Component

Human pendrin / SLC26A4

Canonical human pendrin anion transporter; physiological effects depend on tissue and membrane localization.

7 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. Pendrin knockdown did not change measured Calu-3 bicarbonate secretion.

    Human pendrin / SLC26A4 → Airway epithelial bicarbonate secretion source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/chloride-research/29536650.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "9da6a23e90b30ab4d0c2b537af65076e93cc3370470f64a9dafdeaaff525f157", "start_char": 0, "end_char": 1519, "text_sha256": "9da6a23e90b30ab4d0c2b537af65076e93cc3370470f64a9dafdeaaff525f157"}
    experimental_model
    Knockdown and epithelial secretion assays
    exposure
    Pendrin shRNA, CFTR deficiency, culture conditions
    limitations
    Authors explicitly limit extrapolation to other airway epithelia.
    nutrient_topic
    Chloride research collection; topical membership is not evidence of a direct dietary effect. · Chloride
    organism
    Human Calu-3 cell line
    plain_language
    One airway model relied mainly on CFTR, despite detectable pendrin.
    primary_references
    [chloride-p29536650] Most bicarbonate secretion by Calu-3 cells is mediated by CFTR and independent of pendrin. (2018). https://pubmed.ncbi.nlm.nih.gov/29536650/ DOI: 10.14814/phy2.13641
    tissue_or_cell_type
    Airway gland-like epithelial model

    Chloride: transport, acid-base balance, nutrient interactions and loss states (2026-09-17) · lines 1043–1054

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Knockdown and epithelial secretion assays · source_derived_draft · unverified_draft

    ### chloride-calu3-pendrin-null Pendrin knockdown did not change measured Calu-3 bicarbonate secretion. Condition category: normal nutrient_topic: Chloride research collection; topical membership is not evidence of a direct dietary effect. plain_language: One airway model relied mainly on CFTR, despite detectable pendrin. organism: Human Calu-3 cell line tissue_or_cell_type: Airway gland-like epithelial model experimental_model: Knockdown and epithelial secretion assays limitations: Authors explicitly limit extrapolation to other airway epithelia. exposure: Pendrin shRNA, CFTR deficiency, culture conditions evidence_span: {"source_cache": "artifacts/chloride-research/29536650.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "9da6a23e90b30ab4d0c2b537af65076e93cc3370470f64a9dafdeaaff525f157", "start_char": 0, "end_char": 1519, "text_sha256": "9da6a23e90b30ab4d0c2b537af65076e93cc3370470f64a9dafdeaaff525f157"} [chloride-p29536650] Most bicarbonate secretion by Calu-3 cells is mediated by CFTR and independent of pendrin. (2018). https://pubmed.ncbi.nlm.nih.gov/29536650/ DOI: 10.14814/phy2.13641
    Complete structured claim and evidence

  2. IL-4-induced pendrin supported chloride/bicarbonate exchange in primary airway surface cultures.

    Human pendrin / SLC26A4 → Airway epithelial bicarbonate secretion source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/chloride-research/30742493.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "1ff038684ceacd46ad1e237d0cf13337924ec0f611d00a373cd3cbeeeb31864a", "start_char": 0, "end_char": 1882, "text_sha256": "1ff038684ceacd46ad1e237d0cf13337924ec0f611d00a373cd3cbeeeb31864a"}
    experimental_model
    Primary epithelial cultures and native tissue
    exposure
    IL-4 induction and pendrin knockdown
    limitations
    Inflamed surface epithelium differs from Calu-3; no universal airway assignment.
    nutrient_topic
    Chloride research collection; topical membership is not evidence of a direct dietary effect. · Chloride
    organism
    Human nasal and bronchial epithelia
    plain_language
    Different airway cells can use a different balance of the same transport proteins.
    primary_references
    [chloride-p30742493] Pendrin Mediates Bicarbonate Secretion and Enhances Cystic Fibrosis Transmembrane Conductance Regulator Function in Airway Surface Epithelia. (2019). https://pubmed.ncbi.nlm.nih.gov/30742493/ DOI: 10.1165/rcmb.2018-0158oc
    tissue_or_cell_type
    Ciliated airway surface

