Component

Hepcidin

Independent biological entity. Read linked claims for experimental scope and context.

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

Read recorded mechanisms Open recursive mind map

How nutrients influence it

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

How nutrients reach it in more than one step

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

Tracing routes…

What it does

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

Recorded relationships

What it acts on

  1. Hepcidin-induced ferroportin removal reduced cellular iron export.

    Hepcidin → Cellular iron export source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/iron-research/15514116.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "00a292f6693116798182b0f9418f2eb8466aa029f32905019416422002158c4a", "start_char": 0, "end_char": 758, "text_sha256": "00a292f6693116798182b0f9418f2eb8466aa029f32905019416422002158c4a"}
    experimental_model
    Hepcidin binding and cellular export experiments
    exposure
    Hepcidin exposure
    limitations
    Post-translational export regulation; no dose-response to dietary iron is inferred from the cell experiment.
    nutrient_topic
    Iron research collection; topical membership is not evidence of a direct dietary effect. · Iron
    organism
    Tissue-culture ferroportin systems
    plain_language
    Iron can be held inside cells instead of reaching the circulation.
    primary_references
    [iron-p15514116] Hepcidin regulates cellular iron efflux by binding to ferroportin and inducing its internalization. (2004). https://pubmed.ncbi.nlm.nih.gov/15514116/ DOI: 10.1126/science.1104742
    tissue_or_cell_type
    Plasma membrane

    Iron: absorption, trafficking, iron-dependent enzymes and nutrient interactions (2026-09-17) · lines 732–743

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Hepcidin binding and cellular export experiments · source_derived_draft · unverified_draft

    ### iron-hepcidin-export Hepcidin-induced ferroportin removal reduced cellular iron export. Condition category: normal nutrient_topic: Iron research collection; topical membership is not evidence of a direct dietary effect. plain_language: Iron can be held inside cells instead of reaching the circulation. organism: Tissue-culture ferroportin systems tissue_or_cell_type: Plasma membrane experimental_model: Hepcidin binding and cellular export experiments limitations: Post-translational export regulation; no dose-response to dietary iron is inferred from the cell experiment. exposure: Hepcidin exposure evidence_span: {"source_cache": "artifacts/iron-research/15514116.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "00a292f6693116798182b0f9418f2eb8466aa029f32905019416422002158c4a", "start_char": 0, "end_char": 758, "text_sha256": "00a292f6693116798182b0f9418f2eb8466aa029f32905019416422002158c4a"} [iron-p15514116] Hepcidin regulates cellular iron efflux by binding to ferroportin and inducing its internalization. (2004). https://pubmed.ncbi.nlm.nih.gov/15514116/ DOI: 10.1126/science.1104742
    Complete structured claim and evidence

  2. Hepcidin bound ferroportin in tissue-culture cells.

    Hepcidin → Ferroportin / SLC40A1 source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/iron-research/15514116.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "00a292f6693116798182b0f9418f2eb8466aa029f32905019416422002158c4a", "start_char": 0, "end_char": 758, "text_sha256": "00a292f6693116798182b0f9418f2eb8466aa029f32905019416422002158c4a"}
    experimental_model
    Hepcidin binding and cellular export experiments
    exposure
    Hepcidin exposure
    limitations
    Post-translational export regulation; no dose-response to dietary iron is inferred from the cell experiment.
    nutrient_topic
    Iron research collection; topical membership is not evidence of a direct dietary effect. · Iron
    organism
    Tissue-culture ferroportin systems
    plain_language
    The liver-derived control hormone acts directly on the iron-export protein.
    primary_references
    [iron-p15514116] Hepcidin regulates cellular iron efflux by binding to ferroportin and inducing its internalization. (2004). https://pubmed.ncbi.nlm.nih.gov/15514116/ DOI: 10.1126/science.1104742
    tissue_or_cell_type
    Plasma membrane

    Iron: absorption, trafficking, iron-dependent enzymes and nutrient interactions (2026-09-17) · lines 706–717

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Hepcidin binding and cellular export experiments · source_derived_draft · unverified_draft

    ### iron-hepcidin-fpn-binding Hepcidin bound ferroportin in tissue-culture cells. Condition category: normal nutrient_topic: Iron research collection; topical membership is not evidence of a direct dietary effect. plain_language: The liver-derived control hormone acts directly on the iron-export protein. organism: Tissue-culture ferroportin systems tissue_or_cell_type: Plasma membrane experimental_model: Hepcidin binding and cellular export experiments limitations: Post-translational export regulation; no dose-response to dietary iron is inferred from the cell experiment. exposure: Hepcidin exposure evidence_span: {"source_cache": "artifacts/iron-research/15514116.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "00a292f6693116798182b0f9418f2eb8466aa029f32905019416422002158c4a", "start_char": 0, "end_char": 758, "text_sha256": "00a292f6693116798182b0f9418f2eb8466aa029f32905019416422002158c4a"} [iron-p15514116] Hepcidin regulates cellular iron efflux by binding to ferroportin and inducing its internalization. (2004). https://pubmed.ncbi.nlm.nih.gov/15514116/ DOI: 10.1126/science.1104742
    Complete structured claim and evidence

