Iodide ion

experimental_model

Primary airway epithelial cultures and human oral-KI exposure; separate experimental arms.

exposure_category

Study-specific exposure, including pharmacological and in-vitro conditions; normal is the schema fallback outside the three availability categories.

limitations

Culture antiviral activity and human secretion measurements do not establish prevention or treatment of human infection.

nutrient_topic

Potassium iodide research collection; shared-anion and comparator studies are not all KI interventions. · Potassium iodide

plain_language

Changing the enzyme substrate changed antiviral activity.

primary_references

Enhancement of respiratory mucosal antiviral defenses by the oxidation of iodide. · 2011 · https://pubmed.ncbi.nlm.nih.gov/21441383/ · DOI 10.1165/rcmb.2010-0329oc

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AI-assisted research curation; primary-study references, chemical references and label statements individually identified. Not publisher full text. · supports · Primary airway epithelial cultures and human oral-KI exposure; separate experimental arms. · source_derived_draft · unverified_draft

## ki-air-adeno Changing the enzyme substrate changed antiviral activity. Replacing thiocyanate with iodide in the LPO/H2O2 system reduced adenovirus transduction. Model: Primary airway epithelial cultures and human oral-KI exposure; separate experimental arms. Limitations: Culture antiviral activity and human secretion measurements do not establish prevention or treatment of human infection. Evidence location: Primary abstract Enhancement of respiratory mucosal antiviral defenses by the oxidation of iodide. · 2011 · https://pubmed.ncbi.nlm.nih.gov/21441383/ · DOI 10.1165/rcmb.2010-0329oc

experimental_model

Human airway epithelial cells at an air–liquid interface; transepithelial radiotracer transport.

exposure_category

Study-specific exposure, including pharmacological and in-vitro conditions; normal is the schema fallback outside the three availability categories.

limitations

The proposed apical CFTR route was inferred pharmacologically, not proven by this experiment. This is iodide biology, not a KI-specific counter-ion effect.

nutrient_topic

Potassium iodide research collection; shared-anion and comparator studies are not all KI interventions. · Potassium iodide

plain_language

Iodide can compete with another antimicrobial substrate during delivery.

primary_references

Transcellular thiocyanate transport by human airway epithelia. · 2004 · https://pubmed.ncbi.nlm.nih.gov/15345749/ · DOI 10.1113/jphysiol.2004.071548

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AI-assisted research curation; primary-study references, chemical references and label statements individually identified. Not publisher full text. · supports · Human airway epithelial cells at an air–liquid interface; transepithelial radiotracer transport. · source_derived_draft · unverified_draft

## ki-air-competition Iodide can compete with another antimicrobial substrate during delivery. Basolateral iodide reversibly inhibited thiocyanate transport, apparent Ki 9 ± 8 micromolar. Model: Human airway epithelial cells at an air–liquid interface; transepithelial radiotracer transport. Limitations: The proposed apical CFTR route was inferred pharmacologically, not proven by this experiment. This is iodide biology, not a KI-specific counter-ion effect. Evidence location: Primary abstract Transcellular thiocyanate transport by human airway epithelia. · 2004 · https://pubmed.ncbi.nlm.nih.gov/15345749/ · DOI 10.1113/jphysiol.2004.071548

experimental_model

Primary airway epithelial cultures and human oral-KI exposure; separate experimental arms.

exposure_category

Study-specific exposure, including pharmacological and in-vitro conditions; normal is the schema fallback outside the three availability categories.

limitations

Culture antiviral activity and human secretion measurements do not establish prevention or treatment of human infection.

nutrient_topic

Potassium iodide research collection; shared-anion and comparator studies are not all KI interventions. · Potassium iodide

plain_language

Iodide and thiocyanate were not interchangeable against these viruses.

primary_references

Enhancement of respiratory mucosal antiviral defenses by the oxidation of iodide. · 2011 · https://pubmed.ncbi.nlm.nih.gov/21441383/ · DOI 10.1165/rcmb.2010-0329oc

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AI-assisted research curation; primary-study references, chemical references and label statements individually identified. Not publisher full text. · supports · Primary airway epithelial cultures and human oral-KI exposure; separate experimental arms. · source_derived_draft · unverified_draft

## ki-air-rsv Iodide and thiocyanate were not interchangeable against these viruses. The LPO/iodide/H2O2 system reduced RSV titre; the tested thiocyanate system did not inactivate RSV or adenovirus. Model: Primary airway epithelial cultures and human oral-KI exposure; separate experimental arms. Limitations: Culture antiviral activity and human secretion measurements do not establish prevention or treatment of human infection. Evidence location: Primary abstract Enhancement of respiratory mucosal antiviral defenses by the oxidation of iodide. · 2011 · https://pubmed.ncbi.nlm.nih.gov/21441383/ · DOI 10.1165/rcmb.2010-0329oc

experimental_model

Human airway epithelial cells at an air–liquid interface; transepithelial radiotracer transport.

exposure_category

Study-specific exposure, including pharmacological and in-vitro conditions; normal is the schema fallback outside the three availability categories.

limitations

The proposed apical CFTR route was inferred pharmacologically, not proven by this experiment. This is iodide biology, not a KI-specific counter-ion effect.

nutrient_topic

Potassium iodide research collection; shared-anion and comparator studies are not all KI interventions. · Potassium iodide

plain_language

Airway cells can transport iodide.

primary_references

Transcellular thiocyanate transport by human airway epithelia. · 2004 · https://pubmed.ncbi.nlm.nih.gov/15345749/ · DOI 10.1113/jphysiol.2004.071548

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AI-assisted research curation; primary-study references, chemical references and label statements individually identified. Not publisher full text. · supports · Human airway epithelial cells at an air–liquid interface; transepithelial radiotracer transport. · source_derived_draft · unverified_draft

## ki-air-transport Airway cells can transport iodide. Airway epithelia transported iodide with apparent Km 111 ± 69 micromolar. Model: Human airway epithelial cells at an air–liquid interface; transepithelial radiotracer transport. Limitations: The proposed apical CFTR route was inferred pharmacologically, not proven by this experiment. This is iodide biology, not a KI-specific counter-ion effect. Evidence location: Primary abstract Transcellular thiocyanate transport by human airway epithelia. · 2004 · https://pubmed.ncbi.nlm.nih.gov/15345749/ · DOI 10.1113/jphysiol.2004.071548

experimental_model

Purified biochemical reaction; GSH measured by amperometric titration.

exposure_category

Study-specific exposure, including pharmacological and in-vitro conditions; normal is the schema fallback outside the three availability categories.

limitations

No demonstration that ordinary KI intake depletes human glutathione.

nutrient_topic

Potassium iodide research collection; shared-anion and comparator studies are not all KI interventions. · Potassium iodide

plain_language

This iodine chemistry can consume glutathione in a test system.

primary_references

Free radical generation and coupled thiol oxidation by lactoperoxidase/SCN-/H2O2. · 1992 · https://pubmed.ncbi.nlm.nih.gov/1324202/ · DOI 10.1016/0891-5849(92)90014-8

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AI-assisted research curation; primary-study references, chemical references and label statements individually identified. Not publisher full text. · supports · Purified biochemical reaction; GSH measured by amperometric titration. · source_derived_draft · unverified_draft

## ki-gsh This iodine chemistry can consume glutathione in a test system. Iodide substituted for thiocyanate in LPO/H2O2-dependent glutathione oxidation; chloride and bromide were ineffective substitutes. Model: Purified biochemical reaction; GSH measured by amperometric titration. Limitations: No demonstration that ordinary KI intake depletes human glutathione. Evidence location: Primary abstract Free radical generation and coupled thiol oxidation by lactoperoxidase/SCN-/H2O2. · 1992 · https://pubmed.ncbi.nlm.nih.gov/1324202/ · DOI 10.1016/0891-5849(92)90014-8

experimental_model

Purified LPO transient kinetics; pH 7, 15 °C; preparation species unresolved in abstract.

exposure_category

Study-specific exposure, including pharmacological and in-vitro conditions; normal is the schema fallback outside the three availability categories.

limitations

Purified enzyme kinetics; concentrations, substrate competition and reaction order determine relevance in tissues.

nutrient_topic

Potassium iodide research collection; shared-anion and comparator studies are not all KI interventions. · Potassium iodide

plain_language

Iodide supplies electrons to activated lactoperoxidase.

primary_references

Reaction of lactoperoxidase compound I with halides and thiocyanate. · 2002 · https://pubmed.ncbi.nlm.nih.gov/12269834/ · DOI 10.1021/bi026326x

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AI-assisted research curation; primary-study references, chemical references and label statements individually identified. Not publisher full text. · supports · Purified LPO transient kinetics; pH 7, 15 °C; preparation species unresolved in abstract. · source_derived_draft · unverified_draft

## ki-lpo-iodide Iodide supplies electrons to activated lactoperoxidase. Iodide reduced LPO compound I to native enzyme at (1.2 ± 0.04) × 10^8 M−1 s−1. Model: Purified LPO transient kinetics; pH 7, 15 °C; preparation species unresolved in abstract. Limitations: Purified enzyme kinetics; concentrations, substrate competition and reaction order determine relevance in tissues. Evidence location: Primary abstract Reaction of lactoperoxidase compound I with halides and thiocyanate. · 2002 · https://pubmed.ncbi.nlm.nih.gov/12269834/ · DOI 10.1021/bi026326x

experimental_model

Purified LPO crystallography and activity assays; ammonium iodide supplied the anion, not KI.

exposure_category

Study-specific exposure, including pharmacological and in-vitro conditions; normal is the schema fallback outside the three availability categories.

limitations

Structural/biochemical model; enzyme species not assigned from abstract. Cofactor chemistry does not establish dietary iron responsiveness.

nutrient_topic

Potassium iodide research collection; shared-anion and comparator studies are not all KI interventions. · Potassium iodide

plain_language

Iodide can inhibit the enzyme under a different order of exposure.

primary_references

Structure of a ternary complex of lactoperoxidase with iodide and hydrogen peroxide at 1.77 Å resolution. · 2021 · https://pubmed.ncbi.nlm.nih.gov/33882424/ · DOI 10.1016/j.jinorgbio.2021.111461

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AI-assisted research curation; primary-study references, chemical references and label statements individually identified. Not publisher full text. · supports · Purified LPO crystallography and activity assays; ammonium iodide supplied the anion, not KI. · source_derived_draft · unverified_draft

## ki-lpo-substrate-block Iodide can inhibit the enzyme under a different order of exposure. Preincubating LPO with ammonium iodide decreased measured catalytic activity and stabilized a peroxide–iodide ternary complex. Model: Purified LPO crystallography and activity assays; ammonium iodide supplied the anion, not KI. Limitations: Structural/biochemical model; enzyme species not assigned from abstract. Cofactor chemistry does not establish dietary iron responsiveness. Evidence location: Primary abstract Structure of a ternary complex of lactoperoxidase with iodide and hydrogen peroxide at 1.77 Å resolution. · 2021 · https://pubmed.ncbi.nlm.nih.gov/33882424/ · DOI 10.1016/j.jinorgbio.2021.111461

experimental_model

Cell-free LPO/H2O2 reactions with nicotinamide nucleotides.

exposure_category

Study-specific exposure, including pharmacological and in-vitro conditions; normal is the schema fallback outside the three availability categories.

limitations

Chemical oxidation is not evidence that supplementation drains niacin in vivo; the authors expected thiocyanate oxidation to predominate in milk/saliva.

nutrient_topic

Potassium iodide research collection; shared-anion and comparator studies are not all KI interventions. · Potassium iodide

plain_language

The NADH reaction did not simply regenerate normal NAD+.

primary_references

The oxidation of reduced nicotinamide nucleotides by hydrogen peroside in the presence of lactoperoxidase and thiocyanate, iodide or bromide. · 1970 · https://pubmed.ncbi.nlm.nih.gov/4317722/ · DOI 10.1042/bj1170791

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AI-assisted research curation; primary-study references, chemical references and label statements individually identified. Not publisher full text. · supports · Cell-free LPO/H2O2 reactions with nicotinamide nucleotides. · source_derived_draft · unverified_draft

## ki-nadh The NADH reaction did not simply regenerate normal NAD+. LPO/H2O2/iodide oxidized NADH to a product chemically distinct from NAD+, unlike the thiocyanate and bromide systems. Model: Cell-free LPO/H2O2 reactions with nicotinamide nucleotides. Limitations: Chemical oxidation is not evidence that supplementation drains niacin in vivo; the authors expected thiocyanate oxidation to predominate in milk/saliva. Evidence location: Primary abstract The oxidation of reduced nicotinamide nucleotides by hydrogen peroside in the presence of lactoperoxidase and thiocyanate, iodide or bromide. · 1970 · https://pubmed.ncbi.nlm.nih.gov/4317722/ · DOI 10.1042/bj1170791

experimental_model

Cell-free LPO/H2O2 reactions with nicotinamide nucleotides.

