Effective cellular uptake and efflux of thyroid hormone by human monocarboxylate transporter 10
Open accessAbstract
Cellular entry of thyroid hormone is mediated by plasma membrane transporters, among others a T-type (aromatic) amino acid transporter. Monocarboxylate transporter 10 (MCT10) has been reported to transport aromatic amino acids but not iodothyronines. Within the MCT family, MCT10 is most homologous to MCT8, which is a very important iodothyronine transporter but does not transport amino acids. In view of this paradox, we decided to reinvestigate the possible transport of thyroid hormone by human (h) MCT10 in comparison with hMCT8. Transfection of COS1 cells with hMCT10 cDNA resulted in 1) the production of an approximately 55 kDa protein located to the plasma membrane as shown by immunoblotting and confocal microscopy, 2) a strong increase in the affinity labeling of intracellular type I deiodinase by N-bromoacetyl-[125I]T3, 3) a marked stimulation of cellular T4 and, particularly, T3 uptake, 4) a significant inhibition of T3 uptake by phenylalanine, tyrosine, and tryptophan of 12.5%, 22.2%, and 51.4%, respectively, and 5) a marked increase in the intracellular deiodination of T4 and T3 by different deiodinases. Cotransfection studies using the cytosolic thyroid hormone-binding protein μ-crystallin (CRYM) indicated that hMCT10 facilitates both cellular uptake and efflux of T4 and T3. In the absence of CRYM, hMCT10 and hMCT8 increased T3 uptake after 5 min incubation up to 4.0- and 1.9-fold, and in the presence of CRYM up to 6.9- and 5.8-fold, respectively. hMCT10 was less active toward T4 than hMCT8. These findings establish that hMCT10 is at least as active a thyroid hormone transporter as hMCT8, and that both transporters facilitate iodothyronine uptake as well as efflux.
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MCT10 has a similar effect on transporting T3 to MCT8 but is less active toward T4, as demonstrated in COS1 cells transfected with human MCT10 cDNA.
“MCT10 has a similar effect on transporting T3 to MCT8 but is less active toward T4 than MCT8, as demonstrated in COS1 cells transfected with human MCT10 cDNA (103).”
From Intrathyroidal feedforward and feedback network regulating thyroid hormone synthesis and secretion (2022) · cites this paper as [103]
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“In terminal ileum, the staining patterns of OATP1C1, OATP2B1, and MCT10 were similar between control and the patient (Figures 3A–”
BackgroundInfluential
- Authors
- Friesema, E. C. H., Jansen, J., Jachtenberg, J.-W., Visser, W. E., Kester, M. H. A., & Visser, T. J.
- Affiliations
- Erasmus MC (NL)
- Corresponding author
- Visser, Theo J.
- Venue
- Molecular Endocrinology
- Publisher
- The Endocrine Society
- Published
- 2008-06-01
- Volume
- 22
- Issue
- 6
- Pages
- 1357-1369
- ISSN
- 0888-8809 (ISSN-L)
- 1944-9917
- PMC
- PMC5419535
- OpenAlex
- W2102129489
- Cited by
- 285
- References
- 4
- Citations by year
- 2026: 9 · 2025: 15 · 2024: 10 · 2023: 6 · 2022: 11 · 2021: 11 · 2020: 13 · 2019: 18 · 2018: 14 · 2017: 19 · 2016: 16 · 2015: 14 · 2014: 18 · 2013: 25 · 2012: 16
- FWCI
- 16.14
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Molecular Endocrinology (publishedVersion)
- PubMed Central (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
- Fondation pour la Recherche Médicale
- Nederlandse Organisatie voor Wetenschappelijk Onderzoek
- Topics
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Thyroid Disorders and Treatments
- Health Sciences › Medicine › Oncology › Drug Transport and Resistance Mechanisms
- Physical Sciences › Environmental Science › Health, Toxicology and Mutagenesis › Chemical Analysis and Environmental Impact
- Keywords
- thyroid hormone transport, MCT10, MCT8, type I deiodinase, type 2 deiodinase, CRYM, thyroxine, triiodothyronine, phenylalanine, tyrosine, tryptophan
- MeSH terms
- mu-Crystallins, Amino Acid Sequence, Animals, Biological Transport, Cells, Cultured, Chlorocebus aethiops, Efficiency, Humans, Molecular Sequence Data, Phylogeny, Thyroid Hormones, Time Factors, Transfection, Sequence Homology, Amino Acid, COS Cells, Amino Acid Transport Systems, Neutral, Monocarboxylic Acid Transporters, Symporters
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