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      Transcriptional Changes Caused by Bisphenol A in Oryzias javanicus, a Fish Species Highly Adaptable to Environmental Salinity

      research-article
      1 , 2 , 1 , *
      Marine Drugs
      MDPI
      Oryzias javanicus, cDNA microarray, bisphenol A, gene expression, salinity

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          Abstract

          The Javanese medaka, Oryzias javanicus, is a fish highly adaptable to various environmental salinities. Here, we investigated the effects of the environmental pollutant bisphenol A (BPA; an endocrine disrupting chemical) on gene expression levels in this species acclimated to different salinities. Using cDNA microarrays, we detected the induction of differential expression of genes by BPA, and compared the transcriptional changes caused by chemical exposure at different salinities. There were marked transcriptional changes induced by BPA between treatments. While 533 genes were induced by a factor of more than two when O. javanicus was exposed to BPA in seawater, only 215 genes were induced in freshwater. Among those genes, only 78 were shared and changed significantly their expression in both seawater and freshwater. Those genes were mainly involved in cellular processes and signaling pathway. We then categorized by functional group genes specifically induced by BPA exposure in seawater or freshwater. Gene expression changes were further confirmed in O. javanicus exposed to various concentrations of BPA, using quantitative real-time reverse transcription PCR based on primer sets for 28 selected genes.

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          Most cited references39

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          Interaction of the small interstitial proteoglycans biglycan, decorin and fibromodulin with transforming growth factor beta.

          We have analysed the interactions of three proteoglycans of the decorin family, decorin, biglycan and fibromodulin, with transforming growth factor beta (TGF-beta). The proteoglycan core proteins, expressed from human cDNAs as fusion proteins with Escherichia coli maltose-binding protein, each bound TGF-beta 1. They showed only negligible binding to several other growth factors. Intact decorin, biglycan and fibromodulin isolated from bovine tissues competed with the fusion proteins for the TGF-beta binding. Affinity measurements suggest a two-site binding model with Kd values ranging from 1 to 20 nM for a high-affinity binding site and 50 to 200 nM for the lower-affinity binding site. The stoichiometry indicated that the high-affinity binding site was present in one of ten proteoglycan core molecules and that each molecule contained a low-affinity binding site. Tissue-derived biglycan and decorin were less effective competitors for TGF-beta binding than fibromodulin or the non-glycosylated fusion proteins; removal of the chondroitin/dermatan sulphate chains of decorin and biglycan (fibromodulin is a keratan sulphate proteoglycan) increased the activities of decorin and biglycan, suggesting that the glycosaminoglycan chains may hinder the interaction of the core proteins with TGF-beta. The fusion proteins competed for the binding of radiolabelled TGF-beta to Mv 1 Lu cells and endothelial cells. Affinity labelling showed that the binding of TGF-beta to betaglycan and the type-I receptors in Mv 1 Lu cells and to endoglin in endothelial cells was reduced, but the binding to the type-II receptors was unaffected. TGF-beta 2 and 3 also bound to all three fusion proteins. Latent recombinant TGF-beta 1 precursor bound slightly to fibromodulin and not at all to decorin and biglycan. The results show that the three decorin-type proteoglycans each bind TGF-beta isoforms and that slight differences exist in their binding properties. They may regulate TGF-beta activities by sequestering TGF-beta into extracellular matrix.
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            A model for measurement error for gene expression arrays.

            We introduce a model for measurement error in gene expression arrays as a function of the expression level. This model, together with analysis methods, data transformations, and weighting, allows much more precise comparisons of gene expression, and provides guidance for analysis of background, determination of confidence intervals, and preprocessing data for multivariate analysis.
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              New modes of action for endocrine-disrupting chemicals.

              Endocrine-disrupting chemicals (EDC) are commonly considered to be compounds that mimic or block the transcriptional activation elicited by naturally circulating steroid hormones by binding to steroid hormone receptors. For example, the Food Quality Protection Act of 1996 defines EDC as those, that "may have an effect in humans that is similar to an effect produced by a naturally occurring estrogen, or other such endocrine effect as the Administrator may designate." The definition of EDC was later expanded to include those that act on the estrogen, androgen, and thyroid hormone receptors. In this minireview, we discuss new avenues through which xenobiotic chemicals influence these and other hormone-dependent signaling pathways. EDC can increase or block the metabolism of naturally occurring steroid hormones and other xenobiotic chemicals by activating or antagonizing nuclear hormone receptors. EDC affect the transcriptional activity of nuclear receptors by modulating proteasome-mediated degradation of nuclear receptors and their coregulators. Xenobiotics and environmental contaminants can act as hormone sensitizers by inhibiting histone deacetylase activity and stimulating mitogen-activated protein kinase activity. Some endocrine disrupters can have genome-wide effects on DNA methylation status. Others can modulate lipid metabolism and adipogenesis, perhaps contributing to the current epidemic of obesity. Additional elucidation of these new modes of endocrine disruption will be key in understanding the nature of xenobiotic effects on the endocrine system.
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                Author and article information

                Journal
                Mar Drugs
                Mar Drugs
                marinedrugs
                Marine Drugs
                MDPI
                1660-3397
                14 February 2014
                February 2014
                : 12
                : 2
                : 983-998
                Affiliations
                [1 ]South Sea Environment Research Division, Korea Institute of Ocean Science and Technology, Geoje 656-830, Korea; E-Mail: cwoo@ 123456kiost.ac
                [2 ]Biodiversity Research Centre, Academia Sinica, Taipei 115, Taiwan; E-Mail: vianney.denis@ 123456gmail.com
                Author notes
                [†]

                These authors contributed equally to this work.

                [* ]Author to whom correspondence should be addressed; E-Mail: syum@ 123456kiost.ac ; Tel.: +82-55-639-8540; Fax: +82-55-639-8509.
                Article
                marinedrugs-12-00983
                10.3390/md12020983
                3944526
                24534842
                fa81af4c-6674-4ea9-92d5-7fe8aeee1742
                © 2014 by the authors; licensee MDPI, Basel, Switzerland.

                This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license ( http://creativecommons.org/licenses/by/3.0/).

                History
                : 10 December 2013
                : 06 January 2014
                : 06 February 2014
                Categories
                Article

                Pharmacology & Pharmaceutical medicine
                oryzias javanicus,cdna microarray,bisphenol a,gene expression,salinity

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