exposure_category

Study-specific exposure, including pharmacological and in-vitro conditions; normal is the schema fallback outside the three availability categories.

limitations

Chemical oxidation is not evidence that supplementation drains niacin in vivo; the authors expected thiocyanate oxidation to predominate in milk/saliva.

nutrient_topic

Potassium iodide research collection; shared-anion and comparator studies are not all KI interventions. · Potassium iodide

plain_language

The chemistry also reaches the NADPH reducing pool.

primary_references

The oxidation of reduced nicotinamide nucleotides by hydrogen peroside in the presence of lactoperoxidase and thiocyanate, iodide or bromide. · 1970 · https://pubmed.ncbi.nlm.nih.gov/4317722/ · DOI 10.1042/bj1170791

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AI-assisted research curation; primary-study references, chemical references and label statements individually identified. Not publisher full text. · supports · Cell-free LPO/H2O2 reactions with nicotinamide nucleotides. · source_derived_draft · unverified_draft

## ki-nadph The chemistry also reaches the NADPH reducing pool. NADPH was also oxidized under the LPO/H2O2/iodide conditions. Model: Cell-free LPO/H2O2 reactions with nicotinamide nucleotides. Limitations: Chemical oxidation is not evidence that supplementation drains niacin in vivo; the authors expected thiocyanate oxidation to predominate in milk/saliva. Evidence location: Primary abstract The oxidation of reduced nicotinamide nucleotides by hydrogen peroside in the presence of lactoperoxidase and thiocyanate, iodide or bromide. · 1970 · https://pubmed.ncbi.nlm.nih.gov/4317722/ · DOI 10.1042/bj1170791

experimental_model

Rose bengal plus 540-nm light; up to 100 mM KI; microbial assays and a mouse skin-abrasion model.

exposure_category

Study-specific exposure, including pharmacological and in-vitro conditions; normal is the schema fallback outside the three availability categories.

limitations

Local photochemical system, not an effect of oral KI alone. Peroxyiodide intermediates were proposed, not directly established.

nutrient_topic

Potassium iodide research collection; shared-anion and comparator studies are not all KI interventions. · Potassium iodide

plain_language

Iodide intercepted singlet oxygen in the photochemical system.

primary_references

Potassium Iodide Potentiates Antimicrobial Photodynamic Inactivation Mediated by Rose Bengal in In Vitro and In Vivo Studies. · 2017 · https://pubmed.ncbi.nlm.nih.gov/28438946/ · DOI 10.1128/aac.00467-17

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AI-assisted research curation; primary-study references, chemical references and label statements individually identified. Not publisher full text. · supports · Rose bengal plus 540-nm light; up to 100 mM KI; microbial assays and a mouse skin-abrasion model. · source_derived_draft · unverified_draft

## ki-pdt-singlet Iodide intercepted singlet oxygen in the photochemical system. KI shortened singlet-oxygen lifetime; derived quenching rate was 1.1 × 10^6 M−1 s−1. Model: Rose bengal plus 540-nm light; up to 100 mM KI; microbial assays and a mouse skin-abrasion model. Limitations: Local photochemical system, not an effect of oral KI alone. Peroxyiodide intermediates were proposed, not directly established. Evidence location: Full-text Figure 5 Potassium Iodide Potentiates Antimicrobial Photodynamic Inactivation Mediated by Rose Bengal in In Vitro and In Vivo Studies. · 2017 · https://pubmed.ncbi.nlm.nih.gov/28438946/ · DOI 10.1128/aac.00467-17

cross_nutrient

false

evidence_span

{"source_cache": "artifacts/iodine-synthesis-sources/2841932.json", "json_field": "abstractText", "text_sha256": "00e19301656f8e8fdb9a047cfa29daf1c66f9a73c84d6c450ff805a6d8b497eb", "text_characters": 1113, "note": "Exact publisher passage retained in the cited local source cache; locator and digest supplied here."}

experimental_model

Dog thyroid slices with iodide, stimulatory probes and methimazole

exposure

Iodide exposure in dog thyroid slices stimulated by thyrotropin, carbamylcholine or intracellular-signaling probes; concentrations not given in abstract.

limitations

Ex-vivo dog tissue; does not identify human DUOX2 as a directly bound molecular target.

nutrient_topic

Iodine research collection; topical membership is not evidence of a direct dietary effect. · Iodine

organism

Canis lupus familiaris

plain_language

Excess iodide can suppress the peroxide supply required for its own incorporation.

primary_references

[iodine-syn-block1988] Inhibition by iodide of iodide binding to proteins: the "Wolff-Chaikoff" effect is caused by inhibition of H2O2 generation. (1988). https://pubmed.ncbi.nlm.nih.gov/2841932/ DOI: 10.1016/0006-291x(88)90279-3

tissue_or_cell_type

Thyroid slices

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AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Dog thyroid slices with iodide, stimulatory probes and methimazole · source_derived_draft · unverified_draft

### iodine-syn-acute-peroxide-block Iodide inhibited stimulated H2O2 generation in dog thyroid slices, including responses to probes acting downstream of receptor activation. Condition category: normal nutrient_topic: Iodine research collection; topical membership is not evidence of a direct dietary effect. plain_language: Excess iodide can suppress the peroxide supply required for its own incorporation. organism: Canis lupus familiaris tissue_or_cell_type: Thyroid slices experimental_model: Dog thyroid slices with iodide, stimulatory probes and methimazole limitations: Ex-vivo dog tissue; does not identify human DUOX2 as a directly bound molecular target. exposure: Iodide exposure in dog thyroid slices stimulated by thyrotropin, carbamylcholine or intracellular-signaling probes; concentrations not given in abstract. cross_nutrient: false evidence_span: {"source_cache": "artifacts/iodine-synthesis-sources/2841932.json", "json_field": "abstractText", "text_sha256": "00e19301656f8e8fdb9a047cfa29daf1c66f9a73c84d6c450ff805a6d8b497eb", "text_characters": 1113, "note": "Exact publisher passage retained in the cited local source cache; locator and digest supplied here."} [iodine-syn-block1988] Inhibition by iodide of iodide binding to proteins: the "Wolff-Chaikoff" effect is caused by inhibition of H2O2 generation. (1988). https://pubmed.ncbi.nlm.nih.gov/2841932/ DOI: 10.1016/0006-291x(88)90279-3

cross_nutrient

false

evidence_span

{"source_cache": "artifacts/iodine-synthesis-sources/32025030.txt", "start_char": 37603, "end_char": 38323, "text_sha256": "dfd7b409d46dbfe4e78cf481b6074477d36d70e14b5731f95a6b99ef0c43b33a", "text_characters": 720, "note": "Exact publisher passage retained in the cited local source cache; locator and digest supplied here."}

experimental_model

Human TG cryo-EM, recombinant HEK293T-expressed TG and site-directed mutants

exposure

0.1 micromolar human TG, 1 mM KI, 24 mM glucose, 2 micrograms/mL glucose oxidase and 3 micrograms/mL lactoperoxidase; 10 minutes at 37 C followed by approximately 2.5 micrograms/mL Pronase and T4 ELISA. Most assays used lactoperoxidase after comparison with human TPO.

limitations

Artificial reaction with lactoperoxidase in most assays; not an intake-response curve.

nutrient_topic

Iodine research collection; topical membership is not evidence of a direct dietary effect. · Iodine

organism

Homo sapiens TG expressed in HEK293T cells

plain_language

Iodide supplies the iodine needed to build T4 on thyroglobulin.

primary_references

[iodine-syn-tg2020] The structure of human thyroglobulin. (2020). https://pubmed.ncbi.nlm.nih.gov/32025030/ DOI: 10.1038/s41586-020-1995-4

tissue_or_cell_type

Purified-protein reaction

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AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human TG cryo-EM, recombinant HEK293T-expressed TG and site-directed mutants · source_derived_draft · unverified_draft

### iodine-syn-tg-iodide-required Recombinant human TG produced a T4 signal after in-vitro iodination and proteolysis, whereas omission of iodide prevented the reaction. Condition category: normal nutrient_topic: Iodine research collection; topical membership is not evidence of a direct dietary effect. plain_language: Iodide supplies the iodine needed to build T4 on thyroglobulin. organism: Homo sapiens TG expressed in HEK293T cells tissue_or_cell_type: Purified-protein reaction experimental_model: Human TG cryo-EM, recombinant HEK293T-expressed TG and site-directed mutants limitations: Artificial reaction with lactoperoxidase in most assays; not an intake-response curve. exposure: 0.1 micromolar human TG, 1 mM KI, 24 mM glucose, 2 micrograms/mL glucose oxidase and 3 micrograms/mL lactoperoxidase; 10 minutes at 37 C followed by approximately 2.5 micrograms/mL Pronase and T4 ELISA. Most assays used lactoperoxidase after comparison with human TPO. cross_nutrient: false evidence_span: {"source_cache": "artifacts/iodine-synthesis-sources/32025030.txt", "start_char": 37603, "end_char": 38323, "text_sha256": "dfd7b409d46dbfe4e78cf481b6074477d36d70e14b5731f95a6b99ef0c43b33a", "text_characters": 720, "note": "Exact publisher passage retained in the cited local source cache; locator and digest supplied here."} [iodine-syn-tg2020] The structure of human thyroglobulin. (2020). https://pubmed.ncbi.nlm.nih.gov/32025030/ DOI: 10.1038/s41586-020-1995-4

experimental_model

Rat thyroid PCCl3 cells; 1 mM NaI unless specified.

exposure_category

Experimental iodide excess; normal is the schema category outside deficiency, machinery impairment and biomarker context.

limitations

Nonpolarized cells; concurrent changes do not establish pendrin necessity, human protection, or an intake threshold.

measurement

Western blot; Figure 1.

nutrient_topic

Iodine · Iodine

primary_references

Calil-Silveira et al. (2016). Iodide excess regulates its own efflux: a possible involvement of pendrin. DOI: 10.1152/ajpcell.00210.2015. https://pubmed.ncbi.nlm.nih.gov/26791486/

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Calil-Silveira et al. (2016). Iodide excess regulates its own efflux: a possible involvement of pendrin. DOI: 10.1152/ajpcell.00210.2015. https://pubmed.ncbi.nlm.nih.gov/26791486/ · supports · Rat thyroid PCCl3 cells; 1 mM NaI unless specified. · source_derived_draft · unverified_draft

## abundance Pendrin abundance increased after 24 hours at 1 mM NaI; lower tested concentrations and 48-hour total abundance showed no significant increase. Measurement: Western blot; Figure 1.

experimental_model

Rat thyroid PCCl3 cells; 1 mM NaI unless specified.

exposure_category

Experimental iodide excess; normal is the schema category outside deficiency, machinery impairment and biomarker context.

limitations

Nonpolarized cells; concurrent changes do not establish pendrin necessity, human protection, or an intake threshold.

measurement

Real-time PCR; Figure 6.

nutrient_topic

Iodine · Iodine

primary_references

Calil-Silveira et al. (2016). Iodide excess regulates its own efflux: a possible involvement of pendrin. DOI: 10.1152/ajpcell.00210.2015. https://pubmed.ncbi.nlm.nih.gov/26791486/

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Calil-Silveira et al. (2016). Iodide excess regulates its own efflux: a possible involvement of pendrin. DOI: 10.1152/ajpcell.00210.2015. https://pubmed.ncbi.nlm.nih.gov/26791486/ · supports · Rat thyroid PCCl3 cells; 1 mM NaI unless specified. · source_derived_draft · unverified_draft

## ano1-null Ano1 mRNA abundance did not significantly change after 24 hours of excess iodide. Measurement: Real-time PCR; Figure 6.

experimental_model

Rat thyroid PCCl3 cells; 1 mM NaI unless specified.

exposure_category

Experimental iodide excess; normal is the schema category outside deficiency, machinery impairment and biomarker context.

limitations

Nonpolarized cells; concurrent changes do not establish pendrin necessity, human protection, or an intake threshold.

measurement

Radioiodide release; perchlorate blocked reuptake; Figure 5B.

nutrient_topic

Iodine · Iodine

primary_references

Calil-Silveira et al. (2016). Iodide excess regulates its own efflux: a possible involvement of pendrin. DOI: 10.1152/ajpcell.00210.2015. https://pubmed.ncbi.nlm.nih.gov/26791486/

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Calil-Silveira et al. (2016). Iodide excess regulates its own efflux: a possible involvement of pendrin. DOI: 10.1152/ajpcell.00210.2015. https://pubmed.ncbi.nlm.nih.gov/26791486/ · supports · Rat thyroid PCCl3 cells; 1 mM NaI unless specified. · source_derived_draft · unverified_draft

