Component

Human SLC26A7 anion transporter

Human SLC26A7 protein; direct iodide/chloride transport and thyroid localization must retain experimental context.

9 recorded relationships. Experimental role, claim status and evidence remain attached to each record.

Read recorded mechanisms Open recursive mind map

How nutrients influence it

Every nutrient with a recorded effect on this component, credited to the nutrient that acted rather than the chapter that recorded it. Open a nutrient to see the findings and the conditions they were measured under.

How nutrients reach it in more than one step

Chains of two or more recorded steps that end here, grouped by the nutrient they start from. Each step is a separate finding, so a chain is a route a mechanism could take, not proof that it does.

Tracing routes…

What it does

Every recorded relationship this component is part of, grouped by its role. Plain wording comes first; the technical statement follows.

Recorded relationships

What it acts on

  1. Ishii et al. detected human thyroid SLC26A7 staining predominantly on the apical side facing the follicular lumen.

    Human SLC26A7 anion transporter → Thyrocyte apical membrane source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    false
    experimental_model
    Human thyroid tissue; recombinant human SLC26A7 in Nthy, MDCK, COS-7 and HEK293T cells; two affected siblings
    exposure
    SLC26A7 immunofluorescence with NIS/pendrin localization comparisons; Fig. 1.
    limitations
    Other studies report basolateral localization; antibody, tissue and experimental context remain relevant.
    nutrient_topic
    Iodine research collection; topical membership is not evidence of a direct dietary effect. · Iodine
    organism
    Homo sapiens
    plain_language
    One human thyroid study placed SLC26A7 mainly toward the follicular space.
    primary_references
    [iodine-trans-slc26a7-2019] Congenital goitrous hypothyroidism is caused by dysfunction of the iodide transporter SLC26A7. (2019). https://pubmed.ncbi.nlm.nih.gov/31372509/ DOI: 10.1038/s42003-019-0503-6
    tissue_or_cell_type
    Thyroid follicular tissue

    Iodine: thyroid hormone production, deficiency, excess and nutrient interactions (2026-09-17) · lines 323–334

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human thyroid tissue; recombinant human SLC26A7 in Nthy, MDCK, COS-7 and HEK293T cells; two affected siblings · source_derived_draft · unverified_draft

    ### iodine-trans-a7-apical2019 Ishii et al. detected human thyroid SLC26A7 staining predominantly on the apical side facing the follicular lumen. Condition category: normal nutrient_topic: Iodine research collection; topical membership is not evidence of a direct dietary effect. plain_language: One human thyroid study placed SLC26A7 mainly toward the follicular space. organism: Homo sapiens tissue_or_cell_type: Thyroid follicular tissue experimental_model: Human thyroid tissue; recombinant human SLC26A7 in Nthy, MDCK, COS-7 and HEK293T cells; two affected siblings limitations: Other studies report basolateral localization; antibody, tissue and experimental context remain relevant. exposure: SLC26A7 immunofluorescence with NIS/pendrin localization comparisons; Fig. 1. cross_nutrient: false [iodine-trans-slc26a7-2019] Congenital goitrous hypothyroidism is caused by dysfunction of the iodide transporter SLC26A7. (2019). https://pubmed.ncbi.nlm.nih.gov/31372509/ DOI: 10.1038/s42003-019-0503-6
    Complete structured claim and evidence

  2. The 2026 Finnish SLC26A7 study reported basolateral SLC26A7 localization in human thyrocytes, with intense staining in hyperthyroid samples.

    Human SLC26A7 anion transporter → Thyrocyte basolateral membrane source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    false
    experimental_model
    Six human thyroid samples including two homozygous carriers, goitrous/hyperactive samples and controls; additional mouse models
    exposure
    Six human tissue samples spanning carriers, goitrous/hyperactive tissues and controls; abstract-level tissue localization result.
    limitations
    Small heterogeneous tissue set and abstract-only extraction; this differs from the 2019 apical result and does not prove all thyroid contexts share one location.
    nutrient_topic
    Iodine research collection; topical membership is not evidence of a direct dietary effect. · Iodine
    organism
    Homo sapiens
    plain_language
    A later human thyroid study placed SLC26A7 on the blood-facing side.
    primary_references
    [iodine-trans-slc26a7-localization2026] Finnish-Enriched SLC26A7 Variant in Congenital Hypothyroidism: Clinical Spectrum, Thyroid Histopathology, and Expression Analysis. (2026). https://pubmed.ncbi.nlm.nih.gov/41791885/ DOI: 10.1177/10507256251411983
    tissue_or_cell_type
    Human thyroid tissue

