Evidence map›Paper›PMID 26601072›Full record

ArticleEuropean thyroid journal2015

Involvement of the L-Type Amino Acid Transporter Lat2 in the Transport of 3,3'-Diiodothyronine across the Plasma Membrane.

Anita Kinne, Melanie Wittner, Eva K Wirth, Katrin M Hinz, Ralf Schülein, Josef Köhrle, Gerd Krause

Open access · bronzeAbstract read
In one paragraph

Article in European thyroid journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
2.3field-weighted citation impact, top 13% 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

13 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Review
  3. Thyroid Hormone Transporters in Pregnancy and Fetal Development.International journal of molecular sciences · 2022
    Review
  4. Article
  5. Thyroid Hormone Transporters in a Human Placental Cell Model.Thyroid : official journal of the American Thyroid Association · 2022
    Article
  6. Review
  7. Article
  8. Review
  9. Review
  10. Review
  11. Article
  12. Article
  13. Article
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

7 authors at 2 institutions in 1 country.

Anita KinneLeibniz-Institut für Molekulare Pharmakologie (FMP), Berlin, Germany.
Melanie WittnerLeibniz-Institut für Molekulare Pharmakologie (FMP), Berlin, Germany.
Eva K WirthInstitut für Experimentelle Endokrinologie, Charité-Universitätsmedizin Berlin, Berlin, Germany.
Katrin M HinzLeibniz-Institut für Molekulare Pharmakologie (FMP), Berlin, Germany.
Ralf SchüleinLeibniz-Institut für Molekulare Pharmakologie (FMP), Berlin, Germany.
Josef KöhrleInstitut für Experimentelle Endokrinologie, Charité-Universitätsmedizin Berlin, Berlin, Germany.
Gerd KrauseLeibniz-Institut für Molekulare Pharmakologie (FMP), Berlin, Germany.
Leibniz-Forschungsinstitut für Molekulare Pharmakologie · DECharité - Universitätsmedizin Berlin · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Thyroid hormones are transported across cell membranes by transmembrane transporter proteins, for example by members of the monocarboxylate transporter (MCT) and the L-type amino acid transporter (LAT) families. LATs consist of a light chain (e.g. LAT2) and a heavy chain (CD98), which is essential for their cell surface expression and functionality. The specificity of Lat2 for thyroid hormones and their metabolites and its role in their transport was not fully clear. This fact motivated us to establish a cell system to elucidate the uptake of thyroid hormones and their metabolites by mouse Lat2. The coinjection of cRNA coding for Lat2 and CD98 into Xenopus laevis oocytes resulted in a markedly increased level of 3,3'-diiodo-L-thyronine (3,3'-T2) and to some extent also enhanced T3 transport. To gain insight into properties of thyroid hormones and their metabolites transported by Lat2, we inhibited 3,3'-T2 uptake by various iodothyronine derivatives. T1 and T2 derivatives as well as 2-aminobicyclo-[2, 2,1]-heptane-2-carboxylic acid strongly competed with 3,3'-T2 uptake. In addition, we performed T2 uptake measurements with the thyroid hormone-specific transporter MCT8. For both Lat2 and MCT8, Km values in a low micromolar range were calculated. We demonstrated that oocytes are a suitable system for thyroid hormone transport studies mediated by Lat2. Our data indicates that Lat2 compared to other thyroid hormone transporters prefers 3,3'-T2 as the substrate. Thus, Lat2 might contribute to the availability of thyroid hormone by importing and/or exporting 3,3'-T2, which is generated either by T3 inactivation or by rapid deiodinase 1-mediated rT3 degradation.

Indexed as

3,3′-DiiodothyronineL-type amino acid transporter 2Molecular uptakeOocytesT3Thyroid hormonesTransporters

Identifiers

PMID26601072
PMCPMC4640293
OpenAlexW2258117015

What OpenQuestion holds

Textmetadata
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.