## efflux Iodide pretreatment for 12, 24 and 48 hours increased fractional radioiodide efflux despite reduced iodide uptake. Measurement: Radioiodide release; perchlorate blocked reuptake; Figure 5B.

experimental_model

Rat thyroid PCCl3 cells; 1 mM NaI unless specified.

exposure_category

Experimental iodide excess; normal is the schema category outside deficiency, machinery impairment and biomarker context.

limitations

Nonpolarized cells; concurrent changes do not establish pendrin necessity, human protection, or an intake threshold.

measurement

Cycloheximide chase; Figure 4.

nutrient_topic

Iodine · Iodine

primary_references

Calil-Silveira et al. (2016). Iodide excess regulates its own efflux: a possible involvement of pendrin. DOI: 10.1152/ajpcell.00210.2015. https://pubmed.ncbi.nlm.nih.gov/26791486/

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Calil-Silveira et al. (2016). Iodide excess regulates its own efflux: a possible involvement of pendrin. DOI: 10.1152/ajpcell.00210.2015. https://pubmed.ncbi.nlm.nih.gov/26791486/ · supports · Rat thyroid PCCl3 cells; 1 mM NaI unless specified. · source_derived_draft · unverified_draft

## stability Excess iodide slowed pendrin loss during cycloheximide treatment, supporting increased protein stability. Measurement: Cycloheximide chase; Figure 4.

experimental_model

Rat thyroid PCCl3 cells; 1 mM NaI unless specified.

exposure_category

Experimental iodide excess; normal is the schema category outside deficiency, machinery impairment and biomarker context.

limitations

Nonpolarized cells; concurrent changes do not establish pendrin necessity, human protection, or an intake threshold.

measurement

Nonpermeabilized staining; Figures 2–3.

nutrient_topic

Iodine · Iodine

primary_references

Calil-Silveira et al. (2016). Iodide excess regulates its own efflux: a possible involvement of pendrin. DOI: 10.1152/ajpcell.00210.2015. https://pubmed.ncbi.nlm.nih.gov/26791486/

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Calil-Silveira et al. (2016). Iodide excess regulates its own efflux: a possible involvement of pendrin. DOI: 10.1152/ajpcell.00210.2015. https://pubmed.ncbi.nlm.nih.gov/26791486/ · supports · Rat thyroid PCCl3 cells; 1 mM NaI unless specified. · source_derived_draft · unverified_draft

## surface Surface pendrin increased at 24 and 48 hours by flow cytometry; immunofluorescence also detected an increase at 12 hours. Measurement: Nonpermeabilized staining; Figures 2–3.

experimental_model

Chemical formula KI; molar mass 166.0028 g/mol.

exposure_category

Study-specific exposure, including pharmacological and in-vitro conditions; normal is the schema fallback outside the three availability categories.

limitations

Chemical identity, not an efficacy experiment.

nutrient_topic

Potassium iodide research collection; shared-anion and comparator studies are not all KI interventions. · Potassium iodide

plain_language

KI supplies iodide, which follows the existing iodine pathways.

primary_references

NIST Chemistry WebBook: potassium iodide · chemical reference · https://webbook.nist.gov/cgi/cbook.cgi?ID=7681110

Potassium iodide: thyroid and non-thyroid mechanisms, interactions and discovery questions (2026-09-18) · lines 32–38

AI-assisted research curation; primary-study references, chemical references and label statements individually identified. Not publisher full text. · supports · Chemical formula KI; molar mass 166.0028 g/mol. · source_derived_draft · unverified_draft

## ki-iodide KI supplies iodide, which follows the existing iodine pathways. A formula unit of potassium iodide supplies one iodide ion on dissolution. Model: Chemical formula KI; molar mass 166.0028 g/mol. Limitations: Chemical identity, not an efficacy experiment. Evidence location: Primary abstract NIST Chemistry WebBook: potassium iodide · chemical reference · https://webbook.nist.gov/cgi/cbook.cgi?ID=7681110

experimental_model

Chemical formula KI; molar mass 166.0028 g/mol.

exposure_category

Study-specific exposure, including pharmacological and in-vitro conditions; normal is the schema fallback outside the three availability categories.

limitations

Stoichiometric calculation using K 39.0983 and I 126.9045 g/mol; not a dose recommendation.

nutrient_topic

Potassium iodide research collection; shared-anion and comparator studies are not all KI interventions. · Potassium iodide

plain_language

Milligrams of KI are not milligrams of iodine.

primary_references

NIST Chemistry WebBook: potassium iodide · chemical reference · https://webbook.nist.gov/cgi/cbook.cgi?ID=7681110

Potassium iodide: thyroid and non-thyroid mechanisms, interactions and discovery questions (2026-09-18) · lines 48–54

AI-assisted research curation; primary-study references, chemical references and label statements individually identified. Not publisher full text. · supports · Chemical formula KI; molar mass 166.0028 g/mol. · source_derived_draft · unverified_draft

## ki-mass Milligrams of KI are not milligrams of iodine. Calculated from formula masses, KI is about 76.45% iodine and 23.55% potassium by mass; 130 mg KI contains about 99.4 mg iodine and 30.6 mg potassium. Model: Chemical formula KI; molar mass 166.0028 g/mol. Limitations: Stoichiometric calculation using K 39.0983 and I 126.9045 g/mol; not a dose recommendation. Evidence location: Primary abstract NIST Chemistry WebBook: potassium iodide · chemical reference · https://webbook.nist.gov/cgi/cbook.cgi?ID=7681110

cross_nutrient

true

evidence_span

{"source_cache": "artifacts/iodine-synthesis-sources/25395621.txt", "start_char": 11103, "end_char": 12723, "text_sha256": "726c34262182d49a45a4741a29a49ef70bf6d529c79d75cfbb0e9ea59ffd256b", "text_characters": 1620, "note": "Exact publisher passage retained in the cited local source cache; locator and digest supplied here."}

experimental_model

Recombinant human IYD lacking residues 1–31; crystallography, radiotracer kinetics and redox titration

exposure

0–70 micromolar [125I]DIT; sodium dithionite supplies reducing equivalents.

limitations

Anchor-deleted enzyme and artificial reductant; does not identify the physiological electron donor.

nutrient_topic

Iodine research collection; topical membership is not evidence of a direct dietary effect. · Iodine

organism

Homo sapiens recombinant protein

plain_language

IYD recovers iodine from leftover iodinated tyrosine.

primary_references

[iodine-syn-iyd2015] A switch between one- and two-electron chemistry of the human flavoprotein iodotyrosine deiodinase is controlled by substrate. (2015). https://pubmed.ncbi.nlm.nih.gov/25395621/ DOI: 10.1074/jbc.m114.605964

tissue_or_cell_type

Purified soluble IYD

Iodine: thyroid hormone production, deficiency, excess and nutrient interactions (2026-09-17) · lines 688–700

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant human IYD lacking residues 1–31; crystallography, radiotracer kinetics and redox titration · source_derived_draft · unverified_draft

### iodine-syn-iyd-dit-salvage Purified soluble human IYD released radiolabeled iodide from diiodotyrosine during reductive enzyme assays. Condition category: normal nutrient_topic: Iodine research collection; topical membership is not evidence of a direct dietary effect. plain_language: IYD recovers iodine from leftover iodinated tyrosine. organism: Homo sapiens recombinant protein tissue_or_cell_type: Purified soluble IYD experimental_model: Recombinant human IYD lacking residues 1–31; crystallography, radiotracer kinetics and redox titration limitations: Anchor-deleted enzyme and artificial reductant; does not identify the physiological electron donor. exposure: 0–70 micromolar [125I]DIT; sodium dithionite supplies reducing equivalents. cross_nutrient: true evidence_span: {"source_cache": "artifacts/iodine-synthesis-sources/25395621.txt", "start_char": 11103, "end_char": 12723, "text_sha256": "726c34262182d49a45a4741a29a49ef70bf6d529c79d75cfbb0e9ea59ffd256b", "text_characters": 1620, "note": "Exact publisher passage retained in the cited local source cache; locator and digest supplied here."} [iodine-syn-iyd2015] A switch between one- and two-electron chemistry of the human flavoprotein iodotyrosine deiodinase is controlled by substrate. (2015). https://pubmed.ncbi.nlm.nih.gov/25395621/ DOI: 10.1074/jbc.m114.605964

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

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

cross_nutrient

true

experimental_model

Purified tagged unglycosylated rat NIS expressed in human 293F cells; cryo-EM and functional comparison

exposure

Tagged N225Q/N485Q/N497Q rat NIS; iodide-bound structure at 3.12 Å.

limitations

Structural ion assignments and engineered construct support a binding mechanism; they do not alone measure physiological transport rates.

nutrient_topic

Iodine research collection; topical membership is not evidence of a direct dietary effect. · Iodine

organism

Rat protein produced in human 293F cells

plain_language

The NIS structure shows where iodide and its two sodium partners bind.

primary_references

[iodine-trans-nis-structure2022] Structural insights into the mechanism of the sodium/iodide symporter. (2022). https://pubmed.ncbi.nlm.nih.gov/36517601/ DOI: 10.1038/s41586-022-05530-2

tissue_or_cell_type

Purified detergent-solubilized membrane protein

Iodine: thyroid hormone production, deficiency, excess and nutrient interactions (2026-09-17) · lines 193–204

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified tagged unglycosylated rat NIS expressed in human 293F cells; cryo-EM and functional comparison · source_derived_draft · unverified_draft

### iodine-trans-nis-bound-ions The iodide-bound cryo-EM structure of engineered rat NIS contained density assigned to one iodide and two sodium ions in the substrate-binding cavity. Condition category: normal nutrient_topic: Iodine research collection; topical membership is not evidence of a direct dietary effect. plain_language: The NIS structure shows where iodide and its two sodium partners bind. organism: Rat protein produced in human 293F cells tissue_or_cell_type: Purified detergent-solubilized membrane protein experimental_model: Purified tagged unglycosylated rat NIS expressed in human 293F cells; cryo-EM and functional comparison limitations: Structural ion assignments and engineered construct support a binding mechanism; they do not alone measure physiological transport rates. exposure: Tagged N225Q/N485Q/N497Q rat NIS; iodide-bound structure at 3.12 Å. cross_nutrient: true [iodine-trans-nis-structure2022] Structural insights into the mechanism of the sodium/iodide symporter. (2022). https://pubmed.ncbi.nlm.nih.gov/36517601/ DOI: 10.1038/s41586-022-05530-2

evidence_access

Primary abstract

experimental_model

Human TG and engineered bacterial maltose-binding-protein hormone-production assays.

limitations

The engineered bacterial scaffold is an in vitro demonstration, not a physiological human alternative.

nutrient_topic

L-Tyrosine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Tyrosine

plain_language

Having the building blocks is not enough; their arrangement matters.

primary_references

The structure of human thyroglobulin. · 2020 · https://pubmed.ncbi.nlm.nih.gov/32025030/ · DOI 10.1038/s41586-020-1995-4

L-Tyrosine: catecholamines, thyroid chemistry, pigment, metabolism and cross-nutrient mechanisms (2026-09-19) · lines 140–146

AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human TG and engineered bacterial maltose-binding-protein hormone-production assays. · source_derived_draft · unverified_draft

## l-tyrosine-tg-geometry Having the building blocks is not enough; their arrangement matters. Mutational and engineered-scaffold experiments implicated tyrosine proximity, flexibility and solvent exposure in hormone formation. Model: Human TG and engineered bacterial maltose-binding-protein hormone-production assays. Limitations: The engineered bacterial scaffold is an in vitro demonstration, not a physiological human alternative. Evidence access: Primary abstract The structure of human thyroglobulin. · 2020 · https://pubmed.ncbi.nlm.nih.gov/32025030/ · DOI 10.1038/s41586-020-1995-4

evidence_access

Primary abstract

experimental_model

Human TG expressed in HEK293T cells; cryo-EM and in vitro hormone assays.

limitations

This does not mean free tyrosine is directly iodinated into circulating thyroid hormone.

nutrient_topic

L-Tyrosine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Tyrosine

plain_language

The thyroid uses selected tyrosines already built into a protein.

primary_references

The structure of human thyroglobulin. · 2020 · https://pubmed.ncbi.nlm.nih.gov/32025030/ · DOI 10.1038/s41586-020-1995-4

L-Tyrosine: catecholamines, thyroid chemistry, pigment, metabolism and cross-nutrient mechanisms (2026-09-19) · lines 132–138

AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human TG expressed in HEK293T cells; cryo-EM and in vitro hormone assays. · source_derived_draft · unverified_draft