    Chloride: transport, acid-base balance, nutrient interactions and loss states (2026-09-17) · lines 1056–1067

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Primary epithelial cultures and native tissue · source_derived_draft · unverified_draft

    ### chloride-surface-pendrin IL-4-induced pendrin supported chloride/bicarbonate exchange in primary airway surface cultures. Condition category: normal nutrient_topic: Chloride research collection; topical membership is not evidence of a direct dietary effect. plain_language: Different airway cells can use a different balance of the same transport proteins. organism: Human nasal and bronchial epithelia tissue_or_cell_type: Ciliated airway surface experimental_model: Primary epithelial cultures and native tissue limitations: Inflamed surface epithelium differs from Calu-3; no universal airway assignment. exposure: IL-4 induction and pendrin knockdown evidence_span: {"source_cache": "artifacts/chloride-research/30742493.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "1ff038684ceacd46ad1e237d0cf13337924ec0f611d00a373cd3cbeeeb31864a", "start_char": 0, "end_char": 1882, "text_sha256": "1ff038684ceacd46ad1e237d0cf13337924ec0f611d00a373cd3cbeeeb31864a"} [chloride-p30742493] Pendrin Mediates Bicarbonate Secretion and Enhances Cystic Fibrosis Transmembrane Conductance Regulator Function in Airway Surface Epithelia. (2019). https://pubmed.ncbi.nlm.nih.gov/30742493/ DOI: 10.1165/rcmb.2018-0158oc
    Complete structured claim and evidence

  3. Inducing pendrin approximately doubled the forskolin-stimulated CFTR-sensitive current in the tested cells.

    Human pendrin / SLC26A4 → CFTR anion conductance source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/chloride-research/30742493.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "1ff038684ceacd46ad1e237d0cf13337924ec0f611d00a373cd3cbeeeb31864a", "start_char": 0, "end_char": 1882, "text_sha256": "1ff038684ceacd46ad1e237d0cf13337924ec0f611d00a373cd3cbeeeb31864a"}
    experimental_model
    Primary epithelial cultures and native tissue
    exposure
    IL-4 induction and pendrin knockdown
    limitations
    Inflamed surface epithelium differs from Calu-3; no universal airway assignment.
    nutrient_topic
    Chloride research collection; topical membership is not evidence of a direct dietary effect. · Chloride
    organism
    Human nasal and bronchial epithelia
    plain_language
    One transporter can influence another channel’s measured activity.
    primary_references
    [chloride-p30742493] Pendrin Mediates Bicarbonate Secretion and Enhances Cystic Fibrosis Transmembrane Conductance Regulator Function in Airway Surface Epithelia. (2019). https://pubmed.ncbi.nlm.nih.gov/30742493/ DOI: 10.1165/rcmb.2018-0158oc
    tissue_or_cell_type
    Ciliated airway surface

    Chloride: transport, acid-base balance, nutrient interactions and loss states (2026-09-17) · lines 1069–1080

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Primary epithelial cultures and native tissue · source_derived_draft · unverified_draft

    ### chloride-surface-pendrin-cftr Inducing pendrin approximately doubled the forskolin-stimulated CFTR-sensitive current in the tested cells. Condition category: normal nutrient_topic: Chloride research collection; topical membership is not evidence of a direct dietary effect. plain_language: One transporter can influence another channel’s measured activity. organism: Human nasal and bronchial epithelia tissue_or_cell_type: Ciliated airway surface experimental_model: Primary epithelial cultures and native tissue limitations: Inflamed surface epithelium differs from Calu-3; no universal airway assignment. exposure: IL-4 induction and pendrin knockdown evidence_span: {"source_cache": "artifacts/chloride-research/30742493.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "1ff038684ceacd46ad1e237d0cf13337924ec0f611d00a373cd3cbeeeb31864a", "start_char": 0, "end_char": 1882, "text_sha256": "1ff038684ceacd46ad1e237d0cf13337924ec0f611d00a373cd3cbeeeb31864a"} [chloride-p30742493] Pendrin Mediates Bicarbonate Secretion and Enhances Cystic Fibrosis Transmembrane Conductance Regulator Function in Airway Surface Epithelia. (2019). https://pubmed.ncbi.nlm.nih.gov/30742493/ DOI: 10.1165/rcmb.2018-0158oc
    Complete structured claim and evidence

