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  • 1
    Electronic Resource
    Electronic Resource
    Studies on the Role of the Ah Receptor in Hexachlorobenzene-Induced Porphyria (1987)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 514 (1987), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1987.tb48791.x
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  • 2
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    Development and characterization of polyclonal antibodies against the aryl hydrocarbon receptor protein family (AHR1, AHR2, and AHR repressor) of Atlantic killifish Fundulus heteroclitus (2006)
    Details
    Publication Date: 2022-05-25
    Description: Author Posting. © The Authors, 2005. This is the author's version of the work. It is posted here by permission of Elsevier B. V. for personal use, not for redistribution. The definitive version was published in Comparative Biochemistry and Physiology Part C: Toxicology & Pharmacology 142 (2006): 85-94, doi:10.1016/j.cbpc.2005.10.013.
    Description: The aryl hydrocarbon receptor (AHR) and AHR repressor (AHRR) proteins regulate gene expression in response to some halogenated aromatic hydrocarbons and polycyclic aromatic hydrocarbons. The Atlantic killifish is a valuable model of the AHR signaling pathway, but antibodies are not available to fully characterize AHR and AHRR proteins. Using bacterially expressed AHRs, we developed specific and sensitive polyclonal antisera against the killifish AHR1, AHR2, and AHRR. In immunoblots, these antibodies recognized full-length killifish AHR and AHRR proteins synthesized in rabbit reticulocyte lysate, proteins expressed in mammalian cells transfected with killifish AHR and AHRR constructs, and AHR proteins in cytosol preparations from killifish tissues. Killifish AHR1 and AHR2 proteins were detected in brain, gill, kidney, heart, liver, and spleen. Antisera specifically precipitated their respective target proteins in immunoprecipitation experiments with in vitro-expressed proteins. Killifish ARNT2 co-precipitated with AHR1 and AHR2. These sensitive, specific, and versatile antibodies will be valuable to researchers investigating AHR signaling and other physiological processes involving AHR and AHRR proteins.
    Description: Funding for this research was provided by National Institutes of Health, National Research Service Award (F32 ES05935) from the National Institute of Environmental Health Sciences (RRM), NIEHS Superfund Basic Research Program Grant P42 ES007381 at Boston University (MEH), and the Oliver S. and Jennie R. Donaldson Charitable Trust (MEH and RRM).
    Keywords: Aryl hydrocarbon receptor (AHR) ; AHR repressor (AHRR) ; Basic helix-loop-helix Per-ARNT-Sim (bHLH-PAS) ; Fish ; Halogenated aromatic hydrocarbons (HAH); ; Polynuclear aromatic hydrocarbons (PAH) ; Recombinant protein ; Teleost
    Repository Name: Woods Hole Open Access Server
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  • 3
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    Development of the morpholino gene knockdown technique in Fundulus heteroclitus : a tool for studying molecular mechanisms in an established environmental model (2008)
    Details
    Publication Date: 2022-05-25
    Description: Author Posting. © Elsevier B.V., 2008. This is the author's version of the work. It is posted here by permission of Elsevier B.V. for personal use, not for redistribution. The definitive version was published in Aquatic Toxicology 87 (2008): 289-295, doi:10.1016/j.aquatox.2008.02.010.
    Description: A significant challenge in environmental toxicology is that many genetic and genomic tools available in laboratory models are not developed for commonly used environmental models. The Atlantic killifish (Fundulus heteroclitus) is one of the most studied teleost environmental models, yet few genetic or genomic tools have been developed for use in this species. The advancement of genetic and evolutionary toxicology will require that many of the tools developed in laboratory models be transferred into species more applicable to environmental toxicology. Antisense morpholino oligonucleotide (MO) gene knockdown technology has been widely utilized to study development in zebrafish and has been proven to be a powerful tool in toxicological investigations through direct manipulation of molecular pathways. To expand the utility of killifish as an environmental model, MO gene knockdown technology was adapted for use in Fundulus. Morpholino microinjection methods were altered to overcome the significant differences between these two species. Morpholino efficacy and functional duration were evaluated with molecular and phenotypic methods. A cytochrome P450-1A (CYP1A) MO was used to confirm effectiveness of the methodology. For CYP1A MO-injected embryos, a 70% reduction in CYP1A activity, a 86% reduction in total CYP1A protein, a significant increase in β-naphthoflavone-induced teratogenicity, and estimates of functional duration (50% reduction in activity 10 dpf, and 86% reduction in total protein 12 dpf) conclusively demonstrated that MO technologies can be used effectively in killifish and will likely be just as informative as they have been in zebrafish.