## l-tyrosine-tg-iodinated-pairs The thyroid uses selected tyrosines already built into a protein. Human thyroglobulin cryo-EM and site-directed mutagenesis identified tyrosine donor-acceptor pairs supporting hormone formation in vitro. Model: Human TG expressed in HEK293T cells; cryo-EM and in vitro hormone assays. Limitations: This does not mean free tyrosine is directly iodinated into circulating thyroid hormone. Evidence access: Primary abstract The structure of human thyroglobulin. · 2020 · https://pubmed.ncbi.nlm.nih.gov/32025030/ · DOI 10.1038/s41586-020-1995-4

experimental_model

Primary airway epithelial cultures and human oral-KI exposure; separate experimental arms.

exposure_category

Study-specific exposure, including pharmacological and in-vitro conditions; normal is the schema fallback outside the three availability categories.

limitations

Culture antiviral activity and human secretion measurements do not establish prevention or treatment of human infection.

nutrient_topic

Potassium iodide research collection; shared-anion and comparator studies are not all KI interventions. · Potassium iodide

plain_language

Airway cells supplied the oxidant needed by the enzyme.

primary_references

Enhancement of respiratory mucosal antiviral defenses by the oxidation of iodide. · 2011 · https://pubmed.ncbi.nlm.nih.gov/21441383/ · DOI 10.1165/rcmb.2010-0329oc

Potassium iodide: thyroid and non-thyroid mechanisms, interactions and discovery questions (2026-09-18) · lines 88–94

AI-assisted research curation; primary-study references, chemical references and label statements individually identified. Not publisher full text. · supports · Primary airway epithelial cultures and human oral-KI exposure; separate experimental arms. · source_derived_draft · unverified_draft

## ki-air-peroxide Airway cells supplied the oxidant needed by the enzyme. Differentiated airway epithelia supplied sufficient peroxide for antiviral activity when LPO and iodide were added. Model: Primary airway epithelial cultures and human oral-KI exposure; separate experimental arms. Limitations: Culture antiviral activity and human secretion measurements do not establish prevention or treatment of human infection. Evidence location: Primary abstract Enhancement of respiratory mucosal antiviral defenses by the oxidation of iodide. · 2011 · https://pubmed.ncbi.nlm.nih.gov/21441383/ · DOI 10.1165/rcmb.2010-0329oc

experimental_model

Purified LPO crystallography and activity assays; ammonium iodide supplied the anion, not KI.

exposure_category

Study-specific exposure, including pharmacological and in-vitro conditions; normal is the schema fallback outside the three availability categories.

limitations

Structural/biochemical model; enzyme species not assigned from abstract. Cofactor chemistry does not establish dietary iron responsiveness.

nutrient_topic

Potassium iodide research collection; shared-anion and comparator studies are not all KI interventions. · Potassium iodide

plain_language

The oxidized iodine product was observed structurally.

primary_references

Structural evidence of the oxidation of iodide ion into hyper-reactive hypoiodite ion by mammalian heme lactoperoxidase. · 2022 · https://pubmed.ncbi.nlm.nih.gov/34761444/ · DOI 10.1002/pro.4230

Potassium iodide: thyroid and non-thyroid mechanisms, interactions and discovery questions (2026-09-18) · lines 232–238

AI-assisted research curation; primary-study references, chemical references and label statements individually identified. Not publisher full text. · supports · Purified LPO crystallography and activity assays; ammonium iodide supplied the anion, not KI. · source_derived_draft · unverified_draft

## ki-lpo-product The oxidized iodine product was observed structurally. Peroxide-preincubated LPO exposed to iodide yielded a crystal complex containing hypoiodite in its substrate channel. Model: Purified LPO crystallography and activity assays; ammonium iodide supplied the anion, not KI. Limitations: Structural/biochemical model; enzyme species not assigned from abstract. Cofactor chemistry does not establish dietary iron responsiveness. Evidence location: Primary abstract Structural evidence of the oxidation of iodide ion into hyper-reactive hypoiodite ion by mammalian heme lactoperoxidase. · 2022 · https://pubmed.ncbi.nlm.nih.gov/34761444/ · DOI 10.1002/pro.4230

cross_nutrient

false

evidence_span

{"source_cache": "artifacts/iodine-synthesis-sources/2841932.json", "json_field": "abstractText", "text_sha256": "00e19301656f8e8fdb9a047cfa29daf1c66f9a73c84d6c450ff805a6d8b497eb", "text_characters": 1113, "note": "Exact publisher passage retained in the cited local source cache; locator and digest supplied here."}

experimental_model

Dog thyroid slices with iodide, stimulatory probes and methimazole

exposure

Iodide exposure in dog thyroid slices stimulated by thyrotropin, carbamylcholine or intracellular-signaling probes; concentrations not given in abstract. Methimazole coexposure.

limitations

Pharmacological probe supports oxidation dependence; the inhibitory iodinated species was not identified.

nutrient_topic

Iodine research collection; topical membership is not evidence of a direct dietary effect. · Iodine

organism

Canis lupus familiaris

plain_language

Preventing iodide oxidation blocked this feedback effect in thyroid tissue.

primary_references

[iodine-syn-block1988] Inhibition by iodide of iodide binding to proteins: the "Wolff-Chaikoff" effect is caused by inhibition of H2O2 generation. (1988). https://pubmed.ncbi.nlm.nih.gov/2841932/ DOI: 10.1016/0006-291x(88)90279-3

tissue_or_cell_type

Thyroid slices

Iodine: thyroid hormone production, deficiency, excess and nutrient interactions (2026-09-17) · lines 814–826

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Dog thyroid slices with iodide, stimulatory probes and methimazole · source_derived_draft · unverified_draft

### iodine-syn-acute-block-oxidation Methimazole suppressed the inhibitory effects of iodide on stimulated H2O2 generation in dog thyroid slices. Condition category: normal nutrient_topic: Iodine research collection; topical membership is not evidence of a direct dietary effect. plain_language: Preventing iodide oxidation blocked this feedback effect in thyroid tissue. organism: Canis lupus familiaris tissue_or_cell_type: Thyroid slices experimental_model: Dog thyroid slices with iodide, stimulatory probes and methimazole limitations: Pharmacological probe supports oxidation dependence; the inhibitory iodinated species was not identified. exposure: Iodide exposure in dog thyroid slices stimulated by thyrotropin, carbamylcholine or intracellular-signaling probes; concentrations not given in abstract. Methimazole coexposure. cross_nutrient: false evidence_span: {"source_cache": "artifacts/iodine-synthesis-sources/2841932.json", "json_field": "abstractText", "text_sha256": "00e19301656f8e8fdb9a047cfa29daf1c66f9a73c84d6c450ff805a6d8b497eb", "text_characters": 1113, "note": "Exact publisher passage retained in the cited local source cache; locator and digest supplied here."} [iodine-syn-block1988] Inhibition by iodide of iodide binding to proteins: the "Wolff-Chaikoff" effect is caused by inhibition of H2O2 generation. (1988). https://pubmed.ncbi.nlm.nih.gov/2841932/ DOI: 10.1016/0006-291x(88)90279-3

availability_state

machinery_impairment Imported condition classification; unverified.

cross_nutrient

false

evidence_span

{"source_cache": "artifacts/iodine-synthesis-sources/12110737.json", "json_field": "abstractText", "text_sha256": "a0fa87eb7c584eb2b54cdc1de43ef65dd31bb4b7300f06c5b9ff4a8f703a151e", "text_characters": 1953, "note": "Exact publisher passage retained in the cited local source cache; locator and digest supplied here."}

experimental_model

Sequencing of nine newborn-screened patients with iodide-organification defects and their relatives

exposure

Inherited DUOX2 truncation; no imposed dietary iodine restriction.

limitations

Small selected genetic series; no universal genotype-to-prognosis rule.

nutrient_topic

Iodine research collection; topical membership is not evidence of a direct dietary effect. · Iodine

organism

Homo sapiens

plain_language

A broken peroxide generator can prevent iodine from being incorporated into thyroid proteins.

primary_references

[iodine-syn-duox2002] Inactivating mutations in the gene for thyroid oxidase 2 (THOX2) and congenital hypothyroidism. (2002). https://pubmed.ncbi.nlm.nih.gov/12110737/ DOI: 10.1056/nejmoa012752

tissue_or_cell_type

Thyroid

trigger_kind

machinery_impairment Imported condition classification; unverified.

Iodine: thyroid hormone production, deficiency, excess and nutrient interactions (2026-09-17) · lines 520–532

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Sequencing of nine newborn-screened patients with iodide-organification defects and their relatives · source_derived_draft · unverified_draft

### iodine-syn-duox2-organification A homozygous truncating DUOX2 mutation accompanied a complete iodide-organification defect in the severe permanent case in the 2002 series. Condition category: machinery_impairment nutrient_topic: Iodine research collection; topical membership is not evidence of a direct dietary effect. plain_language: A broken peroxide generator can prevent iodine from being incorporated into thyroid proteins. organism: Homo sapiens tissue_or_cell_type: Thyroid experimental_model: Sequencing of nine newborn-screened patients with iodide-organification defects and their relatives limitations: Small selected genetic series; no universal genotype-to-prognosis rule. exposure: Inherited DUOX2 truncation; no imposed dietary iodine restriction. cross_nutrient: false evidence_span: {"source_cache": "artifacts/iodine-synthesis-sources/12110737.json", "json_field": "abstractText", "text_sha256": "a0fa87eb7c584eb2b54cdc1de43ef65dd31bb4b7300f06c5b9ff4a8f703a151e", "text_characters": 1953, "note": "Exact publisher passage retained in the cited local source cache; locator and digest supplied here."} [iodine-syn-duox2002] Inactivating mutations in the gene for thyroid oxidase 2 (THOX2) and congenital hypothyroidism. (2002). https://pubmed.ncbi.nlm.nih.gov/12110737/ DOI: 10.1056/nejmoa012752

availability_state

machinery_impairment Imported condition classification; unverified.

cross_nutrient

false

evidence_span

{"source_cache": "artifacts/iodine-synthesis-sources/18042646.json", "json_field": "abstractText", "text_sha256": "99a0667a0a4036b9ad94f59e6ba82a4c80c7f4b4228f11029f63db5c5b811da7", "text_characters": 1847, "note": "Exact publisher passage retained in the cited local source cache; locator and digest supplied here."}

experimental_model

Human genetic case finding and heterologous DUOX2 reconstitution

exposure

Inherited homozygous Y246X; no dietary manipulation.

limitations

Single proband; heterozygotes in the family were euthyroid.

nutrient_topic

Iodine research collection; topical membership is not evidence of a direct dietary effect. · Iodine

organism

Homo sapiens

plain_language

The enzyme-helper defect was linked to impaired hormone production from birth.

primary_references

[iodine-syn-duoxa2008] Biallelic inactivation of the dual oxidase maturation factor 2 (DUOXA2) gene as a novel cause of congenital hypothyroidism. (2008). https://pubmed.ncbi.nlm.nih.gov/18042646/ DOI: 10.1210/jc.2007-2020

tissue_or_cell_type

Thyroid

trigger_kind

machinery_impairment Imported condition classification; unverified.

