Kgs Lyngby, Denmark.
    Belkin, Shimshon
    Institute of Life Sciences, The Hebrew University, Jerusalem, Israel.
    Blaha, Ludek
    Faculty of Science, RECETOX, Masaryk University, Brno, Czech Republic.
    Brion, Francois
    National Institute for Industrial Environment and Risks, Verneuil en Halatte, France.
    Conti, Daniela
    Istituto Superiore per la Protezione e la Ricerca Ambientale (ISPRA), Rome, Italy.
    Creusot, Nicolas
    National Institute for Industrial Environment and Risks, Verneuil en Halatte, France.
    Essig, Yona
    Analytical and Environmental Sciences Division, King's College, London, UK.
    Ferrero, Valentina E. V.
    European Commission-DG Joint Research Centre, Institute for Environment and Sustainability, Ispra, Italy.
    Flander-Putrle, Vesna
    Marine Biology Station Piran, National Institute of Biology, Ljubljana, Slovenia.
    Furhacker, Maria
    University of Natural Resources and Life Sciences, Vienna, Austria.
    Grillari-Voglauer, Regina
    University of Natural Resources and Life Sciences, Vienna, Austria.
    Hogstrand, Christer
    Diabetes and Nutritional Sciences Division, King's College London, London, UK.
    Jonas, Adam
    Faculty of Science, RECETOX, Masaryk University, Brno, Czech Republic.
    Kharlyngdoh, Joubert B.
    Örebro University, School of Science and Technology.
    Loos, Robert
    European Commission-DG Joint Research Centre, Institute for Environment and Sustainability, Ispra, Italy.
    Lundebye, Anne-Katrine
    National Institute of Nutrition and Seafood Research, Bergen, Norway.
    Modig, Carina
    Örebro University, School of Science and Technology. Life Science Center, Örebro University, Örebro, Sweden.
    Olsson, Per-Erik
    Örebro University, School of Science and Technology. Life Science Center, Örebro University, Örebro, Sweden.
    Pillai, Smitha
    University of Natural Resources and Life Sciences, Vienna, Austria.
    Polak, Natasa
    Analytical and Environmental Sciences Division, King's College, London, UK.
    Potalivo, Monica
    Istituto Superiore per la Protezione e la Ricerca Ambientale (ISPRA), Rome, Italy.
    Sanchez, Wilfried
    National Institute for Industrial Environment and Risks, Verneuil en Halatte, France.
    Schifferli, Andrea
    Swiss Centre for Applied Ecotoxicology, Eawag-EPFL, Dübendorf, Switzerland.
    Schirmer, Kristin
    Swiss Centre for Applied Ecotoxicology, Eawag-EPFL, Dübendorf, Switzerland.
    Sforzini, Susanna
    Department of Environmental and Life Sciences, Universita del Piemonte Orientale Vercelli Novara Alessandria, Alessandria, Italy.
    Sturzenbaum, Stephen R.
    Analytical and Environmental Sciences Division, King's College, London, UK.
    Søfteland, Liv
    National Institute of Nutrition and Seafood Research, Bergen, Norway.
    Turk, Valentina
    Marine Biology Station Piran, National Institute of Biology, Ljubljana, Slovenia.
    Viarengo, Aldo
    Department of Environmental and Life Sciences, Università del Piemonte Orientale Vercelli Novara Alessandria, Alessandria, Italy.
    Werner, Inge
    Swiss Centre for Applied Ecotoxicology, Swiss Federal Institute of Aquatic Science and Technology ( Eawag-EPFL), Dübendorf, Switzerland.
    Yagur-Kroll, Sharon
    Institute of Life Sciences, The Hebrew University, Jerusalem, Israel.
    Zounkova, Radka
    Faculty of Science, RECETOX, Masaryk University, Brno, Czech Republic.
    Lettieri, Teresa
    European Commission-DG Joint Research Centre, Institute for Environment and Sustainability, Rome, Italy.
    Mixtures of chemical pollutants at European legislation safety concentrations: how safe are they?2014In: Toxicological Sciences, ISSN 1096-6080, E-ISSN 1096-0929, Vol. 141, no 1, p. 218-233Article in journal (Refereed)
    Abstract [en]