    Iodine: thyroid hormone production, deficiency, excess and nutrient interactions (2026-09-17) · lines 479–490

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Six human thyroid samples including two homozygous carriers, goitrous/hyperactive samples and controls; additional mouse models · source_derived_draft · unverified_draft

    ### iodine-trans-a7-basolateral2026 The 2026 Finnish SLC26A7 study reported basolateral SLC26A7 localization in human thyrocytes, with intense staining in hyperthyroid samples. Condition category: normal nutrient_topic: Iodine research collection; topical membership is not evidence of a direct dietary effect. plain_language: A later human thyroid study placed SLC26A7 on the blood-facing side. organism: Homo sapiens tissue_or_cell_type: Human thyroid tissue experimental_model: Six human thyroid samples including two homozygous carriers, goitrous/hyperactive samples and controls; additional mouse models limitations: Small heterogeneous tissue set and abstract-only extraction; this differs from the 2019 apical result and does not prove all thyroid contexts share one location. exposure: Six human tissue samples spanning carriers, goitrous/hyperactive tissues and controls; abstract-level tissue localization result. cross_nutrient: false [iodine-trans-slc26a7-localization2026] Finnish-Enriched SLC26A7 Variant in Congenital Hypothyroidism: Clinical Spectrum, Thyroid Histopathology, and Expression Analysis. (2026). https://pubmed.ncbi.nlm.nih.gov/41791885/ DOI: 10.1177/10507256251411983
    Complete structured claim and evidence

  3. Human SLC26A7 cryo-EM maps in the iodide-loaded state supported iodide assignments at a canonical site and a second site near the gate-domain interface.

    Human SLC26A7 anion transporter → Iodide ion source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    true
    experimental_model
    Purified human SLC26A7 cryo-EM; recombinant human SLC26A7 in HEK293T cells with whole-cell patch clamp
    exposure
    Apo and iodide-loaded cryo-EM structures at approximately 3.2 and 3.1 Å; Fig. 2.
    limitations
    Binding-site structures support transport capability but do not establish apical versus basolateral thyroid localization.
    nutrient_topic
    Iodine research collection; topical membership is not evidence of a direct dietary effect. · Iodine
    organism
    Homo sapiens
    plain_language
    A recent structure directly supports iodide binding by human SLC26A7.
    primary_references
    [iodine-trans-slc26a7-structure2025] Structural basis for substrate recognition mechanism of human SLC26A7. (2025). https://pubmed.ncbi.nlm.nih.gov/40817112/ DOI: 10.1038/s41467-025-62792-w
    tissue_or_cell_type
    Purified membrane protein

    Iodine: thyroid hormone production, deficiency, excess and nutrient interactions (2026-09-17) · lines 453–464

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified human SLC26A7 cryo-EM; recombinant human SLC26A7 in HEK293T cells with whole-cell patch clamp · source_derived_draft · unverified_draft

    ### iodine-trans-a7-bound-iodide2025 Human SLC26A7 cryo-EM maps in the iodide-loaded state supported iodide assignments at a canonical site and a second site near the gate-domain interface. Condition category: normal nutrient_topic: Iodine research collection; topical membership is not evidence of a direct dietary effect. plain_language: A recent structure directly supports iodide binding by human SLC26A7. organism: Homo sapiens tissue_or_cell_type: Purified membrane protein experimental_model: Purified human SLC26A7 cryo-EM; recombinant human SLC26A7 in HEK293T cells with whole-cell patch clamp limitations: Binding-site structures support transport capability but do not establish apical versus basolateral thyroid localization. exposure: Apo and iodide-loaded cryo-EM structures at approximately 3.2 and 3.1 Å; Fig. 2. cross_nutrient: true [iodine-trans-slc26a7-structure2025] Structural basis for substrate recognition mechanism of human SLC26A7. (2025). https://pubmed.ncbi.nlm.nih.gov/40817112/ DOI: 10.1038/s41467-025-62792-w
    Complete structured claim and evidence

  4. MDCK monolayers coexpressing human NIS and SLC26A7 transferred more basal-chamber radioiodide into the apical chamber after 45 minutes than monolayers expressing NIS alone.

