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  • Endocrine  (2)
  • Heat shock protein  (2)
  • Nuclear receptor  (2)
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  • 1
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    Hormonal signaling in cnidarians : do we understand the pathways well enough to know whether they are being disrupted? (2007)
    Details
    Publication Date: 2022-05-25
    Description: Author Posting. © The Author, 2006. This is the author's version of the work. It is posted here by permission of Springer for personal use, not for redistribution. The definitive version was published in Ecotoxicology 16 (2007): 5-13, doi:10.1007/s10646-006-0121-1.
    Description: Cnidarians occupy a key evolutionary position as basal metazoans and are ecologically important as predators, prey and structure-builders. Bioregulatory molecules (e.g., amines, peptides and steroids) have been identified in cnidarians, but cnidarian signaling pathways remain poorly characterized. Cnidarians, especially hydras, are regularly used in toxicity testing, but few studies have used cnidarians in explicit testing for signal disruption. Sublethal endpoints developed in cnidarians include budding, regeneration, gametogenesis, mucus production and larval metamorphosis. Cnidarian genomic databases, microarrays and other molecular tools are increasingly facilitating mechanistic investigation of signaling pathways and signal disruption. Elucidation of cnidarian signaling processes in a comparative context can provide insight into the evolution and diversification of metazoan bioregulation. Characterizing signaling and signal disruption in cnidarians may also provide unique opportunities for evaluating risk to valuable marine resources, such as coral reefs.
    Keywords: Bioregulation ; Cnidaria ; Coral ; Endocrine ; Signal Disruption
    Repository Name: Woods Hole Open Access Server
    Type: Preprint
    Format: 72795 bytes
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  • 2
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    Heat shock protein expression during stress and diapause in the marine copepod Calanus finmarchicus (2011)
    Details
    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 Journal of Insect Physiology 57 (2011): 665-675, doi:10.1016/j.jinsphys.2011.03.007.
    Description: Calanoid copepods, such as Calanus finmarchicus, are a key component of marine food webs. C. finmarchicus undergoes a facultative diapause during juvenile development, which profoundly affects their seasonal distribution and availability to their predators. The current ignorance of how copepod diapause is regulated limits understanding of copepod population dynamics, distribution, and ecosystem interactions. Heat shock proteins (Hsps) are a superfamily of molecular chaperones characteristically upregulated in response to stress conditions and frequently associated with diapause in other taxa. In this study, 8 heat shock proteins were identified in C. finmarchicus C5 copepodids (Hsp21, Hsp22, p26, Hsp90, and 4 forms of Hsp70), and expression of these transcripts was characterized in response to handling stress and in association with diapause. Hsp21, Hsp22, and Hsp70A (cytosolic subfamily) were induced by handling stress. Expression of Hsp70A was also elevated in shallow active copepodids relative to deep diapausing copepodids, which may reflect induction of this gene by varied stressors in active animals. In contrast, expression of Hsp22 was elevated in deep diapausing animals; Hsp22 may play a role both in short-term stress responses and in protecting proteins from degradation during diapause. Expression of most of the Hsps examined did not vary in response to diapause, perhaps because the diapause of C. finmarchicus is not associated with the extreme environmental conditions (e.g., freezing, desiccation) experienced by many other taxa, such as overwintering insects or Artemia cysts.
    Description: Funding for AMA was provided by the WHOI Summer Student Fellowship Program and an EPA STAR fellowship.
    Keywords: Copepod ; Crustacean ; Diapause ; Heat shock protein ; Stress response
    Repository Name: Woods Hole Open Access Server
    Type: Preprint
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  • 3
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    Gene expression in American lobster (Homarus americanus) with epizootic shell disease (2012)
    National Shellfisheries Association
    Details
    Publication Date: 2022-05-25
    Description: Author Posting. © National Shellfisheries Association, 2012. This article is posted here by permission of National Shellfisheries Association for personal use, not for redistribution. The definitive version was published in Journal of Shellfish Research 31 (2012): 505-513, doi:10.2983/035.031.0210.
    Description: Epizootic shell disease (ESD) has been reported widely in American lobster (Homarus americanus, Milne Edwards) in southern New England. The appearance of irregular, deep lesions—characteristic of ESD—has been associated previously with elevated levels of ecdysteroids and premature molting, but the underlying molecular and physiological changes associated with ESD remain poorly understood. Previously, we identified several genes, including arginine kinase and hemocyanin, that were expressed differentially in lobsters exhibiting signs of ESD (diseased) versus those lobsters exhibiting no signs of ESD (assumed healthy), and quantified their expression. In this study, we extend these findings and measure expression of a suite of 12 genes in tissues from 36 female lobsters of varying disease condition. In addition, molt stage is evaluated as a possible confounding factor in the expression of the selected genes. The expression of several genes changed significantly with disease stage. Arginine kinase expression decreased significantly in thoracic muscle of lobsters with signs of ESD. Ecdysteroid receptor expression was elevated significantly in both muscle and hepatopancreas of lobsters with signs of ESD. CYP45, a cytochrome P450 form that was shown previously to covary with ecdysteroid levels and to be inducible by some xenobiotics, showed significantly increased expression in hepatopancreas of lobsters with signs of ESD. Together, these results demonstrate that the expression of several genes is altered in lobsters showing signs of ESD, even when accounting for variation in molt stage. Given the observed changes in ecdysteroid receptor, arginine kinase, and CYP45 expression, further investigations of the association, if any, between molting, muscular function and xenobiotic metabolism and ESD are warranted.