Iodine: thyroid hormone production, deficiency, excess and nutrient interactions (2026-09-17) · lines 548–560

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human genetic case finding and heterologous DUOX2 reconstitution · source_derived_draft · unverified_draft

### iodine-syn-duoxa-mutant-phenotype The homozygous DUOXA2 Y246X proband had congenital hypothyroidism with goiter and partial iodine-organification impairment. Condition category: machinery_impairment nutrient_topic: Iodine research collection; topical membership is not evidence of a direct dietary effect. plain_language: The enzyme-helper defect was linked to impaired hormone production from birth. organism: Homo sapiens tissue_or_cell_type: Thyroid experimental_model: Human genetic case finding and heterologous DUOX2 reconstitution limitations: Single proband; heterozygotes in the family were euthyroid. exposure: Inherited homozygous Y246X; no dietary manipulation. cross_nutrient: false evidence_span: {"source_cache": "artifacts/iodine-synthesis-sources/18042646.json", "json_field": "abstractText", "text_sha256": "99a0667a0a4036b9ad94f59e6ba82a4c80c7f4b4228f11029f63db5c5b811da7", "text_characters": 1847, "note": "Exact publisher passage retained in the cited local source cache; locator and digest supplied here."} [iodine-syn-duoxa2008] Biallelic inactivation of the dual oxidase maturation factor 2 (DUOXA2) gene as a novel cause of congenital hypothyroidism. (2008). https://pubmed.ncbi.nlm.nih.gov/18042646/ DOI: 10.1210/jc.2007-2020

cross_nutrient

false

evidence_span

{"source_cache": "artifacts/iodine-synthesis-sources/10433193.json", "json_field": "abstractText", "text_sha256": "edf82df926d65731111d3f6b8005965a95e9928421170aa4cb5cef0709adc924", "text_characters": 2339, "note": "Exact publisher passage retained in the cited local source cache; locator and digest supplied here."}

experimental_model

Rat oral and intraperitoneal sodium iodide experiments

exposure

0.05% sodium iodide in drinking water for 1 or 6 days.

limitations

Rodent pharmacological exposure; recovery time and susceptibility cannot be imposed on humans.

nutrient_topic

Iodine research collection; topical membership is not evidence of a direct dietary effect. · Iodine

organism

Rattus norvegicus

plain_language

The initial hormone suppression wore off despite continued high iodide exposure.

primary_references

[iodine-syn-escape1999] Escape from the acute Wolff-Chaikoff effect is associated with a decrease in thyroid sodium/iodide symporter messenger ribonucleic acid and protein. (1999). https://pubmed.ncbi.nlm.nih.gov/10433193/ DOI: 10.1210/endo.140.8.6893

tissue_or_cell_type

Serum

Iodine: thyroid hormone production, deficiency, excess and nutrient interactions (2026-09-17) · lines 786–798

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Rat oral and intraperitoneal sodium iodide experiments · source_derived_draft · unverified_draft

### iodine-syn-escape-hormone-recovery During continued 0.05% NaI exposure, rat serum T4 and T3 fell at day 1 but returned to normal by day 6. Condition category: normal nutrient_topic: Iodine research collection; topical membership is not evidence of a direct dietary effect. plain_language: The initial hormone suppression wore off despite continued high iodide exposure. organism: Rattus norvegicus tissue_or_cell_type: Serum experimental_model: Rat oral and intraperitoneal sodium iodide experiments limitations: Rodent pharmacological exposure; recovery time and susceptibility cannot be imposed on humans. exposure: 0.05% sodium iodide in drinking water for 1 or 6 days. cross_nutrient: false evidence_span: {"source_cache": "artifacts/iodine-synthesis-sources/10433193.json", "json_field": "abstractText", "text_sha256": "edf82df926d65731111d3f6b8005965a95e9928421170aa4cb5cef0709adc924", "text_characters": 2339, "note": "Exact publisher passage retained in the cited local source cache; locator and digest supplied here."} [iodine-syn-escape1999] Escape from the acute Wolff-Chaikoff effect is associated with a decrease in thyroid sodium/iodide symporter messenger ribonucleic acid and protein. (1999). https://pubmed.ncbi.nlm.nih.gov/10433193/ DOI: 10.1210/endo.140.8.6893

cross_nutrient

false

evidence_span

{"source_cache": "artifacts/iodine-synthesis-sources/10433193.json", "json_field": "abstractText", "text_sha256": "edf82df926d65731111d3f6b8005965a95e9928421170aa4cb5cef0709adc924", "text_characters": 2339, "note": "Exact publisher passage retained in the cited local source cache; locator and digest supplied here."}

experimental_model

Rat oral and intraperitoneal sodium iodide experiments

exposure

0.05% sodium iodide in drinking water for 1 or 6 days.

limitations

Expression data support an escape mechanism but do not independently prove NIS reduction sufficient for escape.

nutrient_topic

Iodine research collection; topical membership is not evidence of a direct dietary effect. · Iodine

organism

Rattus norvegicus

plain_language

Sustained excess iodide reduced the thyroid uptake machinery in rats.

primary_references

[iodine-syn-escape1999] Escape from the acute Wolff-Chaikoff effect is associated with a decrease in thyroid sodium/iodide symporter messenger ribonucleic acid and protein. (1999). https://pubmed.ncbi.nlm.nih.gov/10433193/ DOI: 10.1210/endo.140.8.6893

tissue_or_cell_type

Thyroid

Iodine: thyroid hormone production, deficiency, excess and nutrient interactions (2026-09-17) · lines 772–784

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Rat oral and intraperitoneal sodium iodide experiments · source_derived_draft · unverified_draft

### iodine-syn-escape-nis Rats given 0.05% NaI in drinking water had lower thyroid NIS mRNA and protein at both 1 and 6 days. Condition category: normal nutrient_topic: Iodine research collection; topical membership is not evidence of a direct dietary effect. plain_language: Sustained excess iodide reduced the thyroid uptake machinery in rats. organism: Rattus norvegicus tissue_or_cell_type: Thyroid experimental_model: Rat oral and intraperitoneal sodium iodide experiments limitations: Expression data support an escape mechanism but do not independently prove NIS reduction sufficient for escape. exposure: 0.05% sodium iodide in drinking water for 1 or 6 days. cross_nutrient: false evidence_span: {"source_cache": "artifacts/iodine-synthesis-sources/10433193.json", "json_field": "abstractText", "text_sha256": "edf82df926d65731111d3f6b8005965a95e9928421170aa4cb5cef0709adc924", "text_characters": 2339, "note": "Exact publisher passage retained in the cited local source cache; locator and digest supplied here."} [iodine-syn-escape1999] Escape from the acute Wolff-Chaikoff effect is associated with a decrease in thyroid sodium/iodide symporter messenger ribonucleic acid and protein. (1999). https://pubmed.ncbi.nlm.nih.gov/10433193/ DOI: 10.1210/endo.140.8.6893

cross_nutrient

true

evidence_span

{"source_cache": "artifacts/iodine-synthesis-sources/32025030.txt", "start_char": 37661, "end_char": 38631, "text_sha256": "edbab2cbd62ebd263ef59f543f10aad3692d3a3983ef5abad904e697ea34ca04", "text_characters": 970, "note": "Exact publisher passage retained in the cited local source cache; locator and digest supplied here."}

experimental_model

Human TG cryo-EM, recombinant HEK293T-expressed TG and site-directed mutants

exposure

Extended Data Fig.6c: 0.1 micromolar TG, 1 mM KI, glucose/glucose oxidase peroxide supply, 10 minutes at 37 C; TPO added at fivefold the LPO concentration to compensate for approximately 20% heme occupancy; T4 measured after Pronase digestion.

limitations

This identifies the TPO-containing assay arm; most TG mutagenesis experiments used LPO. The measured T4 was liberated by assay proteolysis after formation on TG.

nutrient_topic

Iodine research collection; topical membership is not evidence of a direct dietary effect. · Iodine

organism

Homo sapiens TG and TPO; HEK293T TG expression and insect-cell TPO expression

plain_language

Human TPO can drive hormone formation on human thyroglobulin.

primary_references

[iodine-syn-tg2020] The structure of human thyroglobulin. (2020). https://pubmed.ncbi.nlm.nih.gov/32025030/ DOI: 10.1038/s41586-020-1995-4

tissue_or_cell_type

Purified-protein reconstitution

Iodine: thyroid hormone production, deficiency, excess and nutrient interactions (2026-09-17) · lines 842–854

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human TG cryo-EM, recombinant HEK293T-expressed TG and site-directed mutants · source_derived_draft · unverified_draft

### iodine-syn-human-tpo-t4-synthesis Recombinant human TPO catalyzed T4 formation from recombinant human TG in the direct TPO-versus-lactoperoxidase comparison. Condition category: normal nutrient_topic: Iodine research collection; topical membership is not evidence of a direct dietary effect. plain_language: Human TPO can drive hormone formation on human thyroglobulin. organism: Homo sapiens TG and TPO; HEK293T TG expression and insect-cell TPO expression tissue_or_cell_type: Purified-protein reconstitution experimental_model: Human TG cryo-EM, recombinant HEK293T-expressed TG and site-directed mutants limitations: This identifies the TPO-containing assay arm; most TG mutagenesis experiments used LPO. The measured T4 was liberated by assay proteolysis after formation on TG. exposure: Extended Data Fig.6c: 0.1 micromolar TG, 1 mM KI, glucose/glucose oxidase peroxide supply, 10 minutes at 37 C; TPO added at fivefold the LPO concentration to compensate for approximately 20% heme occupancy; T4 measured after Pronase digestion. cross_nutrient: true evidence_span: {"source_cache": "artifacts/iodine-synthesis-sources/32025030.txt", "start_char": 37661, "end_char": 38631, "text_sha256": "edbab2cbd62ebd263ef59f543f10aad3692d3a3983ef5abad904e697ea34ca04", "text_characters": 970, "note": "Exact publisher passage retained in the cited local source cache; locator and digest supplied here."} [iodine-syn-tg2020] The structure of human thyroglobulin. (2020). https://pubmed.ncbi.nlm.nih.gov/32025030/ DOI: 10.1038/s41586-020-1995-4

availability_state

machinery_impairment Imported condition classification; unverified.

cross_nutrient

true

evidence_span

{"source_cache": "artifacts/iodine-synthesis-sources/18434651.json", "json_field": "abstractText", "text_sha256": "f257956854445e268691cd3df1388ca16cea3f41320a48753df200a381c56431", "text_characters": 914, "note": "Exact publisher passage retained in the cited local source cache; locator and digest supplied here."}

experimental_model

Four selected patients from three unrelated families plus in-vitro mutant enzyme assays

exposure

Two missense variants and one three-base-pair deletion; no nutrient-restriction experiment.

limitations

Abstract does not provide exact variant residues or assay dose.

nutrient_topic

Iodine research collection; topical membership is not evidence of a direct dietary effect. · Iodine

organism

Homo sapiens proteins

plain_language

Genetic defects can disable iodine recycling.

primary_references

[iodine-syn-iyd2008] Mutations in the iodotyrosine deiodinase gene and hypothyroidism. (2008). https://pubmed.ncbi.nlm.nih.gov/18434651/ DOI: 10.1056/nejmoa0706819

tissue_or_cell_type

In-vitro enzyme assays

trigger_kind

machinery_impairment Imported condition classification; unverified.

Iodine: thyroid hormone production, deficiency, excess and nutrient interactions (2026-09-17) · lines 744–756

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Four selected patients from three unrelated families plus in-vitro mutant enzyme assays · source_derived_draft · unverified_draft

### iodine-syn-iyd-mutant-activity The IYD variants identified in four affected patients showed markedly reduced iodotyrosine-deiodinase activity in vitro. Condition category: machinery_impairment nutrient_topic: Iodine research collection; topical membership is not evidence of a direct dietary effect. plain_language: Genetic defects can disable iodine recycling. organism: Homo sapiens proteins tissue_or_cell_type: In-vitro enzyme assays experimental_model: Four selected patients from three unrelated families plus in-vitro mutant enzyme assays limitations: Abstract does not provide exact variant residues or assay dose. exposure: Two missense variants and one three-base-pair deletion; no nutrient-restriction experiment. cross_nutrient: true evidence_span: {"source_cache": "artifacts/iodine-synthesis-sources/18434651.json", "json_field": "abstractText", "text_sha256": "f257956854445e268691cd3df1388ca16cea3f41320a48753df200a381c56431", "text_characters": 914, "note": "Exact publisher passage retained in the cited local source cache; locator and digest supplied here."} [iodine-syn-iyd2008] Mutations in the iodotyrosine deiodinase gene and hypothyroidism. (2008). https://pubmed.ncbi.nlm.nih.gov/18434651/ DOI: 10.1056/nejmoa0706819

availability_state

machinery_impairment Imported condition classification; unverified.

cross_nutrient

false

evidence_span

{"source_cache": "artifacts/iodine-synthesis-sources/18434651.json", "json_field": "abstractText", "text_sha256": "f257956854445e268691cd3df1388ca16cea3f41320a48753df200a381c56431", "text_characters": 914, "note": "Exact publisher passage retained in the cited local source cache; locator and digest supplied here."}

experimental_model

Four selected patients from three unrelated families plus in-vitro mutant enzyme assays

exposure

Inherited enzyme variants in three unrelated families.

limitations

Selected cases; does not establish dietary deficiency or population prevalence.

nutrient_topic

Iodine research collection; topical membership is not evidence of a direct dietary effect. · Iodine

organism

Homo sapiens

plain_language

Failure to recycle iodine can impair hormone production after birth.

primary_references

[iodine-syn-iyd2008] Mutations in the iodotyrosine deiodinase gene and hypothyroidism. (2008). https://pubmed.ncbi.nlm.nih.gov/18434651/ DOI: 10.1056/nejmoa0706819

tissue_or_cell_type

Thyroid and systemic thyroid function

trigger_kind

machinery_impairment Imported condition classification; unverified.