    The risk posed by complex chemical mixtures in the environment to wildlife and humans is increasingly debated, but has been rarely tested under environmentally relevant scenarios. To address this issue, two mixtures of 14 or 19 substances of concern (pesticides, pharmaceuticals, heavy metals, polyaromatic hydrocarbons, a surfactant, and a plasticizer), each present at its safety limit concentration imposed by the European legislation, were prepared and tested for their toxic effects. The effects of the mixtures were assessed in 35 bioassays, based on 11 organisms representing different trophic levels. A consortium of 16 laboratories was involved in performing the bioassays. The mixtures elicited quantifiable toxic effects on some of the test systems employed, including i) changes in marine microbial composition, ii) microalgae toxicity, iii) immobilization in the crustacean Daphnia magna, iv) fish embryo toxicity, v) impaired frog embryo development, and vi) increased expression on oxidative stress-linked reporter genes. Estrogenic activity close to regulatory safety limit concentrations was uncovered by receptor-binding assays. The results highlight the need of precautionary actions on the assessment of chemical mixtures even in cases where individual toxicants are present at seemingly harmless concentrations.

  • 4.
    Kling, Peter
    et al.
    University of Gothenburg , Göteborg, Sweden.
    Modig, Carina
    Örebro University, School of Science and Technology.
    Mujahed, Huthayfa
    Örebro University, School of Science and Technology.
    Khalaf, Hazem
    Örebro University, School of Science and Technology.
    von Hofsten, Jonas
    Umeå University, Umeå, Sweden.
    Olsson, Per-Erik
    Örebro University, School of Science and Technology.
    Differential regulation of the rainbow trout (Oncorhynchus mykiss) MT-A gene by nuclear factor interleukin-6 and activator protein-12013In: BMC Molecular Biology, ISSN 1471-2199, E-ISSN 1471-2199, Vol. 14, no 1, p. 28-Article in journal (Refereed)
    Abstract [en]

    BACKGROUND: Previously we have identified a distal region of the rainbow trout (Oncorhynchus mykiss) metallothionein-A (rtMT-A) enhancer region, being essential for free radical activation of the rtMT-A gene. The distal promoter region included four activator protein 1 (AP1) cis-acting elements and a single nuclear factor interleukin-6 (NF-IL6) element. In the present study we used the rainbow trout hepatoma (RTH-149) cell line to further examine the involvement of NF-IL6 and AP1 in rtMT-A gene expression following exposure to oxidative stress and tumour promotion.

    RESULTS: Using enhancer deletion studies we observed strong paraquat (PQ)-induced rtMT-A activation via NF-IL6 while the AP1 cis-elements showed a weak but significant activation. In contrast to mammals the metal responsive elements were not activated by oxidative stress. Electrophoretic mobility shift assay (EMSA) mutation analysis revealed that the two most proximal AP1 elements, AP11,2, exhibited strong binding to the AP1 consensus sequence, while the more distal AP1 elements, AP13,4 were ineffective. Phorbol-12-myristate-13-acetate (PMA), a known tumor promoter, resulted in a robust induction of rtMT-A via the AP1 elements alone. To determine the conservation of regulatory functions we transfected human HepG2 cells with the rtMT-A enhancer constructs and were able to demonstrate that the cis-elements were functionally conserved. The importance of NF-IL6 in regulation of teleost MT is supported by the conservation of these elements in MT genes from different teleosts. In addition, PMA and PQ injection of rainbow trout resulted in increased hepatic rtMT-A mRNA levels.