    Description: This work was supported by the National Marine Fisheries Service as the New England Lobster Research Initiative: Lobster Shell Disease under NOAA grant NA06NMF4720100 to the University of Rhode Island Fisheries Center.
    Keywords: Arginine kinase ; 100 lobsters ; Cytochrome P450 ; Ecdysteroid ; Endocrine ; Hepatopancreas ; Heat shock protein ; Epizootic shell disease ; American lobster ; Shade
    Repository Name: Woods Hole Open Access Server
    Type: Article
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  • 4
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    Conservation of DNA and ligand binding properties of retinoid X receptor from the placozoan Trichoplax adhaerens to human (2018)
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    Publication Date: 2022-05-25
    Description: Author Posting. © The Author(s), 2018. 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 Journal of Steroid Biochemistry and Molecular Biology 184 (2018): 3-10, doi:10.1016/j.jsbmb.2018.02.010.
    Description: Nuclear receptors are a superfamily of transcription factors restricted to animals. These transcription factors regulate a wide variety of genes with diverse roles in cellular homeostasis, development, and physiology. The origin and specificity of ligand binding within lineages of nuclear receptors (e.g., subfamilies) continues to be a focus of investigation geared toward understanding how the functions of these proteins were shaped over evolutionary history. Among early-diverging animal lineages, the retinoid X receptor (RXR) is first detected in the placozoan, Trichoplax adhaerens. To gain insight into RXR evolution, we characterized ligand- and DNA-binding activity of the RXR from T. adhaerens (TaRXR). Like bilaterian RXRs, TaRXR specifically bound 9-cis-retinoic acid, which is consistent with a recently published result and supports a conclusion that the ancestral RXR bound ligand. DNA binding site specificity of TaRXR was determined through protein binding microarrays (PBMs) and compared with human RXR. The binding sites for these two RXR proteins were broadly conserved (~85% shared high-affinity sequences within a targeted array), suggesting evolutionary constraint for the regulation of downstream genes. We searched for predicted binding motifs of the T. adhaerens genome within 1000 bases of annotated genes to identify potential regulatory targets. We identified 648 unique protein coding regions with predicted TaRXR binding sites that had diverse predicted functions, with enriched processes related to intracellular signal transduction and protein transport. Together, our data support hypotheses that the original RXR protein in animals bound a ligand with structural similarity to 9-cis-retinoic acid; the DNA motif recognized by RXR has changed little in more than 1 billion years of evolution; and the suite of processes regulated by this transcription factor diversified early in animal evolution.
    Description: Support for AMT was provided by the Tropical Research Initiative and an Internal Research and Development Award from the Woods Hole Oceanographic Institution. AMR was supported by NIH award R15GM114740. JM was supported by NSF award 1536530 to AMR. DM-P, BF and FMS were supported by NIH award R01DK094707 to FMS.
    Keywords: DNA binding motif ; Nuclear receptor ; Protein binding microarray
    Repository Name: Woods Hole Open Access Server
    Type: Preprint
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  • 5
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    Correlated evolution of androgen receptor and aromatase revisited (2010)
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    Publication Date: 2022-05-25
    Description: Author Posting. © The Authors, 2010. This is the author's version of the work. It is posted here by permission of Oxford University Press for personal use, not for redistribution. The definitive version was published in Molecular Biology and Evolution 27 (2010): 2211-2215, doi:10.1093/molbev/msq129.
    Description: Conserved interactions among proteins or other molecules can provide strong evidence for coevolution across their evolutionary history. Diverse phylogenetic methods have been applied to identify potential coevolutionary relationships. In most cases, these methods minimally require comparisons of orthologous sequences and appropriate controls to separate effects of selection from the overall evolutionary relationships. In vertebrates, androgen receptor (AR) and cytochrome p450 aromatase (CYP19) share an affinity for androgenic steroids, which serve as receptor ligands and enzyme substrates. In a recent study, Tiwary and Li (2009) reported that AR and CYP19 displayed a signature of ancient and conserved interactions throughout all of the Eumetazoa (i.e., cnidarians, protostomes, and deuterostomes). Because these findings conflicted with a number of previous studies, we reanalyzed the data set used by Tiwary and Li. First, our analyses demonstrate that the invertebrate genes used in the previous analysis are not orthologous sequences, but instead represent a diverse set of nuclear receptors and cytochrome p450 enzymes with no confirmed or hypothesized relationships with androgens. Second, we show that (1) their analytical approach, which measures correlations in evolutionary distances between proteins, potentially led to spurious significant relationships due simply to conserved domains and (2) control comparisons provide positive evidence for a strong influence of evolutionary history. We discuss how corrections to this method and analysis of key taxa (e.g., duplications in the teleost fish and suiform lineages) can inform investigations of the coevolutionary relationships between androgen receptor and aromatase.
    Description: AMR was supported by the Postdoctoral Scholar Program at the Woods Hole Oceanographic Institution, with funding provided by The Beacon Institute for Rivers and Estuaries, and AMT was supported by WHOI Assistant Scientist Endowed Support.
    Keywords: Androgen receptor ; Aromatase ; Correlated evolution ; Cytochrome p450 ; Nuclear receptor
    Repository Name: Woods Hole Open Access Server
    Type: Preprint
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