Iodine: thyroid hormone production, deficiency, excess and nutrient interactions (2026-09-17) · lines 758–770

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Four selected patients from three unrelated families plus in-vitro mutant enzyme assays · source_derived_draft · unverified_draft

### iodine-syn-iyd-mutant-phenotype The four patients with damaging IYD variants developed severe goitrous hypothyroidism evident in infancy or childhood. Condition category: machinery_impairment nutrient_topic: Iodine research collection; topical membership is not evidence of a direct dietary effect. plain_language: Failure to recycle iodine can impair hormone production after birth. organism: Homo sapiens tissue_or_cell_type: Thyroid and systemic thyroid function experimental_model: Four selected patients from three unrelated families plus in-vitro mutant enzyme assays limitations: Selected cases; does not establish dietary deficiency or population prevalence. exposure: Inherited enzyme variants in three unrelated families. cross_nutrient: false evidence_span: {"source_cache": "artifacts/iodine-synthesis-sources/18434651.json", "json_field": "abstractText", "text_sha256": "f257956854445e268691cd3df1388ca16cea3f41320a48753df200a381c56431", "text_characters": 914, "note": "Exact publisher passage retained in the cited local source cache; locator and digest supplied here."} [iodine-syn-iyd2008] Mutations in the iodotyrosine deiodinase gene and hypothyroidism. (2008). https://pubmed.ncbi.nlm.nih.gov/18434651/ DOI: 10.1056/nejmoa0706819

cross_nutrient

false

evidence_span

{"source_cache": "artifacts/iodine-synthesis-sources/32025030.txt", "start_char": 8677, "end_char": 9897, "text_sha256": "fcdc18c2b096fdd24073329828fe9c6681e101b7f29bf985938e538faf6fb3fe", "text_characters": 1220, "note": "Exact publisher passage retained in the cited local source cache; locator and digest supplied here."}

experimental_model

Human TG cryo-EM, recombinant HEK293T-expressed TG and site-directed mutants

exposure

0.1 micromolar human TG, 1 mM KI, 24 mM glucose, 2 micrograms/mL glucose oxidase and 3 micrograms/mL lactoperoxidase; 10 minutes at 37 C followed by approximately 2.5 micrograms/mL Pronase and T4 ELISA. Most assays used lactoperoxidase after comparison with human TPO. Four acceptor substitutions.

limitations

Engineered multi-site mutant; no human congenital phenotype inferred.

nutrient_topic

Iodine research collection; topical membership is not evidence of a direct dietary effect. · Iodine

organism

Homo sapiens TG

plain_language

Four hormone-forming acceptor sites account for the measured T4 production.

primary_references

[iodine-syn-tg2020] The structure of human thyroglobulin. (2020). https://pubmed.ncbi.nlm.nih.gov/32025030/ DOI: 10.1038/s41586-020-1995-4

tissue_or_cell_type

Purified-protein reaction

Iodine: thyroid hormone production, deficiency, excess and nutrient interactions (2026-09-17) · lines 632–644

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human TG cryo-EM, recombinant HEK293T-expressed TG and site-directed mutants · source_derived_draft · unverified_draft

### iodine-syn-tg-acceptor-mutants Replacing human TG acceptors Y24, Y2573, Y2766 and Y1310 with phenylalanine eliminated detectable T4 formation in the reconstituted assay. Condition category: normal nutrient_topic: Iodine research collection; topical membership is not evidence of a direct dietary effect. plain_language: Four hormone-forming acceptor sites account for the measured T4 production. organism: Homo sapiens TG tissue_or_cell_type: Purified-protein reaction experimental_model: Human TG cryo-EM, recombinant HEK293T-expressed TG and site-directed mutants limitations: Engineered multi-site mutant; no human congenital phenotype inferred. exposure: 0.1 micromolar human TG, 1 mM KI, 24 mM glucose, 2 micrograms/mL glucose oxidase and 3 micrograms/mL lactoperoxidase; 10 minutes at 37 C followed by approximately 2.5 micrograms/mL Pronase and T4 ELISA. Most assays used lactoperoxidase after comparison with human TPO. Four acceptor substitutions. cross_nutrient: false evidence_span: {"source_cache": "artifacts/iodine-synthesis-sources/32025030.txt", "start_char": 8677, "end_char": 9897, "text_sha256": "fcdc18c2b096fdd24073329828fe9c6681e101b7f29bf985938e538faf6fb3fe", "text_characters": 1220, "note": "Exact publisher passage retained in the cited local source cache; locator and digest supplied here."} [iodine-syn-tg2020] The structure of human thyroglobulin. (2020). https://pubmed.ncbi.nlm.nih.gov/32025030/ DOI: 10.1038/s41586-020-1995-4

cross_nutrient

false

evidence_span

{"source_cache": "artifacts/iodine-synthesis-sources/32025030.txt", "start_char": 9120, "end_char": 9940, "text_sha256": "8b8cd3eb09e3950bb40977268ed2a95e242386b632a9d45ccd8a2e156aead2b1", "text_characters": 820, "note": "Exact publisher passage retained in the cited local source cache; locator and digest supplied here."}

experimental_model

Human TG cryo-EM, recombinant HEK293T-expressed TG and site-directed mutants

exposure

0.1 micromolar human TG, 1 mM KI, 24 mM glucose, 2 micrograms/mL glucose oxidase and 3 micrograms/mL lactoperoxidase; 10 minutes at 37 C followed by approximately 2.5 micrograms/mL Pronase and T4 ELISA. Most assays used lactoperoxidase after comparison with human TPO. Five donor substitutions.

limitations

Multi-site mutagenesis supports the donor set; not an isolated rate for every individual site.

nutrient_topic

Iodine research collection; topical membership is not evidence of a direct dietary effect. · Iodine

organism

Homo sapiens TG

plain_language

The paired donor tyrosines are also needed to assemble T4.

primary_references

[iodine-syn-tg2020] The structure of human thyroglobulin. (2020). https://pubmed.ncbi.nlm.nih.gov/32025030/ DOI: 10.1038/s41586-020-1995-4

tissue_or_cell_type

Purified-protein reaction

Iodine: thyroid hormone production, deficiency, excess and nutrient interactions (2026-09-17) · lines 646–658

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human TG cryo-EM, recombinant HEK293T-expressed TG and site-directed mutants · source_derived_draft · unverified_draft

### iodine-syn-tg-donor-mutants Replacing human TG donor residues Y2540, Y2766, Y108, Y234 and Y149 with phenylalanine suppressed significant T4 synthesis. Condition category: normal nutrient_topic: Iodine research collection; topical membership is not evidence of a direct dietary effect. plain_language: The paired donor tyrosines are also needed to assemble T4. organism: Homo sapiens TG tissue_or_cell_type: Purified-protein reaction experimental_model: Human TG cryo-EM, recombinant HEK293T-expressed TG and site-directed mutants limitations: Multi-site mutagenesis supports the donor set; not an isolated rate for every individual site. exposure: 0.1 micromolar human TG, 1 mM KI, 24 mM glucose, 2 micrograms/mL glucose oxidase and 3 micrograms/mL lactoperoxidase; 10 minutes at 37 C followed by approximately 2.5 micrograms/mL Pronase and T4 ELISA. Most assays used lactoperoxidase after comparison with human TPO. Five donor substitutions. cross_nutrient: false evidence_span: {"source_cache": "artifacts/iodine-synthesis-sources/32025030.txt", "start_char": 9120, "end_char": 9940, "text_sha256": "8b8cd3eb09e3950bb40977268ed2a95e242386b632a9d45ccd8a2e156aead2b1", "text_characters": 820, "note": "Exact publisher passage retained in the cited local source cache; locator and digest supplied here."} [iodine-syn-tg2020] The structure of human thyroglobulin. (2020). https://pubmed.ncbi.nlm.nih.gov/32025030/ DOI: 10.1038/s41586-020-1995-4

cross_nutrient

false

evidence_span

{"source_cache": "artifacts/iodine-synthesis-sources/6706940.json", "json_field": "abstractText", "text_sha256": "e7d184d64b66b0dc89f61c511688c79ffc9785b20233e7746ef4c97de351c78c", "text_characters": 1442, "note": "Exact publisher passage retained in the cited local source cache; locator and digest supplied here."}

experimental_model

Purified hog thyroid peroxidase with hog thyroglobulin; steady-state and stopped-flow kinetics

exposure

Purified hog TPO; native TG with 1.0% iodine and further-iodinated TG with 1.2% iodine; reagent concentrations not stated in abstract.

limitations

Reaction measures TG iodination, not free iodotyrosine recycling. The proposed iodinium intermediate is a model, not imported as an established mechanism.

nutrient_topic

Iodine research collection; topical membership is not evidence of a direct dietary effect. · Iodine

organism

Sus scrofa

plain_language

TPO attaches iodine to tyrosine residues within the TG protein.

primary_references

[iodine-syn-tpo-iodination1984] Iodination and oxidation of thyroglobulin catalyzed by thyroid peroxidase. (1984). https://pubmed.ncbi.nlm.nih.gov/6706940/ DOI: 10.1016/s0021-9258(17)43667-2

tissue_or_cell_type

Purified thyroid enzyme and protein substrate

Iodine: thyroid hormone production, deficiency, excess and nutrient interactions (2026-09-17) · lines 828–840

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified hog thyroid peroxidase with hog thyroglobulin; steady-state and stopped-flow kinetics · source_derived_draft · unverified_draft

### iodine-syn-tpo-protein-iodination Purified hog TPO catalyzed iodine incorporation into hog thyroglobulin in kinetic assays of protein iodination. Condition category: normal nutrient_topic: Iodine research collection; topical membership is not evidence of a direct dietary effect. plain_language: TPO attaches iodine to tyrosine residues within the TG protein. organism: Sus scrofa tissue_or_cell_type: Purified thyroid enzyme and protein substrate experimental_model: Purified hog thyroid peroxidase with hog thyroglobulin; steady-state and stopped-flow kinetics limitations: Reaction measures TG iodination, not free iodotyrosine recycling. The proposed iodinium intermediate is a model, not imported as an established mechanism. exposure: Purified hog TPO; native TG with 1.0% iodine and further-iodinated TG with 1.2% iodine; reagent concentrations not stated in abstract. cross_nutrient: false evidence_span: {"source_cache": "artifacts/iodine-synthesis-sources/6706940.json", "json_field": "abstractText", "text_sha256": "e7d184d64b66b0dc89f61c511688c79ffc9785b20233e7746ef4c97de351c78c", "text_characters": 1442, "note": "Exact publisher passage retained in the cited local source cache; locator and digest supplied here."} [iodine-syn-tpo-iodination1984] Iodination and oxidation of thyroglobulin catalyzed by thyroid peroxidase. (1984). https://pubmed.ncbi.nlm.nih.gov/6706940/ DOI: 10.1016/s0021-9258(17)43667-2

cross_nutrient

false

evidence_span

{"source_cache": "artifacts/iodine-synthesis-sources/7372636.txt", "start_char": 6216, "end_char": 8536, "text_sha256": "753e684061b9063528196c840b23404015abc2b7b836a3887497aea0f8fe20a6", "text_characters": 2320, "note": "Exact publisher passage retained in the cited local source cache; locator and digest supplied here."}

experimental_model

Purified hog TPO with human goiter TG or tyrosine-radiolabeled hog TG; chromatographic hormone and dehydroalanine analyses

exposure

Human goiter TG initially 0.04% iodine, iodinated for 90 minutes to approximately 60 iodine atoms per TG; the same preparation contained 2.6 T4 residues per molecule.

limitations

Reconstituted mixed-species experiment. Hormone residues are protein-bound before hydrolysis; the assay is not evidence that free MIT and DIT are routinely coupled in blood.

nutrient_topic

Iodine research collection; topical membership is not evidence of a direct dietary effect. · Iodine

organism

Sus scrofa enzyme; Homo sapiens substrate

plain_language

TPO-driven chemistry can make T3 directly within TG, before the hormone is released.

primary_references

[iodine-syn-tpo-coupling1980] Formation of dehydroalanine residues during thyroid hormone synthesis in thyroglobulin. (1980). https://pubmed.ncbi.nlm.nih.gov/7372636/ DOI: 10.1016/S0021-9258(19)70782-0

tissue_or_cell_type

Purified TPO and human goiter TG

Iodine: thyroid hormone production, deficiency, excess and nutrient interactions (2026-09-17) · lines 856–868

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified hog TPO with human goiter TG or tyrosine-radiolabeled hog TG; chromatographic hormone and dehydroalanine analyses · source_derived_draft · unverified_draft

### iodine-syn-tpo-t3-formation Iodinating human goiter TG with hog TPO for 90 minutes produced 0.3 T3 residues per TG molecule, measured after enzymatic hydrolysis. Condition category: normal nutrient_topic: Iodine research collection; topical membership is not evidence of a direct dietary effect. plain_language: TPO-driven chemistry can make T3 directly within TG, before the hormone is released. organism: Sus scrofa enzyme; Homo sapiens substrate tissue_or_cell_type: Purified TPO and human goiter TG experimental_model: Purified hog TPO with human goiter TG or tyrosine-radiolabeled hog TG; chromatographic hormone and dehydroalanine analyses limitations: Reconstituted mixed-species experiment. Hormone residues are protein-bound before hydrolysis; the assay is not evidence that free MIT and DIT are routinely coupled in blood. exposure: Human goiter TG initially 0.04% iodine, iodinated for 90 minutes to approximately 60 iodine atoms per TG; the same preparation contained 2.6 T4 residues per molecule. cross_nutrient: false evidence_span: {"source_cache": "artifacts/iodine-synthesis-sources/7372636.txt", "start_char": 6216, "end_char": 8536, "text_sha256": "753e684061b9063528196c840b23404015abc2b7b836a3887497aea0f8fe20a6", "text_characters": 2320, "note": "Exact publisher passage retained in the cited local source cache; locator and digest supplied here."} [iodine-syn-tpo-coupling1980] Formation of dehydroalanine residues during thyroid hormone synthesis in thyroglobulin. (1980). https://pubmed.ncbi.nlm.nih.gov/7372636/ DOI: 10.1016/S0021-9258(19)70782-0

