Transport of Iodothyronines by Human L-Type Amino Acid Transporters

Zevenbergen, Chantal; Meima, Marcel E.; Lima de Souza, Elaine C.; Peeters, Robin P.; Kinne, Anita; Krause, Gerd; Visser, W. Edward; Visser, Theo J.

doi:10.1210/en.2015-1140

Cited by 55Amino Acid Enzymes and MetabolismThyroid Disorders and TreatmentsDrug Transport and Resistance Mechanisms

Transport of Iodothyronines by Human L-Type Amino Acid Transporters

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Zevenbergen, Chantal, Meima, Marcel E., Lima de Souza, Elaine C., Peeters, Robin P., Kinne, Anita, Krause, Gerd, Visser, W. Edward, Visser, Theo J.·2015·Endocrinology

DOI 10.1210/en.2015-1140

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Abstract

Thyroid hormone (TH) transporters facilitate cellular TH influx and efflux, which is paramount for normal physiology. The L-type amino acid transporters LAT1 and LAT2 are known to facilitate TH transport. However, the role of LAT3, LAT4, and LAT5 is still unclear. Therefore, the aim of this study was to further characterize TH transport by LAT1 and LAT2 and to explore possible TH transport by LAT3, LAT4, and LAT5. FLAG-LAT1-5 constructs were transiently expressed in COS1 cells. LAT1 and LAT2 were cotransfected with the CD98 heavy chain. Cellular transport was measured using 10 nM (125)I-labeled T4, T3, rT3, 3,3'-T2, and 10 μM [(125)I]3'-iodotyrosine (MIT) as substrates. Intracellular metabolism of these substrates was determined in cells cotransfected with either of the LATs with type 1 or type 3 deiodinase. LAT1 facilitated cellular uptake of all substrates and LAT2 showed a net uptake of T3, 3,3'-T2, and MIT. Expression of LAT3 or LAT4 did not affect transport of T4 and T3 but resulted in the decreased cellular accumulation of 3,3'-T2 and MIT. LAT5 did not facilitate the transport of any substrate. Cotransfection with LAT3 or LAT4 strongly diminished the cellular accumulation of 3,3'-T2 and MIT by LAT1 and LAT2. These data were confirmed by metabolism studies. LAT1 and LAT2 show distinct preferences for the uptake of the different iodocompounds, whereas LAT3 and LAT4 specifically facilitate the 3,3'-T2 and MIT efflux. Together our findings suggest that different sets of transporters with specific influx or efflux capacities may cooperate to regulate the cellular thyroid state.

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Human iBMECs express LAT1, LAT2, and MCT10, which may transport T4.
“human iBMECs do express LAT1, LAT2, and MCT10, which may transport T4 (Zevenbergen et al., 2015).”
From Modeling Psychomotor Retardation using iPSCs from MCT8-Deficient Patients Indicates a Prominent Role for the Blood-Brain Barrier (2017) · cites this paper as Zevenbergen et al., 2015
The Results report T4 uptake by LAT1 in transfected COS1 cells, while the Discussion describes LAT2 as a poor T4 transporter. The paper does not establish LAT1, LAT2, or MCT10 expression in human iBMECs, and it does not assess T4 transport by MCT10. Thus it supports the possibility of T4 transport by LAT1, but not the full statement attributed to it. (LLM, conf=0.86)
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Authors: Zevenbergen, C., Meima, M. E., Lima de Souza, E. C., Peeters, R. P., Kinne, A., Krause, G., Visser, W. E., & Visser, T. J.
Affiliations: Erasmus MC (NL)
Department of Internal Medicine and Rotterdam Thyroid Center (C.Z., M.E.M., E.C.L.d.S., R.P.P., W.E.V., T.J.V.), Erasmus University Medical Center, 3015 CN, Rotterdam, The Netherlands
Leibniz-Forschungsinstitut für Molekulare Pharmakologie (DE)
Corresponding author: Visser, Theo J.
ORCID: Meima, Marcel E.
Peeters, Robin P.
Krause, Gerd
Visser, W. Edward
Venue: Endocrinology
Publisher: The Endocrine Society
Published: 2015-08-25
Volume: 156
Issue: 11
Pages: 4345-4355
ISSN: 0013-7227 (ISSN-L)
1945-7170
DOI: 10.1210/en.2015-1140
OpenAlex: W1757132757
Cited by: 55
References: 53
Citations by year: 2025: 4 · 2024: 2 · 2023: 5 · 2022: 8 · 2021: 8 · 2020: 5 · 2019: 6 · 2018: 4 · 2017: 7 · 2016: 5
FWCI: 2.66
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: Endocrinology (publishedVersion)
PubMed (publishedVersion)
EUR Research Repository (Erasmus University Rotterdam) (publishedVersion)
EUR Research Repository (Erasmus University Rotterdam) (submittedVersion)
RePub (Erasmus University Rotterdam) (submittedVersion, other-oa)
RePub (Erasmus University Rotterdam) (submittedVersion)
Funders: Erasmus Medisch Centrum
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Amino Acid Enzymes and Metabolism
Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Thyroid Disorders and Treatments
Health Sciences › Medicine › Oncology › Drug Transport and Resistance Mechanisms
Keywords: thyroid hormone transport, L-type amino acid transporter, LAT1, LAT2, thyroxine, triiodothyronine, reverse T3, 3-iodotyrosine, deiodinases
MeSH terms: Animals, Biological Transport, Chlorocebus aethiops, Humans, Thyroid Hormones, COS Cells, Amino Acid Transport System L

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Transport of Iodothyronines by Human L-Type Amino Acid Transporters

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