    Description: This work was funded in part by the National Institute of Environmental Health Sciences through the Duke Superfund Basic Research Center (P42ES010356), the Boston University Superfund Basic Research Program (P42ES007381), and the Duke Integrated Toxicology and Environmental Health Program (ES-T32-0007031). Additional support was provided by a U.S. Environmental Protection Agency STAR fellowship awarded to C.R.F.
    Keywords: Fundulus heteroclitus ; Antisense morpholino oligonucleotide ; CYP1A ; Atlantic killifish ; Genetic toxicology ; Development ; Teratogenesis
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  • 4
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    Proteomic identification, cDNA cloning and enzymatic activity of glutathione S-transferases from the generalist marine gastropod, Cyphoma gibbosum (2008)
    Details
    Publication Date: 2022-05-25
    Description: Author Posting. © Elsevier B.V., 2008. This is the author's version of the work. It is posted here by permission of Elsevier B.V. for personal use, not for redistribution. The definitive version was published in Archives of Biochemistry and Biophysics 478 (2008): 7-17, doi:10.1016/j.abb.2008.07.007.
    Description: Glutathione S-transferases (GST) were characterized from the digestive gland of Cyphoma gibbosum (Mollusca; Gastropoda), to investigate the possible role of these detoxification enzymes in conferring resistance to allelochemicals present in its gorgonian coral diet. We identified the collection of expressed cytosolic Cyphoma GST classes using a proteomic approach involving affinity chromatography, HPLC and nanospray liquid chromatography-tandem mass spectrometry (LC-MS/MS). Two major GST subunits were identified as putative mu-class GSTs; while one minor GST subunit was identified as a putative theta-class GST, apparently the first theta-class GST identified from a mollusc. Two Cyphoma GST cDNAs (CgGSTM1 and CgGSTM2) were isolated by RT-PCR using primers derived from peptide sequences. Phylogenetic analyses established both cDNAs as mu-class GSTs and revealed a mollusc-specific subclass of the GST-mu clade. These results provide new insights into metazoan GST diversity and the biochemical mechanisms used by marine organisms to cope with their chemically defended prey.
    Description: Support was provided by the WHOI-Cole Ocean Ventures Fund (KEW), the WHOI Ocean Life Institute (KEW and MEH), a grant from Walter A. and Hope Noyes Smith (MEH), the National Science Foundation Graduate Research Fellowship (KEW), and by the National Institutes of Health (P42-ES007381 and R01-ES015912 to JVG).
    Keywords: Cyphoma gibbosum ; Glutathione S-transferase ; Gorgonian ; Natural product ; Chemical ecology ; Allelochemical ; Proteomic
    Repository Name: Woods Hole Open Access Server
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  • 5
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    Regulation of constitutive and inducible AHR signaling : complex interactions involving the AHR repressorstar (2009)
    Details
    Publication Date: 2022-05-25
    Description: Author Posting. © Elsevier B.V., 2009. This is the author's version of the work. It is posted here by permission of Elsevier B.V. for personal use, not for redistribution. The definitive version was published in Biochemical Pharmacology 77(2009): 485-497, doi:10.1016/j.bcp.2008.09.016.