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

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

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

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

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

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

cross_nutrient

false

experimental_model

Human NIS cDNA expressed in COS-7 monkey cells

exposure

Transient human NIS cDNA expression; iodide and perchlorate concentrations not reported in the abstract.

limitations

Heterologous uptake establishes protein function, not whole-body iodine absorption.

nutrient_topic

Iodine research collection; topical membership is not evidence of a direct dietary effect. · Iodine

organism

Human protein in African green monkey cells

plain_language

Human NIS can bring iodide into cells.

primary_references

[iodine-trans-human-nis1996] Cloning of the human sodium lodide symporter. (1996). https://pubmed.ncbi.nlm.nih.gov/8806637/ DOI: 10.1006/bbrc.1996.1358

tissue_or_cell_type

COS-7 plasma membrane

Iodine: thyroid hormone production, deficiency, excess and nutrient interactions (2026-09-17) · lines 154–165

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human NIS cDNA expressed in COS-7 monkey cells · source_derived_draft · unverified_draft

### iodine-trans-human-nis-uptake Expression of cloned human NIS conferred perchlorate-sensitive iodide uptake on COS-7 cells. Condition category: normal nutrient_topic: Iodine research collection; topical membership is not evidence of a direct dietary effect. plain_language: Human NIS can bring iodide into cells. organism: Human protein in African green monkey cells tissue_or_cell_type: COS-7 plasma membrane experimental_model: Human NIS cDNA expressed in COS-7 monkey cells limitations: Heterologous uptake establishes protein function, not whole-body iodine absorption. exposure: Transient human NIS cDNA expression; iodide and perchlorate concentrations not reported in the abstract. cross_nutrient: false [iodine-trans-human-nis1996] Cloning of the human sodium lodide symporter. (1996). https://pubmed.ncbi.nlm.nih.gov/8806637/ DOI: 10.1006/bbrc.1996.1358

cross_nutrient

false

experimental_model

CHO cells stably expressing human NIS; individual and mixed anion exposures with 125I uptake

exposure

Joint Hill-equation fit; perchlorate molar potency was 15 times thiocyanate and 240 times nitrate.

limitations

Relative potencies and lack of synergy are assay-specific; they do not predict individual human thyroid outcomes from environmental concentrations.

nutrient_topic

Iodine research collection; topical membership is not evidence of a direct dietary effect. · Iodine

organism

Human NIS in hamster CHO cells

plain_language

These competitors combined approximately additively in the tested cell system.

primary_references

[iodine-trans-inhibitors2004] Relative potencies and additivity of perchlorate, thiocyanate, nitrate, and iodide on the inhibition of radioactive iodide uptake by the human sodium iodide symporter. (2004). https://pubmed.ncbi.nlm.nih.gov/15650353/ DOI: 10.1089/thy.2004.14.1012

tissue_or_cell_type

Cell plasma membrane

Iodine: thyroid hormone production, deficiency, excess and nutrient interactions (2026-09-17) · lines 440–451

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · CHO cells stably expressing human NIS; individual and mixed anion exposures with 125I uptake · source_derived_draft · unverified_draft

### iodine-trans-inhibitor-additivity Mixtures of perchlorate, thiocyanate and nitrate inhibited human NIS-mediated iodide uptake consistently with an additive common competitive model, without evidence of synergism. Condition category: normal nutrient_topic: Iodine research collection; topical membership is not evidence of a direct dietary effect. plain_language: These competitors combined approximately additively in the tested cell system. organism: Human NIS in hamster CHO cells tissue_or_cell_type: Cell plasma membrane experimental_model: CHO cells stably expressing human NIS; individual and mixed anion exposures with 125I uptake limitations: Relative potencies and lack of synergy are assay-specific; they do not predict individual human thyroid outcomes from environmental concentrations. exposure: Joint Hill-equation fit; perchlorate molar potency was 15 times thiocyanate and 240 times nitrate. cross_nutrient: false [iodine-trans-inhibitors2004] Relative potencies and additivity of perchlorate, thiocyanate, nitrate, and iodide on the inhibition of radioactive iodide uptake by the human sodium iodide symporter. (2004). https://pubmed.ncbi.nlm.nih.gov/15650353/ DOI: 10.1089/thy.2004.14.1012

cross_nutrient

false

experimental_model

Rat and mouse intestinal localization, intestinal brush-border vesicles and IEC-6 cells

exposure

Tissue localization; no intake intervention used for this claim.

limitations

Anatomical localization does not quantify the fraction of human iodine absorbed through this route.

nutrient_topic

Iodine research collection; topical membership is not evidence of a direct dietary effect. · Iodine

organism

Rattus norvegicus

plain_language

In the intestine, NIS faces the dietary contents.

primary_references

[iodine-trans-intestine2009] The Na+/I- symporter mediates active iodide uptake in the intestine. (2009). https://pubmed.ncbi.nlm.nih.gov/19052257/ DOI: 10.1152/ajpcell.00509.2008

tissue_or_cell_type

Small-intestinal enterocytes

Iodine: thyroid hormone production, deficiency, excess and nutrient interactions (2026-09-17) · lines 245–256

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Rat and mouse intestinal localization, intestinal brush-border vesicles and IEC-6 cells · source_derived_draft · unverified_draft

### iodine-trans-intestinal-location NIS immunolocalization in rat small-intestinal enterocytes was restricted to their apical surface. Condition category: normal nutrient_topic: Iodine research collection; topical membership is not evidence of a direct dietary effect. plain_language: In the intestine, NIS faces the dietary contents. organism: Rattus norvegicus tissue_or_cell_type: Small-intestinal enterocytes experimental_model: Rat and mouse intestinal localization, intestinal brush-border vesicles and IEC-6 cells limitations: Anatomical localization does not quantify the fraction of human iodine absorbed through this route. exposure: Tissue localization; no intake intervention used for this claim. cross_nutrient: false [iodine-trans-intestine2009] The Na+/I- symporter mediates active iodide uptake in the intestine. (2009). https://pubmed.ncbi.nlm.nih.gov/19052257/ DOI: 10.1152/ajpcell.00509.2008

cross_nutrient

true

experimental_model

Rat and mouse intestinal localization, intestinal brush-border vesicles and IEC-6 cells

exposure

Sodium-dependent vesicle uptake with perchlorate inhibition; concentrations not verified from abstract.

limitations

The abstract does not assign every vesicle experiment to one rodent species; the claim preserves the rodent scope and does not attribute the protein to humans.

nutrient_topic

Iodine research collection; topical membership is not evidence of a direct dietary effect. · Iodine

organism

Rodent intestinal preparation; rat and mouse study

plain_language

Intestinal iodide uptake can use the sodium gradient.

primary_references

[iodine-trans-intestine2009] The Na+/I- symporter mediates active iodide uptake in the intestine. (2009). https://pubmed.ncbi.nlm.nih.gov/19052257/ DOI: 10.1152/ajpcell.00509.2008

tissue_or_cell_type

Intestinal brush-border membrane vesicles

Iodine: thyroid hormone production, deficiency, excess and nutrient interactions (2026-09-17) · lines 258–269

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Rat and mouse intestinal localization, intestinal brush-border vesicles and IEC-6 cells · source_derived_draft · unverified_draft

### iodine-trans-intestinal-sodium-uptake Rodent intestinal brush-border membrane vesicles accumulated iodide in a sodium-dependent, perchlorate-sensitive manner. Condition category: normal nutrient_topic: Iodine research collection; topical membership is not evidence of a direct dietary effect. plain_language: Intestinal iodide uptake can use the sodium gradient. organism: Rodent intestinal preparation; rat and mouse study tissue_or_cell_type: Intestinal brush-border membrane vesicles experimental_model: Rat and mouse intestinal localization, intestinal brush-border vesicles and IEC-6 cells limitations: The abstract does not assign every vesicle experiment to one rodent species; the claim preserves the rodent scope and does not attribute the protein to humans. exposure: Sodium-dependent vesicle uptake with perchlorate inhibition; concentrations not verified from abstract. cross_nutrient: true [iodine-trans-intestine2009] The Na+/I- symporter mediates active iodide uptake in the intestine. (2009). https://pubmed.ncbi.nlm.nih.gov/19052257/ DOI: 10.1152/ajpcell.00509.2008

cross_nutrient

false

experimental_model

Lactating and comparator mouse mammary tissues; mouse NIS cDNA cloning

exposure

Lactating versus comparison mammary tissues; dietary doses not specified.

limitations

Transcript abundance is not a direct milk-transfer rate or evidence for a human supplement dose.

nutrient_topic

Iodine research collection; topical membership is not evidence of a direct dietary effect. · Iodine

organism

Mus musculus

plain_language

The lactating mouse mammary gland increases the transcript for the iodide transporter.

primary_references

[iodine-trans-lactation2001] Cloning of the mouse sodium iodide symporter and its expression in the mammary gland and other tissues. (2001). https://pubmed.ncbi.nlm.nih.gov/11431151/ DOI: 10.1677/joe.0.1700185

tissue_or_cell_type

Mammary gland

Iodine: thyroid hormone production, deficiency, excess and nutrient interactions (2026-09-17) · lines 271–282

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Lactating and comparator mouse mammary tissues; mouse NIS cDNA cloning · source_derived_draft · unverified_draft

### iodine-trans-lactation-mrna Mouse mammary Slc5a5 mRNA abundance increased during lactation. Condition category: normal nutrient_topic: Iodine research collection; topical membership is not evidence of a direct dietary effect. plain_language: The lactating mouse mammary gland increases the transcript for the iodide transporter. organism: Mus musculus tissue_or_cell_type: Mammary gland experimental_model: Lactating and comparator mouse mammary tissues; mouse NIS cDNA cloning limitations: Transcript abundance is not a direct milk-transfer rate or evidence for a human supplement dose. exposure: Lactating versus comparison mammary tissues; dietary doses not specified. cross_nutrient: false [iodine-trans-lactation2001] Cloning of the mouse sodium iodide symporter and its expression in the mammary gland and other tissues. (2001). https://pubmed.ncbi.nlm.nih.gov/11431151/ DOI: 10.1677/joe.0.1700185

cross_nutrient

false

experimental_model

CHO cells stably expressing human NIS; individual and mixed anion exposures with 125I uptake

exposure

Concentration-response experiments with individual anions and 125I uptake; exact concentration series not reported in abstract.

limitations

In vitro potency is not a human dietary exposure threshold, whole-body iodine displacement claim or supplementation instruction.

nutrient_topic

Iodine research collection; topical membership is not evidence of a direct dietary effect. · Iodine

organism

Human NIS in hamster CHO cells

plain_language

A competing anion reduced iodide entry through human NIS in a cell assay.

primary_references

[iodine-trans-inhibitors2004] Relative potencies and additivity of perchlorate, thiocyanate, nitrate, and iodide on the inhibition of radioactive iodide uptake by the human sodium iodide symporter. (2004). https://pubmed.ncbi.nlm.nih.gov/15650353/ DOI: 10.1089/thy.2004.14.1012

tissue_or_cell_type

Cell plasma membrane

Iodine: thyroid hormone production, deficiency, excess and nutrient interactions (2026-09-17) · lines 427–438

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · CHO cells stably expressing human NIS; individual and mixed anion exposures with 125I uptake · source_derived_draft · unverified_draft

### iodine-trans-nitrate-inhibits Nitrate inhibited radioactive iodide uptake in CHO cells stably expressing human NIS. Condition category: normal nutrient_topic: Iodine research collection; topical membership is not evidence of a direct dietary effect. plain_language: A competing anion reduced iodide entry through human NIS in a cell assay. organism: Human NIS in hamster CHO cells tissue_or_cell_type: Cell plasma membrane experimental_model: CHO cells stably expressing human NIS; individual and mixed anion exposures with 125I uptake limitations: In vitro potency is not a human dietary exposure threshold, whole-body iodine displacement claim or supplementation instruction. exposure: Concentration-response experiments with individual anions and 125I uptake; exact concentration series not reported in abstract. cross_nutrient: false [iodine-trans-inhibitors2004] Relative potencies and additivity of perchlorate, thiocyanate, nitrate, and iodide on the inhibition of radioactive iodide uptake by the human sodium iodide symporter. (2004). https://pubmed.ncbi.nlm.nih.gov/15650353/ DOI: 10.1089/thy.2004.14.1012

