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Advancing in vitro assessment of iodide uptake inhibition: integrating a novel biotransformation pretreatment step

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F25%3A00141545" target="_blank" >RIV/00216224:14310/25:00141545 - isvavai.cz</a>

  • Result on the web

    <a href="https://link.springer.com/article/10.1007/s00204-025-04034-y" target="_blank" >https://link.springer.com/article/10.1007/s00204-025-04034-y</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1007/s00204-025-04034-y" target="_blank" >10.1007/s00204-025-04034-y</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Advancing in vitro assessment of iodide uptake inhibition: integrating a novel biotransformation pretreatment step

  • Original language description

    Thyroid hormones (TH) are essential for vertebrate development, growth, and metabolism. The increasing prevalence of anthropogenic chemicals with TH-disrupting potential highlights the urgent need for advanced methods to assess their impact on TH homeostasis. Inhibition of the sodium-iodide symporter (NIS) has been identified as a key molecular initiating event disrupting the TH system across species, with significant relevance for diagnostic and therapeutic applications in various carcinomas. This study presents in vitro bioassays for evaluating the effects of compounds on iodide uptake into cells, a critical step in TH production mediated by NIS. Two novel stably transfected human cell lines overexpressing human NIS were employed along with a rat thyroid cell model FRTL-5, using colorimetric Sandell-Kolthoff (SK) reaction for iodide detection. The results from 23 model compounds demonstrate comparability across various in vitro models and radioactivity-based assays. To enhance physiological relevance, an external biotransformation system (BTS) was integrated and optimized for live-cell compatibility without inducing cytotoxicity or interfering with the assay. Compounds identified as NIS inhibitors were evaluated using the BTS-augmented assay, which revealed that metabolic activity mitigated the inhibitory effects of some chemicals. The augmented assay exhibited strong concordance with in vivo and in silico biotransformation data. Protein sequence alignment confirmed high conservation of NIS functional domains across vertebrates, reinforcing the cross-species applicability of the findings. The SK-based NIS assay, with optional BTS integration, represents a sensitive, robust, and high-throughput amendable alternative to radioactivity-based methods, for characterizing the impacts of individual compounds and complex environmental mixtures on TH homeostasis.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    30108 - Toxicology

Result continuities

  • Project

    <a href="/en/project/EH22_008%2F0004644" target="_blank" >EH22_008/0004644: Saving lives through research in early cancer detection and prevention: Molecular, genomic and societal factors</a><br>

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>S - Specificky vyzkum na vysokych skolach<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2025

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Archives of Toxicology

  • ISSN

    0340-5761

  • e-ISSN

    1432-0738

  • Volume of the periodical

    99

  • Issue of the periodical within the volume

    7

  • Country of publishing house

    DE - GERMANY

  • Number of pages

    17

  • Pages from-to

    2783-2799

  • UT code for WoS article

    001485544500001

  • EID of the result in the Scopus database

    2-s2.0-105004921893