    Description: The AHR is well known for regulating responses to an array of environmental chemicals. A growing body of evidence supports the hypothesis that the AHR also plays perhaps an even more important role in modulating critical aspects of cell function including cell growth, death, and migration. As these and other important AHR activities continue to be elucidated, it becomes apparent that attention now must be directed towards the mechanisms through which the AHR itself is regulated. Here, we review what is known of and what biological outcomes have been attributed to the AHR repressor (AHRR), an evolutionarily conserved bHLH-PAS protein that inhibits both xenobiotic-induced and constitutively active AHR transcriptional activity in multiple species. We discuss the structure and evolution of the AHRR and the dominant paradigm of a xenobiotic-inducible negative feedback loop comprised of AHR-mediated transcriptional up-regulation of AHRR and the subsequent AHRR-mediated suppression of AHR activity. We highlight the role of the AHRR in limiting AHR activity in the absence of xenobiotic AHR ligands and the important contribution of constitutively repressive AHRR to cancer biology. In this context, we also suggest a new hypothesis proposing that, under some circumstances, constitutively active AHR may repress AHRR transcription, resulting in unbridled AHR activity. We also review the predominant hypotheses on the molecular mechanisms through which AHRR inhibits AHR as well as novel mechanisms through which the AHRR may exert AHR-independent effects. Collectively, this discussion emphasizes the importance of this understudied bHLH-PAS protein in tissue development, normal cell biology, xenobiotic responsiveness, and AHR-regulated malignancy.
    Description: Supported by P01-ES11624 (D.H.S.), ArtBeCAUSE (D.H.S.), R01ES006272 (M.E.H.), P42ES007381 (M.E.H. and D.H.S.)
    Keywords: Aryl hydrocarbon receptor ; Aryl hydrocarbon receptor repressor ; PAS proteins ; Cancer ; Toxicology
    Repository Name: Woods Hole Open Access Server
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  • 6
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    Mechanistic research in aquatic toxicology : perspectives and future directions (2011)
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    Publication Date: 2022-05-25
    Description: Author Posting. © The Author(s), 2011. This is the author's version of the work. It is posted here by permission of Elsevier B.V. for personal use, not for redistribution. The definitive version was published in Aquatic Toxicology 105 (2011): 67-71, doi:10.1016/j.aquatox.2011.06.001.
    Description: On the thirtieth anniversary of the journal, I provide a perspective on some of the questions and opportunities for new understanding that will interest aquatic toxicologists during the next thirty years. I focus on mechanisms of toxicity involving transcription factors, signalling pathways, and gene networks involved in toxic and adaptive responses in aquatic animals. Prominent questions address the value of a toxicity pathways approach in aquatic systems, issues involving extrapolation among species, identification of susceptibility genes and useful biomarkers of adverse effect, new emerging contaminants, the importance of epigenetic mechanisms, effects of multiple stressors, evolutionary toxicology, and the relative roles of technical and conceptual limitations to our understanding of chemical effects on aquatic systems.
    Description: I gratefully acknowledge the U.S. National Institutes of Health for support in preparation of this chapter and long-term funding that has allowed my group to conduct research on the comparative biology of AHRs, mechanisms of evolved resistance to PCBs, and (more recently) mechanisms of response to oxidative stress and the role of microRNAs in developmental toxicology [grants R01ES006272, P42ES007381 (Superfund Basic Research Program at Boston University), R01ES016366, and R21ES017304]. I also acknowledge valuable support from the WHOI Sea Grant program with funding from the National Oceanic and Atmospheric Administration for support of research on the role of AHRs in susceptibility of birds and marine mammals to dioxin-like compounds.
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  • 7
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    Species-specific relative ahr1 binding affinities of 2,3,4,7,8-pentachlorodibenzofuran explain avian species differences in its relative potency (2014)
    Details
    Publication Date: 2022-05-25
    Description: Author Posting. © The Author(s), 2013. This is the author's version of the work. It is posted here by permission of Elsevier for personal use, not for redistribution. The definitive version was published in Comparative Biochemistry and Physiology Part C: Toxicology & Pharmacology 161 (2014): 21-25, doi:10.1016/j.cbpc.2013.12.005.