    Human SLC26A7 anion transporter → Cellular iodide efflux source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    false
    experimental_model
    Human thyroid tissue; recombinant human SLC26A7 in Nthy, MDCK, COS-7 and HEK293T cells; two affected siblings
    exposure
    Induced transporter expression 24 hours before assay; basal radioactive NaI and 45-minute transport readout; Fig. 3c.
    limitations
    A 2018 HEK293 efflux assay was negative. This experiment establishes capability under its conditions, not universal apical placement in human thyroid.
    nutrient_topic
    Iodine research collection; topical membership is not evidence of a direct dietary effect. · Iodine
    organism
    Human proteins in canine MDCK cells
    plain_language
    SLC26A7 increased iodide movement across a polarized cell sheet in this experiment.
    primary_references
    [iodine-trans-slc26a7-2019] Congenital goitrous hypothyroidism is caused by dysfunction of the iodide transporter SLC26A7. (2019). https://pubmed.ncbi.nlm.nih.gov/31372509/ DOI: 10.1038/s42003-019-0503-6
    tissue_or_cell_type
    Polarized epithelial bicameral culture

    Iodine: thyroid hormone production, deficiency, excess and nutrient interactions (2026-09-17) · lines 336–347

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human thyroid tissue; recombinant human SLC26A7 in Nthy, MDCK, COS-7 and HEK293T cells; two affected siblings · source_derived_draft · unverified_draft

    ### iodine-trans-a7-efflux2019 MDCK monolayers coexpressing human NIS and SLC26A7 transferred more basal-chamber radioiodide into the apical chamber after 45 minutes than monolayers expressing NIS alone. Condition category: normal nutrient_topic: Iodine research collection; topical membership is not evidence of a direct dietary effect. plain_language: SLC26A7 increased iodide movement across a polarized cell sheet in this experiment. organism: Human proteins in canine MDCK cells tissue_or_cell_type: Polarized epithelial bicameral culture experimental_model: Human thyroid tissue; recombinant human SLC26A7 in Nthy, MDCK, COS-7 and HEK293T cells; two affected siblings limitations: A 2018 HEK293 efflux assay was negative. This experiment establishes capability under its conditions, not universal apical placement in human thyroid. exposure: Induced transporter expression 24 hours before assay; basal radioactive NaI and 45-minute transport readout; Fig. 3c. cross_nutrient: false [iodine-trans-slc26a7-2019] Congenital goitrous hypothyroidism is caused by dysfunction of the iodide transporter SLC26A7. (2019). https://pubmed.ncbi.nlm.nih.gov/31372509/ DOI: 10.1038/s42003-019-0503-6
    Complete structured claim and evidence

  5. Human SLC26A7 expression in HEK293T cells generated chloride and iodide currents that increased when bath halide concentrations rose from 50 to 149 mM.

    Human SLC26A7 anion transporter → Iodide ion source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    true
    experimental_model
    Purified human SLC26A7 cryo-EM; recombinant human SLC26A7 in HEK293T cells with whole-cell patch clamp
    exposure
    Whole-cell patch clamp 24 hours after 2 micrograms plasmid transfection; 50/149 mM total halide conditions; voltage steps from −100 to +100 mV.
    limitations
    Halide concentrations greatly exceed physiological iodide; transport capacity does not settle net thyroid iodide flux, stoichiometry or localization.
    nutrient_topic
    Iodine research collection; topical membership is not evidence of a direct dietary effect. · Iodine
    organism
    Homo sapiens
    plain_language
    Human SLC26A7 can carry both chloride and iodide under controlled laboratory conditions.
    primary_references
    [iodine-trans-slc26a7-structure2025] Structural basis for substrate recognition mechanism of human SLC26A7. (2025). https://pubmed.ncbi.nlm.nih.gov/40817112/ DOI: 10.1038/s41467-025-62792-w
    tissue_or_cell_type
    HEK293T plasma membrane
    transport_effect
    depends Recorded as a halide current that rose with bath halide concentration, so the direction follows the gradient.
    transport_pool
    the cytosol across the plasma membrane Recorded as a halide current that rose with bath halide concentration, so the direction follows the gradient.

