Component

Human thyroid peroxidase

Human thyroid peroxidase

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

Read recorded mechanisms Open recursive mind map

How nutrients influence it

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

How nutrients reach it in more than one step

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

Tracing routes…

What it does

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

Recorded relationships

What acts on it

  1. In CHO cells expressing human TPO, inhibition of heme biosynthesis by succinylacetone decreased surface TPO expression by approximately 80%.

    Succinylacetone → Human thyroid peroxidase source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    true
    evidence_span
    {"source_cache": "artifacts/iodine-synthesis-sources/10187846.json", "json_field": "abstractText", "text_sha256": "97f8a86c7effd5754e2b61c65d769de9e86678a7398c5eb20a0e88ac49a8fdbb", "text_characters": 1855, "note": "Exact publisher passage retained in the cited local source cache; locator and digest supplied here."}
    experimental_model
    CHO cells expressing human TPO; additional primary thyroid cultures
    exposure
    Succinylacetone; concentration not stated in abstract.
    limitations
    Pharmacological heme synthesis perturbation; not evidence of a dietary iron threshold.
    nutrient_topic
    Iodine research collection; topical membership is not evidence of a direct dietary effect. · Iodine
    organism
    Homo sapiens protein; Cricetulus griseus host cells
    plain_language
    Blocking heme production kept much of TPO from reaching the surface.
    primary_references
    [iodine-syn-tpo1999] Role of heme in intracellular trafficking of thyroperoxidase and involvement of H2O2 generated at the apical surface of thyroid cells in autocatalytic covalent heme binding. (1999). https://pubmed.ncbi.nlm.nih.gov/10187846/ DOI: 10.1074/jbc.274.15.10533
    tissue_or_cell_type
    CHO endoplasmic reticulum and cell surface

    Iodine: thyroid hormone production, deficiency, excess and nutrient interactions (2026-09-17) · lines 576–588

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · CHO cells expressing human TPO; additional primary thyroid cultures · source_derived_draft · unverified_draft

    ### iodine-syn-heme-trafficking In CHO cells expressing human TPO, inhibition of heme biosynthesis by succinylacetone decreased surface TPO expression by approximately 80%. Condition category: normal nutrient_topic: Iodine research collection; topical membership is not evidence of a direct dietary effect. plain_language: Blocking heme production kept much of TPO from reaching the surface. organism: Homo sapiens protein; Cricetulus griseus host cells tissue_or_cell_type: CHO endoplasmic reticulum and cell surface experimental_model: CHO cells expressing human TPO; additional primary thyroid cultures limitations: Pharmacological heme synthesis perturbation; not evidence of a dietary iron threshold. exposure: Succinylacetone; concentration not stated in abstract. cross_nutrient: true evidence_span: {"source_cache": "artifacts/iodine-synthesis-sources/10187846.json", "json_field": "abstractText", "text_sha256": "97f8a86c7effd5754e2b61c65d769de9e86678a7398c5eb20a0e88ac49a8fdbb", "text_characters": 1855, "note": "Exact publisher passage retained in the cited local source cache; locator and digest supplied here."} [iodine-syn-tpo1999] Role of heme in intracellular trafficking of thyroperoxidase and involvement of H2O2 generated at the apical surface of thyroid cells in autocatalytic covalent heme binding. (1999). https://pubmed.ncbi.nlm.nih.gov/10187846/ DOI: 10.1074/jbc.274.15.10533
    Complete structured claim and evidence

  2. Exposing human TPO-expressing CHO cells to 10 micromolar H2O2 for 10 minutes increased cell-surface peroxidase activity by 65%.

    Hydrogen peroxide → Human thyroid peroxidase source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    true
    evidence_span
    {"source_cache": "artifacts/iodine-synthesis-sources/10187846.json", "json_field": "abstractText", "text_sha256": "97f8a86c7effd5754e2b61c65d769de9e86678a7398c5eb20a0e88ac49a8fdbb", "text_characters": 1855, "note": "Exact publisher passage retained in the cited local source cache; locator and digest supplied here."}
    experimental_model
    CHO cells expressing human TPO; additional primary thyroid cultures
    exposure
    10 micromolar H2O2, 10 minutes.
    limitations
    Authors interpret activation through covalent heme attachment; no direct nutrient-intake intervention.
    nutrient_topic
    Iodine research collection; topical membership is not evidence of a direct dietary effect. · Iodine
    organism
    Homo sapiens protein; Cricetulus griseus host cells
    plain_language
    Peroxide exposure helped activate surface TPO in this cell model.
    primary_references
    [iodine-syn-tpo1999] Role of heme in intracellular trafficking of thyroperoxidase and involvement of H2O2 generated at the apical surface of thyroid cells in autocatalytic covalent heme binding. (1999). https://pubmed.ncbi.nlm.nih.gov/10187846/ DOI: 10.1074/jbc.274.15.10533
    tissue_or_cell_type
    CHO cell surface

    Iodine: thyroid hormone production, deficiency, excess and nutrient interactions (2026-09-17) · lines 590–602

