Woods Hole Oceanographic Institution

Tim Verslycke

»Copepod diapause
»Lobster Shell Disease
»Crustacean molting receptor
»Lobster Shell Disease
»Mysids as test models for endocrine disruption testing
»Chlorotriazines in the Scheldt estuary
»Energy allocation in grasshopper
»Estrogens in Scheldt estuary
»Marsupial development in mysids to evaluate endocrine disruption
»B[a]P effects on steroid metabolism in mysid
»Ciona CYP3 genes
»Methoprene, nonylphenol, and estrone effects on mysid vitellogenesis
»Methoprene effects on mysid molting
»Mysid growth
»Mysid vitellin ELISA
»Mysid vitellin
»An analytical method to detect estrogens in water
»High levels of endocrine disruptors in wild mysid populations
»Energy allocation in wild mysid populations
»Cellular energy allocation validation with scope for growth
»Dolphin delivery prediction
»PhD thesis
»Endocrine disruptor effects on steroid and energy metabolism in mysid
»Mysid review
»TBT effects on steroid metabolism in mysid
»Metal mixture toxicity to mysid
»TBT effects on energy metabolism in mysid
»dichlorobenzene effects in zebrafish
»Ethinylestradiol effects on amphipod sexual development
»Metabolic studies with mysids
»Abiotic stress and energy metabolism in mysid
»Induced vitellogenesis in rainbow trout
»Steroid metabolism in mysid
»Endocrine disruption in freshwater snails
»Invasive mysid in Belgium

Ann M. Tarrant, Lars Behrendt, John J. Stegeman, and Tim Verslycke, Ecdysteroid receptor from the American lobster Homarus americanus: EcR/RXR isoform cloning and ligand-binding properties, Molecular and Cellular Endocrinology, 2011

In arthropods, ecdysteroids regulate molting by activating a heterodimer formed by the ecdysone receptor (EcR) and retinoid X receptor (RXR). While this mechanism is similar in insects and crustaceans, variation in receptor splicing, dimerization and ligand affinity adds specificity to molting processes. This study reports the EcR and RXR sequences from American lobster, a commercially and ecologically important crustacean. We cloned two EcR splice variants, both of which specifically bind ponasterone A, and two RXR variants, both of which enhance binding of ponasterone A to the EcR. Lobster EcR has high affinity for ponasterone A and muristerone and moderately high affinity for the insecticide tebufenozide. Bisphenol A, diethyl phthalate, and two polychlorinated biphenyls (PCB 29 and PCB 30), environmental chemicals shown to interfere with crustacean molting, showed little or no affinity for lobster EcR. These studies establish the molecular basis for investigation of lobster ecdysteroid signaling and signal disruption by environmental chemicals.

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