    Iodine: thyroid hormone production, deficiency, excess and nutrient interactions (2026-09-17) · lines 466–477

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified human SLC26A7 cryo-EM; recombinant human SLC26A7 in HEK293T cells with whole-cell patch clamp · source_derived_draft · unverified_draft

    ### iodine-trans-a7-halide-current2025 Human SLC26A7 expression in HEK293T cells generated chloride and iodide currents that increased when bath halide concentrations rose from 50 to 149 mM. Condition category: normal nutrient_topic: Iodine research collection; topical membership is not evidence of a direct dietary effect. plain_language: Human SLC26A7 can carry both chloride and iodide under controlled laboratory conditions. organism: Homo sapiens tissue_or_cell_type: HEK293T plasma membrane experimental_model: Purified human SLC26A7 cryo-EM; recombinant human SLC26A7 in HEK293T cells with whole-cell patch clamp limitations: Halide concentrations greatly exceed physiological iodide; transport capacity does not settle net thyroid iodide flux, stoichiometry or localization. exposure: Whole-cell patch clamp 24 hours after 2 micrograms plasmid transfection; 50/149 mM total halide conditions; voltage steps from −100 to +100 mV. cross_nutrient: true [iodine-trans-slc26a7-structure2025] Structural basis for substrate recognition mechanism of human SLC26A7. (2025). https://pubmed.ncbi.nlm.nih.gov/40817112/ DOI: 10.1038/s41467-025-62792-w
    Complete structured claim and evidence

  6. Cangul et al. found no enhancement of radioiodide efflux from HEK293 cells coexpressing human NIS and SLC26A7 compared with control cells, whereas pendrin enhanced efflux.

    Human SLC26A7 anion transporter → Cellular iodide efflux source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    false
    experimental_model
    Six human families, human SLC26A7/NIS-transfected HEK293 cells, Slc26a7-null mice
    exposure
    NIS plus SLC26A7, pendrin or control expression; time-dependent radioiodide efflux; five experiments, Fig. 2E.
    limitations
    A negative result in this assay is not proof that SLC26A7 never conducts iodide; later positive transport and structural evidence is retained.
    nutrient_topic
    Iodine research collection; topical membership is not evidence of a direct dietary effect. · Iodine
    organism
    Homo sapiens protein and HEK293 cells
    plain_language
    An earlier cell assay did not detect an iodide export effect from SLC26A7.
    primary_references
    [iodine-trans-slc26a7-2018] Homozygous loss-of-function mutations in SLC26A7 cause goitrous congenital hypothyroidism. (2018). https://pubmed.ncbi.nlm.nih.gov/30333321/ DOI: 10.1172/jci.insight.99631
    tissue_or_cell_type
    Cultured-cell plasma membrane

    Iodine: thyroid hormone production, deficiency, excess and nutrient interactions (2026-09-17) · lines 375–386

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Six human families, human SLC26A7/NIS-transfected HEK293 cells, Slc26a7-null mice · source_derived_draft · unverified_draft

    ### iodine-trans-a7-no-efflux2018 Cangul et al. found no enhancement of radioiodide efflux from HEK293 cells coexpressing human NIS and SLC26A7 compared with control cells, whereas pendrin enhanced efflux. Condition category: normal nutrient_topic: Iodine research collection; topical membership is not evidence of a direct dietary effect. plain_language: An earlier cell assay did not detect an iodide export effect from SLC26A7. organism: Homo sapiens protein and HEK293 cells tissue_or_cell_type: Cultured-cell plasma membrane experimental_model: Six human families, human SLC26A7/NIS-transfected HEK293 cells, Slc26a7-null mice limitations: A negative result in this assay is not proof that SLC26A7 never conducts iodide; later positive transport and structural evidence is retained. exposure: NIS plus SLC26A7, pendrin or control expression; time-dependent radioiodide efflux; five experiments, Fig. 2E. cross_nutrient: false [iodine-trans-slc26a7-2018] Homozygous loss-of-function mutations in SLC26A7 cause goitrous congenital hypothyroidism. (2018). https://pubmed.ncbi.nlm.nih.gov/30333321/ DOI: 10.1172/jci.insight.99631
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Human SLC26A7 Q500Ter did not produce the wild-type enhancement of iodide-dependent current and iodide-sensitive fluorescence responses in HEK293T cells.