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · CHO cells expressing human TPO; additional primary thyroid cultures · source_derived_draft · unverified_draft

    ### iodine-syn-peroxide-tpo-activation Exposing human TPO-expressing CHO cells to 10 micromolar H2O2 for 10 minutes increased cell-surface peroxidase activity by 65%. Condition category: normal nutrient_topic: Iodine research collection; topical membership is not evidence of a direct dietary effect. plain_language: Peroxide exposure helped activate surface TPO in this cell model. organism: Homo sapiens protein; Cricetulus griseus host cells tissue_or_cell_type: CHO cell surface experimental_model: CHO cells expressing human TPO; additional primary thyroid cultures limitations: Authors interpret activation through covalent heme attachment; no direct nutrient-intake intervention. exposure: 10 micromolar H2O2, 10 minutes. cross_nutrient: true evidence_span: {"source_cache": "artifacts/iodine-synthesis-sources/10187846.json", "json_field": "abstractText", "text_sha256": "97f8a86c7effd5754e2b61c65d769de9e86678a7398c5eb20a0e88ac49a8fdbb", "text_characters": 1855, "note": "Exact publisher passage retained in the cited local source cache; locator and digest supplied here."} [iodine-syn-tpo1999] Role of heme in intracellular trafficking of thyroperoxidase and involvement of H2O2 generated at the apical surface of thyroid cells in autocatalytic covalent heme binding. (1999). https://pubmed.ncbi.nlm.nih.gov/10187846/ DOI: 10.1074/jbc.274.15.10533
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Recombinant human TPO catalyzed T4 formation from recombinant human TG in the direct TPO-versus-lactoperoxidase comparison.

    Human TPO ectodomain residues 1–838 → Human thyroglobulin containing covalent T4 residues source_derived_draftungraded
    Experimental context and source evidence
    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
    Complete structured claim and evidence

  2. Cryo-EM structures of the human TPO extracellular domain resolve heme at the peroxidase active site.

    Human TPO ectodomain residues 1–839 → Heme source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    true
    evidence_span
    {"source_cache": "artifacts/iodine-synthesis-sources/36537574.txt", "start_char": 17835, "end_char": 18855, "text_sha256": "6771d21482631bf712dfa882f1d08e4f40e02507211c65a60c7ef47f0d02e5d4", "text_characters": 1020, "note": "Exact publisher passage retained in the cited local source cache; locator and digest supplied here."}
    experimental_model
    Cryo-EM of recombinant human TPO extracellular domain with antibody fragments
    exposure
    Human TPO residues 1–839 expressed in High Five insect cells and bound to 2G4 or 4F5 antibody fragments.
    limitations
    A structural observation; no selenium catalytic requirement or dietary iron dose is demonstrated.
    nutrient_topic
    Iodine research collection; topical membership is not evidence of a direct dietary effect. · Iodine
    organism
    Homo sapiens protein; Trichoplusia ni expression cells
    plain_language
    TPO contains an iron-bearing heme group at its catalytic center.
    primary_references
    [iodine-syn-tpo2023] Cryo-electron microscopy structures of human thyroid peroxidase (TPO) in complex with TPO antibodies. (2023). https://pubmed.ncbi.nlm.nih.gov/36537574/ DOI: 10.1530/jme-22-0149
    tissue_or_cell_type
    Purified extracellular-domain antibody complexes

    Iodine: thyroid hormone production, deficiency, excess and nutrient interactions (2026-09-17) · lines 604–616

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Cryo-EM of recombinant human TPO extracellular domain with antibody fragments · source_derived_draft · unverified_draft

    ### iodine-syn-tpo-heme-structure Cryo-EM structures of the human TPO extracellular domain resolve heme at the peroxidase active site. Condition category: normal nutrient_topic: Iodine research collection; topical membership is not evidence of a direct dietary effect. plain_language: TPO contains an iron-bearing heme group at its catalytic center. organism: Homo sapiens protein; Trichoplusia ni expression cells tissue_or_cell_type: Purified extracellular-domain antibody complexes experimental_model: Cryo-EM of recombinant human TPO extracellular domain with antibody fragments limitations: A structural observation; no selenium catalytic requirement or dietary iron dose is demonstrated. exposure: Human TPO residues 1–839 expressed in High Five insect cells and bound to 2G4 or 4F5 antibody fragments. cross_nutrient: true evidence_span: {"source_cache": "artifacts/iodine-synthesis-sources/36537574.txt", "start_char": 17835, "end_char": 18855, "text_sha256": "6771d21482631bf712dfa882f1d08e4f40e02507211c65a60c7ef47f0d02e5d4", "text_characters": 1020, "note": "Exact publisher passage retained in the cited local source cache; locator and digest supplied here."} [iodine-syn-tpo2023] Cryo-electron microscopy structures of human thyroid peroxidase (TPO) in complex with TPO antibodies. (2023). https://pubmed.ncbi.nlm.nih.gov/36537574/ DOI: 10.1530/jme-22-0149
    Complete structured claim and evidence

In the sources

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

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

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