Evidence map›Paper›PMID 23584369›Full record

ArticleEnvironmental health perspectives2013

Sulfated metabolites of polychlorinated biphenyls are high-affinity ligands for the thyroid hormone transport protein transthyretin.

Fabian A Grimm, Hans-Joachim Lehmler, Xianran He, Larry W Robertson, Michael W Duffel

Open access · diamondAbstract read
In one paragraph

Article in Environmental health perspectives, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
3.9field-weighted citation impact, top 6% of its field
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

50 citing papers in PubMed, 104 citations in OpenAlex.

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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

5 authors at 1 institution in 1 country.

Fabian A GrimmInterdisciplinary Graduate Program in Human Toxicology, Department of Pharmaceutical Sciences and Experimental Therapeutics, College of Pharmacy, College of Public Health, The University of Iowa, Iowa City, Iowa 52246, USA.
Hans-Joachim Lehmler
Xianran He
Larry W Robertson
Michael W Duffel
University of Iowa · US

Funding

Training CoreP42ES013661 · NIEHS · UNIVERSITY OF IOWA · PI HANS-JOACHIM LEHMLER · 2006 to 2026
$60.3M
Pulmonary Toxicology Facility CoreP30ES005605 · NIEHS · UNIVERSITY OF IOWA · PI Brandi Janssen · 1990 to 2026
$40.5M
NIEHS NIH HHS P30 ES005605NIEHS NIH HHS P30 ES05605NIEHS NIH HHS P42 ES013661
6 · The paper itself

Abstract

backgroundThe displacement of l-thyroxine (T4) from binding sites on transthyretin (TTR) is considered a significant contributing mechanism in polychlorinated biphenyl (PCB)-induced thyroid disruption. Previous research has discovered hydroxylated PCB metabolites (OH-PCBs) as high-affinity ligands for TTR, but the binding potential of conjugated PCB metabolites such as PCB sulfates has not been explored.

objectivesWe evaluated the binding of five lower-chlorinated PCB sulfates to human TTR and compared their binding characteristics to those determined for their OH-PCB precursors and for T4.

methodsWe used fluorescence probe displacement studies and molecular docking simulations to characterize the binding of PCB sulfates to TTR. The stability of PCB sulfates and the reversibility of these interactions were characterized by HPLC analysis of PCB sulfates after their binding to TTR. The ability of OH-PCBs to serve as substrates for human cytosolic sulfotransferase 1A1 (hSULT1A1) was assessed by OH-PCB-dependent formation of adenosine-3',5'-diphosphate, an end product of the sulfation reaction.

resultsAll five PCB sulfates were able to bind to the high-affinity binding site of TTR with equilibrium dissociation constants (Kd values) in the low nanomolar range (4.8-16.8 nM), similar to that observed for T4 (4.7 nM). Docking simulations provided corroborating evidence for these binding interactions and indicated multiple high-affinity modes of binding. All OH-PCB precursors for these sulfates were found to be substrates for hSULT1A1.

conclusionsOur findings show that PCB sulfates are high-affinity ligands for human TTR and therefore indicate, for the first time, a potential relevance for these metabolites in PCB-induced thyroid disruption.

Indexed as

ArylsulfotransferaseHumansLigandsMolecular Docking SimulationPolychlorinated BiphenylsPrealbuminSulfatesThyroxineArylsulfotransferaseLigandsPolychlorinated BiphenylsPrealbuminSulfatesSULT1A1 protein, humanThyroxine

Identifiers

PMID23584369
PMCPMC3672920
OpenAlexW2014056881

What OpenQuestion holds

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Read underepoch 390

Registered trials

None linked

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.