    Human SLC26A7 p.Gln500Ter → SLC26A7 iodide conductance source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    cross_nutrient
    false
    experimental_model
    Human thyroid tissue; recombinant human SLC26A7 in Nthy, MDCK, COS-7 and HEK293T cells; two affected siblings
    exposure
    Whole-cell electrophysiology and NaCl-to-NaI solution exchange; Figure 6; iodide-sensitive YFP readout.
    limitations
    These high-ion expression assays do not measure a physiological thyroid efflux rate; direction is determined by the imposed gradients.
    nutrient_topic
    Iodine research collection; topical membership is not evidence of a direct dietary effect. · Iodine
    organism
    Homo sapiens protein and HEK293T cells
    plain_language
    The truncated transporter failed the functional iodide-transport tests.
    primary_references
    [iodine-trans-slc26a7-2019] Congenital goitrous hypothyroidism is caused by dysfunction of the iodide transporter SLC26A7. (2019). https://pubmed.ncbi.nlm.nih.gov/31372509/ DOI: 10.1038/s42003-019-0503-6
    tissue_or_cell_type
    Cell plasma membrane
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Iodine: thyroid hormone production, deficiency, excess and nutrient interactions (2026-09-17) · lines 362–373

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human thyroid tissue; recombinant human SLC26A7 in Nthy, MDCK, COS-7 and HEK293T cells; two affected siblings · source_derived_draft · unverified_draft

    ### iodine-trans-a7-q500-current Human SLC26A7 Q500Ter did not produce the wild-type enhancement of iodide-dependent current and iodide-sensitive fluorescence responses in HEK293T cells. Condition category: machinery_impairment nutrient_topic: Iodine research collection; topical membership is not evidence of a direct dietary effect. plain_language: The truncated transporter failed the functional iodide-transport tests. organism: Homo sapiens protein and HEK293T cells tissue_or_cell_type: Cell plasma membrane experimental_model: Human thyroid tissue; recombinant human SLC26A7 in Nthy, MDCK, COS-7 and HEK293T cells; two affected siblings limitations: These high-ion expression assays do not measure a physiological thyroid efflux rate; direction is determined by the imposed gradients. exposure: Whole-cell electrophysiology and NaCl-to-NaI solution exchange; Figure 6; iodide-sensitive YFP readout. cross_nutrient: false [iodine-trans-slc26a7-2019] Congenital goitrous hypothyroidism is caused by dysfunction of the iodide transporter SLC26A7. (2019). https://pubmed.ncbi.nlm.nih.gov/31372509/ DOI: 10.1038/s42003-019-0503-6
    Complete structured claim and evidence

  2. Human SLC26A7 Q500Ter expressed in MDCK cells aggregated in the cytosol instead of showing the predominant surface localization of wild-type protein.

    Human SLC26A7 p.Gln500Ter → SLC26A7 membrane localization source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    cross_nutrient
    false
    experimental_model
    Human thyroid tissue; recombinant human SLC26A7 in Nthy, MDCK, COS-7 and HEK293T cells; two affected siblings
    exposure
    FLAG-tagged wild-type versus Q500Ter expression; immunofluorescence Fig. 5.
    limitations
    Tagged heterologous expression; localization and current loss are separate observations.
    nutrient_topic
    Iodine research collection; topical membership is not evidence of a direct dietary effect. · Iodine
    organism
    Human protein in canine MDCK cells
    plain_language
    This truncation prevents normal transporter placement.
    primary_references
    [iodine-trans-slc26a7-2019] Congenital goitrous hypothyroidism is caused by dysfunction of the iodide transporter SLC26A7. (2019). https://pubmed.ncbi.nlm.nih.gov/31372509/ DOI: 10.1038/s42003-019-0503-6
    tissue_or_cell_type
    Cell surface and cytosol
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Iodine: thyroid hormone production, deficiency, excess and nutrient interactions (2026-09-17) · lines 349–360

