Biosensor discovery of thyroxine transport disrupting chemicals.

@article{Marchesini2008BiosensorDO,
  title={Biosensor discovery of thyroxine transport disrupting chemicals.},
  author={Gerardo R Marchesini and Anastasia Meimaridou and Willem Haasnoot and Eline P. Meulenberg and Faywell Albertus and Mineyuki Mizuguchi and Makoto Takeuchi and Hubertus Irth and Albertinka J. Murk},
  journal={Toxicology and applied pharmacology},
  year={2008},
  volume={232 1},
  pages={
          150-60
        }
}
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165 Citations
Highly Influential Citations
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Background Citations
60
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165 Citations

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New approaches to assess the transthyretin binding capacity of bioactivated thyroid hormone disruptors.
  • M. Montaño, E. Cocco, A. Murk
  • Biology, Chemistry
    Toxicological sciences : an official journal of the Society of Toxicology
  • 2012
TLDR
The effectiveness of the in vitro metabolism and extraction of the model compounds CB 77 and BDE 47 was chemically quantified with a newly developed chromatographic method analyzing silylated derivatives of the OH-metabolites and coextractants.
In vitro fluorescence displacement investigation of thyroxine transport disruption by bisphenol A.
Surface plasmon resonance assay of inhibition by pharmaceuticals for thyroxine hormone binging to transport proteins.
Structure-directed screening and analysis of thyroid-disrupting chemicals targeting transthyretin based on molecular recognition and chromatographic separation.
TLDR
A structure-directed strategy for analysing TDCs targeting transthyretin (TTR) based on molecular imprinting and chromatographic separation is reported, suggesting that chemicals can be distinguished as TTR binders and non-binders by retention factors, with a predictive accuracy of more than 90%.
QSARs on the Thyroid Hormone Effects of Polybrominated Diphenyl Ether (PBDE) Derivatives
Halogenated phenolic contaminants inhibit the in vitro activity of the thyroid-regulating deiodinases in human liver.
TLDR
5'-Hydroxy 2,2',4,4',5-pentabromodiphenyl ether was found to be the most potent inhibitor of DI activity, and phenolic structures containing iodine were generally more potent inhibitors ofDI activity relative to brominated, chlorinated, and fluorinated analogues.
Assessment of the binding of hydroxylated polybrominated diphenyl ethers to thyroid hormone transport proteins using a site-specific fluorescence probe.
TLDR
A nonradioactive, site-specific fluorescein-thyroxine (F-T4) conjugate was designed and synthesized as a fluorescence probe to study the binding interaction of hydroxylated PBDEs to thyroxine-binding globulin (TBG) and transthyretin (TTR), two major TH transport proteins in human plasma.
Triple bioaffinity mass spectrometry concept for thyroid transporter ligands.
TLDR
The potential of BioMS using one affinity system, both for rapid screening and for confirmation and identification of known and unknown emerging thyroid EDCs is highlighted.
Structure-based investigation on the binding interaction of hydroxylated polybrominated diphenyl ethers with thyroxine transport proteins.
Evaluation of structurally different brominated flame retardants interacting with the transthyretin and their toxicity on HepG2 cells.
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References

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TLDR
The TPs-based biosensor assays were more sensitive, easier to perform, and faster to perform than the currently used methods such as radioligand binding assays and immunoprecipitation-HPLC.
Interaction of chlorinated phenols with thyroxine binding sites of human transthyretin, albumin and thyroid binding globulin.
Potential mechanisms of thyroid disruption in humans: interaction of organochlorine compounds with thyroid receptor, transthyretin, and thyroid-binding globulin.
TLDR
Hydroxylated PCBs have relatively low affinities for the human thyroid receptor in vitro, but they have a thyroid hormonelike affinity for the serum transport protein transthyretin.
Potent competitive interactions of some brominated flame retardants and related compounds with human transthyretin in vitro.
TLDR
Brominated flame retardants, especially the brominated phenols and tetrabromobisphenol A, are very potent competitors for T(4) binding to human transthyretin in vitro and may have effects on thyroid hormone homeostasis in vivo comparable to the thyroid-disrupting effects of PCBs.
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TLDR
Hydroxylated PHAHs are potent inhibitors of thyroid hormone sulfation, known to accumulate in fetal tissues after maternal exposure to PCBs, which may have implications for fetal thyroid hormone homeostasis and development.
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TLDR
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TLDR
The binding potencies of ortho-PCBs to TTR may represent a signature SAR that predicts specific biologic/toxic effects, consistent with measured biological activities of these PCBs, including effects on cell dopamine content, Ca(2+) homeostasis, and protein kinase C translocation in neuronal cells and brain homogenate preparations.
Thyroid hormone receptor isoform selectivity of thyroid hormone disrupting compounds quantified with an in vitro reporter gene assay.
Hydroxylated polychlorinated biphenyls selectively bind transthyretin in blood and inhibit amyloidogenesis: rationalizing rodent PCB toxicity.
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