    Description: Results of recent studies showed that 2,3,4,7,8-pentachlorodibenzofuran (PeCDF) and 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD) are equipotent in domestic chicken (Gallus gallus domesticus) while PeCDF is more potent than TCDD in ring-necked pheasant (Phasianus colchicus) and Japanese quail (Coturnix japonica). To elucidate the mechanism(s) underlying these differences in relative potency of PeCDF among avian species, we tested the hypothesis that this is due to species-specific differential binding affinity of PeCDF to the aryl hydrocarbon receptor 1 (AHR1). Here, we modified a cell-based binding assay that allowed us to measure the binding affinity of dioxin-like compounds (DLCs) to avian AHR1 expressed in COS-7 (fibroblast-like cells). The results of the binding assay show that PeCDF and TCDD bind with equal affinity to chicken AHR1, but PeCDF binds with greater affinity than TCDD to pheasant (3-fold) and Japanese quail (5-fold) AHR1. The current report introduces a COS-7 whole-cell binding assay and provides a mechanistic explanation for differential relative potencies of PeCDF among species of birds.
    Description: This research was supported by an unrestricted grant from the Dow Chemical Company to the University of Ottawa, Environment Canada’s Wildlife Toxicology and Disease and STAGE programs and, in part, by a Discovery Grant from the National Science and Engineering Research Council of Canada (Project # 326415-07). The authors wish to acknowledge the support of an instrumentation grant from the Canada Foundation for Infrastructure. Professor Giesy was supported by the Canada Research Chair program and an at large Chair Professorship at the Department of Biology and Chemistry and State Key Laboratory in Marine Pollution, City University of Hong Kong, and the Einstein Professor Program of the Chinese Academy of Sciences. M. Hahn was supported by NOAA Sea Grant (grant number NA06OAR4170021 (R/B-179)).
    Keywords: Aryl hydrocarbon receptor ; Cell-based binding assay ; Dioxin ; COS-7 cells ; Bird ; PeCDF ; TCDD
    Repository Name: Woods Hole Open Access Server
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  • 8
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    The genomic landscape of rapid repeated evolutionary adaptation to toxic pollution in wild fish (2016)
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    Publication Date: 2022-05-25
    Description: Author Posting. © The Author(s), 2016. This is the author's version of the work. It is posted here under a nonexclusive, irrevocable, paid-up, worldwide license granted to WHOI. It is made available for personal use, not for redistribution. The definitive version was published in Science 354 (2016): 1305-1308, doi:10.1126/science.aah4993.
    Description: Atlantic killifish populations have rapidly adapted to normally lethal levels of pollution in four urban estuaries. Through analysis of 384 whole killifish genome sequences and comparative transcriptomics in four pairs of sensitive and tolerant populations, we identify the aryl hydrocarbon receptor-based signaling pathway as a shared target of selection. This suggests evolutionary constraint on adaptive solutions to complex toxicant mixtures at each site. However, distinct molecular variants apparently contribute to adaptive pathway modification among tolerant populations. Selection also targets other toxicity-mediating genes, and genes of connected signaling pathways, indicating complex tolerance phenotypes and potentially compensatory adaptations. Molecular changes are consistent with selection on standing genetic variation. In killifish high nucleotide diversity has likely been a crucial substrate for selective sweeps to propel rapid adaptation.
    Description: Primary support was from the United States National Science Foundation (collaborative research grants DEB-1265282, DEB-1120512, DEB- 1120013, DEB-1120263, DEB-1120333, DEB-1120398 to JKC, DLC, MEH, SIK, MFO, JRS, WW, and AW). Further support was provided by the National Institutes of Environmental Health Sciences (1R01ES021934-01 to AW; P42ES007381 to MEH; R01ES019324 to JRS), and the National Science Foundation (OCE-1314567 to AW). BC was supported by the Postdoctoral Research Program at the US EPA administered by the Oak Ridge Institute for Science and Education (Agreement DW92429801).
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  • 9
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    Sequence and functional characterization of hypoxia inducible factors, HIF1α, HIF2αa, and HIF3α, from the estuarine fish, Fundulus heteroclitus (2017)
    Details
    Publication Date: 2022-05-25
    Description: Author Posting. © The Author(s), 2016. This is the author's version of the work. It is posted here under a nonexclusive, irrevocable, paid-up, worldwide license granted to WHOI. It is made available for personal use, not for redistribution. The definitive version was published in American Journal of Physiology-Regulatory Integrative and Comparative Physiology, 312 (2017): R412-R425, doi:10.1152/ajpregu.00402.2016.