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human thyroid tissue; recombinant human SLC26A7 in Nthy, MDCK, COS-7 and HEK293T cells; two affected siblings · source_derived_draft · unverified_draft

    ### iodine-trans-a7-q500-localization Human SLC26A7 Q500Ter expressed in MDCK cells aggregated in the cytosol instead of showing the predominant surface localization of wild-type protein. Condition category: machinery_impairment nutrient_topic: Iodine research collection; topical membership is not evidence of a direct dietary effect. plain_language: This truncation prevents normal transporter placement. organism: Human protein in canine MDCK cells tissue_or_cell_type: Cell surface and cytosol experimental_model: Human thyroid tissue; recombinant human SLC26A7 in Nthy, MDCK, COS-7 and HEK293T cells; two affected siblings limitations: Tagged heterologous expression; localization and current loss are separate observations. exposure: FLAG-tagged wild-type versus Q500Ter expression; immunofluorescence Fig. 5. cross_nutrient: false [iodine-trans-slc26a7-2019] Congenital goitrous hypothyroidism is caused by dysfunction of the iodide transporter SLC26A7. (2019). https://pubmed.ncbi.nlm.nih.gov/31372509/ DOI: 10.1038/s42003-019-0503-6
    Complete structured claim and evidence

  3. Homozygous truncating SLC26A7 variants segregated with goitrous congenital hypothyroidism in six unrelated families studied by Cangul et al.

    Human SLC26A7 truncating pathogenic variants → Goitrous congenital hypothyroidism source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    cross_nutrient
    false
    experimental_model
    Six human families, human SLC26A7/NIS-transfected HEK293 cells, Slc26a7-null mice
    exposure
    Six families with 13 affected individuals; molecular genetic characterization.
    limitations
    Genetic association establishes a machinery disorder, not low dietary iodine; precise physiological transport mechanism remained unresolved.
    nutrient_topic
    Iodine research collection; topical membership is not evidence of a direct dietary effect. · Iodine
    organism
    Homo sapiens
    plain_language
    Inherited SLC26A7 defects can disrupt thyroid hormone production.
    primary_references
    [iodine-trans-slc26a7-2018] Homozygous loss-of-function mutations in SLC26A7 cause goitrous congenital hypothyroidism. (2018). https://pubmed.ncbi.nlm.nih.gov/30333321/ DOI: 10.1172/jci.insight.99631
    tissue_or_cell_type
    Thyroid and whole-person clinical phenotype
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Iodine: thyroid hormone production, deficiency, excess and nutrient interactions (2026-09-17) · lines 388–399

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Six human families, human SLC26A7/NIS-transfected HEK293 cells, Slc26a7-null mice · source_derived_draft · unverified_draft

    ### iodine-trans-a7-truncation-ch Homozygous truncating SLC26A7 variants segregated with goitrous congenital hypothyroidism in six unrelated families studied by Cangul et al. Condition category: machinery_impairment nutrient_topic: Iodine research collection; topical membership is not evidence of a direct dietary effect. plain_language: Inherited SLC26A7 defects can disrupt thyroid hormone production. organism: Homo sapiens tissue_or_cell_type: Thyroid and whole-person clinical phenotype experimental_model: Six human families, human SLC26A7/NIS-transfected HEK293 cells, Slc26a7-null mice limitations: Genetic association establishes a machinery disorder, not low dietary iodine; precise physiological transport mechanism remained unresolved. exposure: Six families with 13 affected individuals; molecular genetic characterization. cross_nutrient: false [iodine-trans-slc26a7-2018] Homozygous loss-of-function mutations in SLC26A7 cause goitrous congenital hypothyroidism. (2018). https://pubmed.ncbi.nlm.nih.gov/30333321/ DOI: 10.1172/jci.insight.99631
    Complete structured claim and evidence

In the sources

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