    CONCLUSIONS: These studies suggest that AP1 primarily is involved in PMA regulation of the rtMT-A gene while NF-IL6 is involved in free radical regulation. Taken together this study demonstrates the functionality of the NF-IL6 and AP-1 elements and suggests an involvement of MT in protection during pathological processes such as inflammation and cancer.

  • 5.
    Modig, Carina
    et al.
    Örebro University, Department of Natural Sciences.
    Modesto, Teresa
    Canario, Adelino
    Cerdà, Joan
    von Hofsten, Jonas
    Olsson, Per-Erik
    Örebro University, Department of Natural Sciences.
    Molecular characterization and expression pattern of zona pellucida proteins in gilthead seabream (Sparus aurata)2006In: Biology of Reproduction, ISSN 0006-3363, E-ISSN 1529-7268, Vol. 75, no 5, p. 717-725Article in journal (Refereed)
    Abstract [en]

    The developing oocyte is surrounded by an acellular envelope that is composed of 2-4 isoforms of zona pellucida (ZP) proteins. The ZP proteins comprise the ZP1, ZP2, ZP3, and ZPX isoforms. While ZP1 (ZPB) and ZP3 (ZPC) are present in all species, ZP2 (ZPA) is not found in teleost fish and ZPX is not found in mammals. In the present study, we identify and characterize the ZP1, ZP3 and ZPX isoforms of gilthead seabream. Furthermore, by analyzing the conserved domains, which include the external hydrophobic patch and the internal hydrophobic patch, we show that ZP2 and ZPX are closely related isoforms. ZP proteins are synthesized in either the liver or ovary of most teleosts. Only in rainbow trout has it been shown that zp3 has dual transcription sites. In gilthead seabream, all four mRNA isoforms are transcribed in both the liver and ovary, with zp1a, zp1b, and zp3 being highly expressed in the liver, and zpx being primarily expressed in the ovary. However, determination of the ZP proteins in plasma showed high levels of ZP1b, ZP3, and ZPX, with low or non-detectable levels of ZP1a. In similarity to other teleost ZPs, the hepatic transcription of all four ZP isoforms is under estrogenic control. Previously, we have shown that cortisol can potentiate estrogen-induced ZP synthesis in salmonids, and now we show that this is not the case in the gilthead seabream. The present study shows for the first time the endocrine regulation of a teleost ZPX isoform, and demonstrates the dual-organ transcriptional activities of all the ZP proteins in one species.

  • 6.
    Modig, Carina
    et al.
    Örebro University, School of Science and Technology.
    Raldúa, Demetrio
    Cerdà, Joan
    Olsson, Per-Erik
    Örebro University, School of Science and Technology.
    Analysis of vitelline envelope synthesis and composition during early oocyte development in gilthead seabream (Sparus aurata)2008In: Molecular Reproduction and Development, ISSN 1040-452X, E-ISSN 1098-2795, Vol. 75, no 8, p. 1351-1360Article in journal (Refereed)
    Abstract [en]

    The oocyte vitelline envelope (VE) of gilthead seabream is composed of four known zona pellucida (ZP) proteins, ZPBa, ZPBb, ZPC, and ZPX. We have previously shown that the gilthead seabream ZP proteins are differentially transcribed in liver and ovary, with the expression in liver being under estrogenic control. However, although mRNA was found in both liver and ovary, only low ZPBa protein levels were detected in liver and plasma. Using isoform-specific ZP antibodies we show that ZPBa and ZPX translation products are present in the cytosol of stage I and II oocytes. In addition, the zpBa and zpX mRNAs were detected in early developing oocytes. During oocyte growth (vitellogenesis), the VE increased in thickness (>10 µm), and we show that the four ZP isoforms are present in different regions of the VE. ZPX was detected closest to the oocyte plasma membrane while the intermediate region was composed of ZPBa, ZPBb, and ZPC. At the outer layer, only ZPC was detected. When oocytes reach the fully grown stage they resume meiosis and hydration. As the oocyte expands, thinning to 4 µm, the VE acquire a striped and compact appearance at the electron microscopy level. This study provides further evidence for the oocyte origin of some ZP proteins in the gilthead seabream and suggests that the ZP proteins are differentially distributed within the VE. Mol. Reprod. Dev. 75: 1351-1360, 2008.