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

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

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

cross_nutrient

false

experimental_model

CHO cells stably expressing human NIS; individual and mixed anion exposures with 125I uptake

exposure

Concentration-response experiments with individual anions and 125I uptake; exact concentration series not reported in abstract.

limitations

In vitro potency is not a human dietary exposure threshold, whole-body iodine displacement claim or supplementation instruction.

nutrient_topic

Iodine research collection; topical membership is not evidence of a direct dietary effect. · Iodine

organism

Human NIS in hamster CHO cells

plain_language

A competing anion reduced iodide entry through human NIS in a cell assay.

primary_references

[iodine-trans-inhibitors2004] Relative potencies and additivity of perchlorate, thiocyanate, nitrate, and iodide on the inhibition of radioactive iodide uptake by the human sodium iodide symporter. (2004). https://pubmed.ncbi.nlm.nih.gov/15650353/ DOI: 10.1089/thy.2004.14.1012

tissue_or_cell_type

Cell plasma membrane

Iodine: thyroid hormone production, deficiency, excess and nutrient interactions (2026-09-17) · lines 401–412

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · CHO cells stably expressing human NIS; individual and mixed anion exposures with 125I uptake · source_derived_draft · unverified_draft

### iodine-trans-perchlorate-inhibits Perchlorate inhibited radioactive iodide uptake in CHO cells stably expressing human NIS. Condition category: normal nutrient_topic: Iodine research collection; topical membership is not evidence of a direct dietary effect. plain_language: A competing anion reduced iodide entry through human NIS in a cell assay. organism: Human NIS in hamster CHO cells tissue_or_cell_type: Cell plasma membrane experimental_model: CHO cells stably expressing human NIS; individual and mixed anion exposures with 125I uptake limitations: In vitro potency is not a human dietary exposure threshold, whole-body iodine displacement claim or supplementation instruction. exposure: Concentration-response experiments with individual anions and 125I uptake; exact concentration series not reported in abstract. cross_nutrient: false [iodine-trans-inhibitors2004] Relative potencies and additivity of perchlorate, thiocyanate, nitrate, and iodide on the inhibition of radioactive iodide uptake by the human sodium iodide symporter. (2004). https://pubmed.ncbi.nlm.nih.gov/15650353/ DOI: 10.1089/thy.2004.14.1012

cross_nutrient

true

experimental_model

Endogenous rat NIS in IEC-6 intestinal epithelial cells; initial-rate transport and statistical thermodynamic fitting

exposure

Initial-rate iodide uptake at 5, 10, 20 or 60 micromolar iodide with 0–260 mM sodium; two-minute incubations; constant osmolarity.

limitations

Kd values depend on the authors’ transport model; the finding does not show that eating extra salt improves iodine status.

nutrient_topic

Iodine research collection; topical membership is not evidence of a direct dietary effect. · Iodine

organism

Rattus norvegicus

plain_language

Sodium binding makes NIS bind iodide more readily.

primary_references

[iodine-trans-sodium-affinity2014] Physiological sodium concentrations enhance the iodide affinity of the Na+/I- symporter. (2014). https://pubmed.ncbi.nlm.nih.gov/24888603/ DOI: 10.1038/ncomms4948

tissue_or_cell_type

IEC-6 intestinal epithelial cells

Iodine: thyroid hormone production, deficiency, excess and nutrient interactions (2026-09-17) · lines 180–191

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Endogenous rat NIS in IEC-6 intestinal epithelial cells; initial-rate transport and statistical thermodynamic fitting · source_derived_draft · unverified_draft

### iodine-trans-sodium-affinity Thermodynamic fits to rat IEC-6 NIS transport data estimated an iodide Kd of 224 micromolar without sodium binding and 22.4 micromolar in the sodium-bound state. Condition category: normal nutrient_topic: Iodine research collection; topical membership is not evidence of a direct dietary effect. plain_language: Sodium binding makes NIS bind iodide more readily. organism: Rattus norvegicus tissue_or_cell_type: IEC-6 intestinal epithelial cells experimental_model: Endogenous rat NIS in IEC-6 intestinal epithelial cells; initial-rate transport and statistical thermodynamic fitting limitations: Kd values depend on the authors’ transport model; the finding does not show that eating extra salt improves iodine status. exposure: Initial-rate iodide uptake at 5, 10, 20 or 60 micromolar iodide with 0–260 mM sodium; two-minute incubations; constant osmolarity. cross_nutrient: true [iodine-trans-sodium-affinity2014] Physiological sodium concentrations enhance the iodide affinity of the Na+/I- symporter. (2014). https://pubmed.ncbi.nlm.nih.gov/24888603/ DOI: 10.1038/ncomms4948

cross_nutrient

true

experimental_model

Rat NIS expressed in Xenopus laevis oocytes; electrophysiology and tracer uptake

exposure

Tracer uptake and electrophysiology; apparent sodium affinity 28 ± 3 mM and iodide affinity 33 ± 9 micromolar.

limitations

Rat-protein assay parameters are not dietary sodium requirements or human iodide thresholds.

nutrient_topic

Iodine research collection; topical membership is not evidence of a direct dietary effect. · Iodine

organism

Rat protein in Xenopus laevis oocytes

plain_language

NIS uses sodium movement to carry iodide into cells.

primary_references

[iodine-trans-stoichiometry1997] Thyroid Na+/I- symporter. Mechanism, stoichiometry, and specificity. (1997). https://pubmed.ncbi.nlm.nih.gov/9341168/ DOI: 10.1074/jbc.272.43.27230

tissue_or_cell_type

Oocyte plasma membrane

Iodine: thyroid hormone production, deficiency, excess and nutrient interactions (2026-09-17) · lines 167–178

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Rat NIS expressed in Xenopus laevis oocytes; electrophysiology and tracer uptake · source_derived_draft · unverified_draft

### iodine-trans-sodium-coupling Rat NIS expressed in Xenopus oocytes transported iodide with two sodium ions per anion and generated inward electrogenic transport. Condition category: normal nutrient_topic: Iodine research collection; topical membership is not evidence of a direct dietary effect. plain_language: NIS uses sodium movement to carry iodide into cells. organism: Rat protein in Xenopus laevis oocytes tissue_or_cell_type: Oocyte plasma membrane experimental_model: Rat NIS expressed in Xenopus laevis oocytes; electrophysiology and tracer uptake limitations: Rat-protein assay parameters are not dietary sodium requirements or human iodide thresholds. exposure: Tracer uptake and electrophysiology; apparent sodium affinity 28 ± 3 mM and iodide affinity 33 ± 9 micromolar. cross_nutrient: true [iodine-trans-stoichiometry1997] Thyroid Na+/I- symporter. Mechanism, stoichiometry, and specificity. (1997). https://pubmed.ncbi.nlm.nih.gov/9341168/ DOI: 10.1074/jbc.272.43.27230

availability_state

machinery_impairment Imported condition classification; unverified.

cross_nutrient

false

experimental_model

Human iodide-transport-defect patient and expression of patient-derived NIS in COS-7 cells

exposure

Patient-derived T354P cDNA expression; uptake concentration not provided in abstract.

limitations

The reported patient had goiter and defective accumulation but was essentially euthyroid; do not turn this case into universal hypothyroidism severity.

nutrient_topic

Iodine research collection; topical membership is not evidence of a direct dietary effect. · Iodine

organism

Human protein in African green monkey cells

plain_language

A defective NIS protein can limit uptake even when iodide is present.

primary_references

[iodine-trans-t354p1997] A homozygous missense mutation of the sodium/iodide symporter gene causing iodide transport defect. (1997). https://pubmed.ncbi.nlm.nih.gov/9398697/ DOI: 10.1210/jcem.82.12.4425

tissue_or_cell_type

COS-7 plasma membrane

trigger_kind

machinery_impairment Imported condition classification; unverified.

Iodine: thyroid hormone production, deficiency, excess and nutrient interactions (2026-09-17) · lines 232–243

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human iodide-transport-defect patient and expression of patient-derived NIS in COS-7 cells · source_derived_draft · unverified_draft

### iodine-trans-t354p-uptake Human NIS T354P expressed in COS-7 cells showed markedly reduced iodide uptake compared with normal NIS. Condition category: machinery_impairment nutrient_topic: Iodine research collection; topical membership is not evidence of a direct dietary effect. plain_language: A defective NIS protein can limit uptake even when iodide is present. organism: Human protein in African green monkey cells tissue_or_cell_type: COS-7 plasma membrane experimental_model: Human iodide-transport-defect patient and expression of patient-derived NIS in COS-7 cells limitations: The reported patient had goiter and defective accumulation but was essentially euthyroid; do not turn this case into universal hypothyroidism severity. exposure: Patient-derived T354P cDNA expression; uptake concentration not provided in abstract. cross_nutrient: false [iodine-trans-t354p1997] A homozygous missense mutation of the sodium/iodide symporter gene causing iodide transport defect. (1997). https://pubmed.ncbi.nlm.nih.gov/9398697/ DOI: 10.1210/jcem.82.12.4425

cross_nutrient

false

experimental_model

CHO cells stably expressing human NIS; individual and mixed anion exposures with 125I uptake

exposure

Concentration-response experiments with individual anions and 125I uptake; exact concentration series not reported in abstract.

limitations

In vitro potency is not a human dietary exposure threshold, whole-body iodine displacement claim or supplementation instruction.

nutrient_topic

Iodine research collection; topical membership is not evidence of a direct dietary effect. · Iodine

organism

Human NIS in hamster CHO cells

plain_language

A competing anion reduced iodide entry through human NIS in a cell assay.

primary_references

[iodine-trans-inhibitors2004] Relative potencies and additivity of perchlorate, thiocyanate, nitrate, and iodide on the inhibition of radioactive iodide uptake by the human sodium iodide symporter. (2004). https://pubmed.ncbi.nlm.nih.gov/15650353/ DOI: 10.1089/thy.2004.14.1012

tissue_or_cell_type

Cell plasma membrane

Iodine: thyroid hormone production, deficiency, excess and nutrient interactions (2026-09-17) · lines 414–425

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · CHO cells stably expressing human NIS; individual and mixed anion exposures with 125I uptake · source_derived_draft · unverified_draft

### iodine-trans-thiocyanate-inhibits Thiocyanate inhibited radioactive iodide uptake in CHO cells stably expressing human NIS. Condition category: normal nutrient_topic: Iodine research collection; topical membership is not evidence of a direct dietary effect. plain_language: A competing anion reduced iodide entry through human NIS in a cell assay. organism: Human NIS in hamster CHO cells tissue_or_cell_type: Cell plasma membrane experimental_model: CHO cells stably expressing human NIS; individual and mixed anion exposures with 125I uptake limitations: In vitro potency is not a human dietary exposure threshold, whole-body iodine displacement claim or supplementation instruction. exposure: Concentration-response experiments with individual anions and 125I uptake; exact concentration series not reported in abstract. cross_nutrient: false [iodine-trans-inhibitors2004] Relative potencies and additivity of perchlorate, thiocyanate, nitrate, and iodide on the inhibition of radioactive iodide uptake by the human sodium iodide symporter. (2004). https://pubmed.ncbi.nlm.nih.gov/15650353/ DOI: 10.1089/thy.2004.14.1012

evidence_access

Primary abstract

experimental_model

Eight kinetic studies in seven thyrotoxic women; serum lithium about 1 mEq/L.

limitations

Compartment-model inference; not evidence that lithium simply removes iodine from the body.

nutrient_topic

Lithium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Lithium

plain_language

Making thyroid hormone and releasing it are separate steps.

primary_references

The use of lithium in the treatment of thyrotoxicosis. · 1972 · https://pubmed.ncbi.nlm.nih.gov/4115707/ · DOI 10.1172/JCI107094

Lithium: metal-sensitive enzymes, transport and cross-nutrient mechanisms (2026-09-19) · lines 392–398

AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Eight kinetic studies in seven thyrotoxic women; serum lithium about 1 mEq/L. · source_derived_draft · unverified_draft

## lithium-thyroid-release Making thyroid hormone and releasing it are separate steps. Lithium reduced hormonal and nonhormonal thyroid iodine release in human radioiodine kinetic studies. Model: Eight kinetic studies in seven thyrotoxic women; serum lithium about 1 mEq/L. Limitations: Compartment-model inference; not evidence that lithium simply removes iodine from the body. Evidence access: Primary abstract The use of lithium in the treatment of thyrotoxicosis. · 1972 · https://pubmed.ncbi.nlm.nih.gov/4115707/ · DOI 10.1172/JCI107094