  4. Human thyroid immunolocalization detected pendrin at the apical membrane in a subset of follicular epithelial cells.

    Human pendrin / SLC26A4 → Thyrocyte apical membrane source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    false
    experimental_model
    Human thyroid immunolocalization; separate rat FRTL-5 regulatory experiments
    exposure
    Peptide-specific antibody immunolocalization; thyroid specimens included Graves disease tissue.
    limitations
    Cell subset and tissue context matter; this does not establish pendrin as the only iodide exit route.
    nutrient_topic
    Iodine research collection; topical membership is not evidence of a direct dietary effect. · Iodine
    organism
    Homo sapiens
    plain_language
    Pendrin can face the thyroid’s hormone-making follicular space.
    primary_references
    [iodine-trans-pendrin-location2000] Pendrin, the protein encoded by the Pendred syndrome gene (PDS), is an apical porter of iodide in the thyroid and is regulated by thyroglobulin in FRTL-5 cells. (2000). https://pubmed.ncbi.nlm.nih.gov/10650967/ DOI: 10.1210/endo.141.2.7303
    tissue_or_cell_type
    Thyroid follicular epithelium

    Iodine: thyroid hormone production, deficiency, excess and nutrient interactions (2026-09-17) · lines 284–295

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human thyroid immunolocalization; separate rat FRTL-5 regulatory experiments · source_derived_draft · unverified_draft

    ### iodine-trans-pendrin-apical Human thyroid immunolocalization detected pendrin at the apical membrane in a subset of follicular epithelial cells. Condition category: normal nutrient_topic: Iodine research collection; topical membership is not evidence of a direct dietary effect. plain_language: Pendrin can face the thyroid’s hormone-making follicular space. organism: Homo sapiens tissue_or_cell_type: Thyroid follicular epithelium experimental_model: Human thyroid immunolocalization; separate rat FRTL-5 regulatory experiments limitations: Cell subset and tissue context matter; this does not establish pendrin as the only iodide exit route. exposure: Peptide-specific antibody immunolocalization; thyroid specimens included Graves disease tissue. cross_nutrient: false [iodine-trans-pendrin-location2000] Pendrin, the protein encoded by the Pendred syndrome gene (PDS), is an apical porter of iodide in the thyroid and is regulated by thyroglobulin in FRTL-5 cells. (2000). https://pubmed.ncbi.nlm.nih.gov/10650967/ DOI: 10.1210/endo.141.2.7303
    Complete structured claim and evidence

  5. Expression of human pendrin increased chloride transport in Xenopus oocytes and Sf9 cells, alongside increased iodide transport.

    Human pendrin / SLC26A4 → Chloride ion source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    true
    experimental_model
    Human pendrin expressed in Xenopus oocytes and Sf9 insect cells
    exposure
    PDS cRNA microinjection or recombinant baculovirus expression; concentrations not provided in abstract.
    limitations
    This demonstrates shared anion transport capability, not that dietary chloride deficiency blocks iodine repletion.
    nutrient_topic
    Iodine research collection; topical membership is not evidence of a direct dietary effect. · Iodine
    organism
    Human protein in Xenopus laevis and Spodoptera frugiperda cells
    plain_language
    Pendrin handles chloride as well as iodide.
    primary_references
    [iodine-trans-pendrin-halides1999] The Pendred syndrome gene encodes a chloride-iodide transport protein. (1999). https://pubmed.ncbi.nlm.nih.gov/10192399/ DOI: 10.1038/7783
    tissue_or_cell_type
    Heterologous cell membranes
    transport_effect
    depends Pendrin is an anion exchanger and the record reports increased transport without naming its direction.
    transport_pool
    the cytosol across the plasma membrane Pendrin is an anion exchanger and the record reports increased transport without naming its direction.