    Description: The hypoxia inducible factor (HIF) family of transcription factors plays central roles in the development, physiology, pathology, and environmental adaptation of animals. Because many aquatic habitats are characterized by episodes of low dissolved oxygen, fish represent ideal models to study the roles of HIF in the response to aquatic hypoxia. The estuarine fish Fundulus heteroclitus occurs in habitats prone to hypoxia, it responds to low oxygen via behavioral, physiological, and molecular changes, and one member of the HIF family, HIF2α, has been previously described. Herein, cDNA sequencing, phylogenetic analyses, and genomic approaches were used to determine other members of the HIFα family from F. heteroclitus and their relationships to HIFα subunits from other vertebrates. In vitro and cellular approaches demonstrated that full-length forms of HIF1α, 2α, and 3α independently formed complexes with the β subunit (ARNT) to bind to hypoxia response elements and activate reporter gene expression. Quantitative PCR showed that HIFα mRNA abundance varied among organs of normoxic fish in an isoform-specific fashion. Analysis of the F. heteroclitus genome revealed a locus encoding a second HIF2α, HIF2αb, a predicted protein lacking oxygen sensing and transactivation domains. Finally, sequence analyses demonstrated polymorphism in the coding sequence of each F. heteroclitus HIFα subunit, suggesting that genetic variation in these transcription factors may play a role in the variation in hypoxia responses among individuals or populations.
    Description: This research was supported in part by the National Science Foundation (IBN-0236494 and DEB-1120263) and by National Institute of Environmental Health Sciences (NIEHS) grant P42ES007381 (Superfund Basic Research Program at Boston University). Data interpretation was aided by reference to a preliminary draft of the F. heteroclitus genome sequence, which was supported by funding from the National Science Foundation (collaborative research grants DEB-1120512, DEB-1265282, DEB-1120013, DEB-1120263, DEB-1120333, DEB-1120398).
    Keywords: Environmental adaptation ; Oxygen ; Gene expression
    Repository Name: Woods Hole Open Access Server
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  • 10
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    The African coelacanth genome provides insights into tetrapod evolution (2013)
    Nature Publishing Group
    Details
    Publication Date: 2022-05-25
    Description: © The Author(s), 2013. This article is distributed under the terms of the Creative Commons Attribution License. The definitive version was published in Nature 496 (2013): 311-316, doi:10.1038/nature12027.
    Description: The discovery of a living coelacanth specimen in 1938 was remarkable, as this lineage of lobe-finned fish was thought to have become extinct 70 million years ago. The modern coelacanth looks remarkably similar to many of its ancient relatives, and its evolutionary proximity to our own fish ancestors provides a glimpse of the fish that first walked on land. Here we report the genome sequence of the African coelacanth, Latimeria chalumnae. Through a phylogenomic analysis, we conclude that the lungfish, and not the coelacanth, is the closest living relative of tetrapods. Coelacanth protein-coding genes are significantly more slowly evolving than those of tetrapods, unlike other genomic features. Analyses of changes in genes and regulatory elements during the vertebrate adaptation to land highlight genes involved in immunity, nitrogen excretion and the development of fins, tail, ear, eye, brain and olfaction. Functional assays of enhancers involved in the fin-to-limb transition and in the emergence of extra-embryonic tissues show the importance of the coelacanth genome as a blueprint for understanding tetrapod evolution.
    Description: cquisition and storage of Latimeria chalumnae samples was supported by grants from the African Coelacanth Ecosystem Programme of the South African National Department of Science and Technology. Generation of the Latimeria chalumnae and Protopterus annectens sequences by the Broad Institute of the Massachusetts Institute of Technology (MIT) and Harvard University was supported by grants from the National Human Genome Research Institute (NHGRI). K.L.T. is the recipient of a EURYI award from the European Science Foundation.
    Keywords: Genome evolution ; Comparative genomics
    Repository Name: Woods Hole Open Access Server
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