  • 7.
    Olsson, Per-Erik
    et al.
    Örebro University, Department of Natural Sciences.
    Berg, A. Håkan
    von Hofsten, Jonas
    Grahn, Birgitta
    Hellqvist, Anna
    Larsson, Anders
    Örebro University, Department of Natural Sciences.
    Karlsson, Johnny
    Örebro University, Department of Natural Sciences.
    Modig, Carina
    Örebro University, Department of Natural Sciences.
    Borg, Bertil
    Thomas, Peter
    Molecular cloning and characterization of a nuclear androgen receptor activated by 11-ketotestosterone2005In: Reproductive biology and endocrinology, ISSN 1477-7827, Vol. 3:37Article in journal (Refereed)
    Abstract [en]

    Although 11-ketotestosterone is a potent androgen and induces male secondary sex characteristics in many teleosts, androgen receptors with high binding affinity for 11-ketotestosterone or preferential activation by 11-ketotestosterone have not been identified. So, the mechanism by which 11-ketotestosterone exhibits such high potency remains unclear. Recently we cloned the cDNA of an 11-ketotestosterone regulated protein, spiggin, from three-spined stickleback renal tissue. As spiggin is the only identified gene product regulated by 11-ketotestosterone, the stickleback kidney is ideal for determination of the mechanism of 11-ketotestosterone gene regulation. A single androgen receptor gene with two splicing variants, belonging to the androgen receptor-beta subfamily was cloned from stickleback kidney. A high affinity, saturable, single class of androgen specific binding sites, with the characteristics of an androgen receptor, was identified in renal cytosolic and nuclear fractions. Measurement of ligand binding moieties in the cytosolic and nuclear fractions as well as to the recombinant receptor revealed lower affinity for 11-ketotestosterone than for dihydrotestosterone. Treatment with different androgens did not up-regulate androgen receptor mRNA level or increase receptor abundance, suggesting that auto-regulation is not involved in differential ligand activation. However, comparison of the trans-activation potential of the stickleback androgen receptor with the human androgen receptor, in both human HepG2 cells and zebrafish ZFL cells, revealed preferential activation by 11-ketotestosterone of the stickleback receptor, but not of the human receptor. These findings demonstrate the presence of a receptor preferentially activated by 11-ketotestosterone in the three-spined stickleback, so far the only one known in any animal.

  • 8.
    Pradhan, Ajay
    et al.
    Örebro University, School of Science and Technology.
    Asnake, Solomon
    Örebro University, School of Science and Technology.
    Kharlyngdoh, Joubert Banjop
    Örebro University, School of Science and Technology.
    Modig, Carina
    Örebro University, School of Science and Technology.
    Olsson, Per-Erik
    Örebro University, School of Science and Technology.
    In silico and biological analysis of anti-androgen activity of the brominated flame retardants ATE, BATE and DPTE in zebrafishManuscript (preprint) (Other academic)
  • 9.
    Pradhan, Ajay
    et al.
    Örebro University, School of Science and Technology.
    Asnake, Solomon
    Örebro University, School of Science and Technology.
    Kharlyngdoh, Joubert Banjop
    Örebro University, School of Science and Technology.
    Modig, Carina
    Örebro University, School of Science and Technology.
    Olsson, Per-Erik
    Örebro University, School of Science and Technology.
    In silico and biological analysis of anti-androgen activity of the brominated flame retardants ATE, BATE and DPTE in zebrafish2015In: Chemico-Biological Interactions, ISSN 0009-2797, E-ISSN 1872-7786, Vol. 233, p. 35-45Article in journal (Refereed)
    Abstract [en]