    Iodine: thyroid hormone production, deficiency, excess and nutrient interactions (2026-09-17) · lines 310–321

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human pendrin expressed in Xenopus oocytes and Sf9 insect cells · source_derived_draft · unverified_draft

    ### iodine-trans-pendrin-chloride Expression of human pendrin increased chloride transport in Xenopus oocytes and Sf9 cells, alongside increased iodide transport. Condition category: normal nutrient_topic: Iodine research collection; topical membership is not evidence of a direct dietary effect. plain_language: Pendrin handles chloride as well as iodide. organism: Human protein in Xenopus laevis and Spodoptera frugiperda cells tissue_or_cell_type: Heterologous cell membranes experimental_model: Human pendrin expressed in Xenopus oocytes and Sf9 insect cells limitations: This demonstrates shared anion transport capability, not that dietary chloride deficiency blocks iodine repletion. exposure: PDS cRNA microinjection or recombinant baculovirus expression; concentrations not provided in abstract. cross_nutrient: true [iodine-trans-pendrin-halides1999] The Pendred syndrome gene encodes a chloride-iodide transport protein. (1999). https://pubmed.ncbi.nlm.nih.gov/10192399/ DOI: 10.1038/7783
    Complete structured claim and evidence

  6. Human pendrin expression supported iodide efflux in COS-7 and CHO mammalian-cell transport experiments.

    Human pendrin / SLC26A4 → Cellular iodide efflux source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    false
    experimental_model
    Human pendrin expressed in COS-7 and CHO cells with NIS; rat FRTL-5 comparison
    exposure
    Pendrin/NIS transfection; concentrations not provided in abstract.
    limitations
    Expression-cell data do not establish exclusive thyroid efflux control or transport specificity in every tissue.
    nutrient_topic
    Iodine research collection; topical membership is not evidence of a direct dietary effect. · Iodine
    organism
    Human protein in monkey COS-7 and hamster CHO cells
    plain_language
    Pendrin can let iodide leave cells.
    primary_references
    [iodine-trans-pendrin-efflux2002] Pendrin is an iodide-specific apical porter responsible for iodide efflux from thyroid cells. (2002). https://pubmed.ncbi.nlm.nih.gov/12107249/ DOI: 10.1210/jcem.87.7.8679
    tissue_or_cell_type
    Cultured-cell plasma membrane

    Iodine: thyroid hormone production, deficiency, excess and nutrient interactions (2026-09-17) · lines 297–308

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human pendrin expressed in COS-7 and CHO cells with NIS; rat FRTL-5 comparison · source_derived_draft · unverified_draft

    ### iodine-trans-pendrin-efflux Human pendrin expression supported iodide efflux in COS-7 and CHO mammalian-cell transport experiments. Condition category: normal nutrient_topic: Iodine research collection; topical membership is not evidence of a direct dietary effect. plain_language: Pendrin can let iodide leave cells. organism: Human protein in monkey COS-7 and hamster CHO cells tissue_or_cell_type: Cultured-cell plasma membrane experimental_model: Human pendrin expressed in COS-7 and CHO cells with NIS; rat FRTL-5 comparison limitations: Expression-cell data do not establish exclusive thyroid efflux control or transport specificity in every tissue. exposure: Pendrin/NIS transfection; concentrations not provided in abstract. cross_nutrient: false [iodine-trans-pendrin-efflux2002] Pendrin is an iodide-specific apical porter responsible for iodide efflux from thyroid cells. (2002). https://pubmed.ncbi.nlm.nih.gov/12107249/ DOI: 10.1210/jcem.87.7.8679
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. 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

In the sources

Preserved passages that mention this component, quoted exactly. Open one to read it in context.

    This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.

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