Evidence map›Paper›PMID 39167138›Full record

ArticleArchives of toxicology2024

Optimized methods for measuring competitive binding of chemical substances to thyroid hormone distributor proteins transthyretin and thyroxine binding globulin.

Yang Shen, Toine F H Bovee, Douwe Molenaar, Yoran Weide, Antsje Nolles, Carmen Braucic Mitrovic, Stefan P J van Leeuwen, Jochem Louisse, Timo Hamers

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Archives of toxicology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

2 citing papers in PubMed.

  1. Article
  2. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors.

Yang ShenWageningen Food Safety Research (WFSR), Wageningen University and Research, Akkermaalsbos 2, 6708 WB, Wageningen, The Netherlands.ORCID 0009-0008-6609-3699
Toine F H BoveeWageningen Food Safety Research (WFSR), Wageningen University and Research, Akkermaalsbos 2, 6708 WB, Wageningen, The Netherlands. toine.bovee@wur.nl.ORCID 0000-0002-6669-0417
Douwe MolenaarAmsterdam Institute for Life and Environment (A-LIFE), Vrije Universiteit Amsterdam, De Boelelaan 1085, 1081 HV, Amsterdam, The Netherlands.
Yoran WeideWageningen Food Safety Research (WFSR), Wageningen University and Research, Akkermaalsbos 2, 6708 WB, Wageningen, The Netherlands.
Antsje NollesWageningen Food Safety Research (WFSR), Wageningen University and Research, Akkermaalsbos 2, 6708 WB, Wageningen, The Netherlands.
Carmen Braucic MitrovicAmsterdam Institute for Life and Environment (A-LIFE), Vrije Universiteit Amsterdam, De Boelelaan 1085, 1081 HV, Amsterdam, The Netherlands.
Stefan P J van LeeuwenWageningen Food Safety Research (WFSR), Wageningen University and Research, Akkermaalsbos 2, 6708 WB, Wageningen, The Netherlands.
Jochem LouisseWageningen Food Safety Research (WFSR), Wageningen University and Research, Akkermaalsbos 2, 6708 WB, Wageningen, The Netherlands.
Timo HamersAmsterdam Institute for Life and Environment (A-LIFE), Vrije Universiteit Amsterdam, De Boelelaan 1085, 1081 HV, Amsterdam, The Netherlands.

Funding

China Scholarship Council 201908610201Ministerie van Landbouw, Natuur en Voedselkwaliteit KB-37-002-023
6 · The paper itself

Abstract

Transthyretin (TTR) and thyroxine-binding globulin (TBG) are two major thyroid hormone (TH) distributor proteins in human plasma, playing important roles in stabilizing the TH levels in plasma, delivery of TH to target tissues, and trans-barrier transport. Binding of xenobiotics to these distributor proteins can potentially affect all these three important roles of distributor proteins. Therefore, fast and cost-effective experimental methods are required for both TTR and TBG to screen both existing and new chemicals for their potential binding. In the present study, the TTR-binding assay was therefore simplified, optimized and pre-validated, while a new TBG-binding assay was developed based on fluorescence polarization as a readout. Seven model compounds (including positive and negative controls) were tested in the pre-validation study of the optimized TTR-binding assay and in the newly developed TBG-binding assay. The dissociation constants of the natural ligand (thyroxine, T4) and potential competitors were determined and compared between two distributor proteins, showing striking differences for perfluorooctanesulfonic acid (PFOS) and perfluorooctanoic acid (PFOA).

Indexed as

Binding, CompetitiveCaprylatesFluorocarbonsPrealbuminProtein BindingThyroxineThyroxine-Binding GlobulinFluorescence PolarizationHumansThyroid HormonesCaprylatesFluorocarbonsperfluorooctanoic acidPrealbuminThyroid HormonesThyroxineThyroxine-Binding GlobulinTTR protein, humanFluorescence polarizationPer- and polyfluoroalkyl substancesTBG bindingThyroid hormone system disruptorsTTR binding

Identifiers

PMID39167138
PMCPMC11489250

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.