    The brominated flame retardants (BFRs) 1,2-dibromo-4-(1,2-dibromoethyl)cyclohexane (TBECH or DBE-DCBH) and allyl 2,4,6-tribromophenyl ether (ATE or TBP-AE) are alternative BFRs that have been introduced to replace banned BFRs. TBECH is a potential endocrine disrupter in human, chicken and zebrafish and in a recent study we showed that ATE, along with the structurally similar BFR 2,3-dibromopropyl 2,4,6-tribromophenyl ether (DPTE or TBP-DBPE) and its metabolite 2-bromoallyl 2,4,6-tribromophenyl ether (BATE or TBP-BAE) are potential endocrine and neuronal disrupters in human. In this study we analyzed ATE, BATE and DPTE for zebrafish androgen receptor (zAR) modulating properties. In silico analysis with two softwares, Molecular Operating Environment (MOE) and Internal Coordinate Mechanics (ICM), showed that ATE, BATE and DPTE bind to zAR. In vitro AR activation assay revealed that these three BFRs down-regulate 11-ketotestosterone (KT) mediated zAR activation. Exposure to 10 mu M DPTE resulted in reduced hatching success and like TBECH, BATE and DPTE at 10 mu M also had teratogenic properties with 20% and 50% back-bone curvature respectively. Gene transcription analysis in zebrafish embryos as well as in juveniles showed down-regulation of the androgen receptor and androgen response genes, which further support that these BFRs are androgen antagonists and potential endocrine disrupting compounds. Genes involved in steroidogenesis were also down-regulated by these BFRs. In view of this, the impact of these BFRs on humans and wildlife needs further analysis.

  • 10. von Hofsten, J.
    et al.
    Modig, Carina
    Örebro University, Department of Natural Sciences.
    Larsson, A.
    Örebro University, Department of Natural Sciences.
    Karlsson, J.
    Örebro University, Department of Natural Sciences.
    Olsson, Per-Erik
    Örebro University, Department of Natural Sciences.
    Determination of the expression pattern of the dual promoter of zebrafish fushi tarazu factor-1a following microinjections into zebrafish one cell stage embryos2005In: General and Comparative Endocrinology, ISSN 0016-6480, E-ISSN 1095-6840, Vol. 142, no 1-2, p. 222-226Article in journal (Refereed)
    Abstract [en]

    The zebrafish fushi tarazu factor-1a (ff1a) is a transcription factor belonging to the NR5A subgroup of nuclear receptors. The NR5A receptors bind DNA as monomers and are considered to be orphans due to their ability to promote transcription of downstream genes without ligands. In zebrafish, four ff1 homologues (Ff1a, Ff1b, Ff1c, and Ff1d) have been identified so far. The gene coding for Ff1a is driven by two separate promoters, and give rise to four splice variants. Ff1a is expressed in the somites and pronephric ducts during somitogenesis and in the brain, liver, and mandibular arch during later embryonic stages. In adults the gene is highly expressed in gonads, liver, and intestine, but can be detected in most tissues. The broad variety of embryonic expression domains indicates several important developmental features. One of the mammalian fushi tarazu factor-1 genes, steroidogenic factor-1 (SF-1), is essential for the development of gonads and adrenals. SF-1 is together with Sox9, WT1, and GATA4 a positive transcriptional regulator of human anti-mullerian hormone (AMH) and thereby linked to the male sex-determining pathway. The zebrafish ff1a dual promoter contains several GATA binding sites and E-boxes, a site for DR4, XFD2, MyoD, Snail, HNF3, S8, and an HMG-box recognition site for Sox9. In a first attempt to dissect the ff1a promoter in vivo we have produced first generation transgenes in order to determine the correlation between the expression of the endogenous ff1a gene and the microinjected ff1a dual promoter coupled to the pEGFP reporter vector. Our results show that the microinjected constructs are expressed in the correct tissues.

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