  3. Hepcidin binding induced ferroportin internalization and degradation.

    Hepcidin → Cell-surface ferroportin abundance source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/iron-research/15514116.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "00a292f6693116798182b0f9418f2eb8466aa029f32905019416422002158c4a", "start_char": 0, "end_char": 758, "text_sha256": "00a292f6693116798182b0f9418f2eb8466aa029f32905019416422002158c4a"}
    experimental_model
    Hepcidin binding and cellular export experiments
    exposure
    Hepcidin exposure
    limitations
    Post-translational export regulation; no dose-response to dietary iron is inferred from the cell experiment.
    nutrient_topic
    Iron research collection; topical membership is not evidence of a direct dietary effect. · Iron
    organism
    Tissue-culture ferroportin systems
    plain_language
    The cell removes the exit route for iron from its surface.
    primary_references
    [iron-p15514116] Hepcidin regulates cellular iron efflux by binding to ferroportin and inducing its internalization. (2004). https://pubmed.ncbi.nlm.nih.gov/15514116/ DOI: 10.1126/science.1104742
    tissue_or_cell_type
    Plasma membrane

    Iron: absorption, trafficking, iron-dependent enzymes and nutrient interactions (2026-09-17) · lines 719–730

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Hepcidin binding and cellular export experiments · source_derived_draft · unverified_draft

    ### iron-hepcidin-fpn-removal Hepcidin binding induced ferroportin internalization and degradation. Condition category: normal nutrient_topic: Iron research collection; topical membership is not evidence of a direct dietary effect. plain_language: The cell removes the exit route for iron from its surface. organism: Tissue-culture ferroportin systems tissue_or_cell_type: Plasma membrane experimental_model: Hepcidin binding and cellular export experiments limitations: Post-translational export regulation; no dose-response to dietary iron is inferred from the cell experiment. exposure: Hepcidin exposure evidence_span: {"source_cache": "artifacts/iron-research/15514116.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "00a292f6693116798182b0f9418f2eb8466aa029f32905019416422002158c4a", "start_char": 0, "end_char": 758, "text_sha256": "00a292f6693116798182b0f9418f2eb8466aa029f32905019416422002158c4a"} [iron-p15514116] Hepcidin regulates cellular iron efflux by binding to ferroportin and inducing its internalization. (2004). https://pubmed.ncbi.nlm.nih.gov/15514116/ DOI: 10.1126/science.1104742
    Complete structured claim and evidence

  4. Hepcidin occupied outward-open ferroportin and blocked its iron-efflux pathway.

    Hepcidin → Ferroportin / SLC40A1 source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/iron-research/32814342.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "8de67bc7ca2250cfab2f2cb71c2da16b4806c05cf5d4b6e648b191596b6e0da0", "start_char": 0, "end_char": 1365, "text_sha256": "8de67bc7ca2250cfab2f2cb71c2da16b4806c05cf5d4b6e648b191596b6e0da0"}
    experimental_model
    Cryo-EM in lipid nanodiscs and binding/transport analysis
    exposure
    Apo state, hepcidin and cobalt mimetic; iron-dependent affinity measurements
    limitations
    Metal sites include a cobalt-bound structural preparation; the degradation-selectivity model is an interpretation, not proof that only loaded molecules are ever degraded.
    nutrient_topic
    Iron research collection; topical membership is not evidence of a direct dietary effect. · Iron
    organism
    Human ferroportin
    plain_language
    Hepcidin can physically block the exit channel as well as promote its removal.
    primary_references
    [iron-p32814342] Structure of hepcidin-bound ferroportin reveals iron homeostatic mechanisms. (2020). https://pubmed.ncbi.nlm.nih.gov/32814342/ DOI: 10.1038/s41586-020-2668-z
    tissue_or_cell_type
    Purified membrane transporter

    Iron: absorption, trafficking, iron-dependent enzymes and nutrient interactions (2026-09-17) · lines 745–756

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Cryo-EM in lipid nanodiscs and binding/transport analysis · source_derived_draft · unverified_draft

    ### iron-hepcidin-plugs-fpn Hepcidin occupied outward-open ferroportin and blocked its iron-efflux pathway. Condition category: normal nutrient_topic: Iron research collection; topical membership is not evidence of a direct dietary effect. plain_language: Hepcidin can physically block the exit channel as well as promote its removal. organism: Human ferroportin tissue_or_cell_type: Purified membrane transporter experimental_model: Cryo-EM in lipid nanodiscs and binding/transport analysis limitations: Metal sites include a cobalt-bound structural preparation; the degradation-selectivity model is an interpretation, not proof that only loaded molecules are ever degraded. exposure: Apo state, hepcidin and cobalt mimetic; iron-dependent affinity measurements evidence_span: {"source_cache": "artifacts/iron-research/32814342.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "8de67bc7ca2250cfab2f2cb71c2da16b4806c05cf5d4b6e648b191596b6e0da0", "start_char": 0, "end_char": 1365, "text_sha256": "8de67bc7ca2250cfab2f2cb71c2da16b4806c05cf5d4b6e648b191596b6e0da0"} [iron-p32814342] Structure of hepcidin-bound ferroportin reveals iron homeostatic mechanisms. (2020). https://pubmed.ncbi.nlm.nih.gov/32814342/ DOI: 10.1038/s41586-020-2668-z
    Complete structured claim and evidence

  5. The IL-6–hepcidin axis mediated inflammation-associated hypoferremia in the studied systems.

    Hepcidin → Serum iron concentration source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    biomarker_context Imported condition classification; unverified.
    evidence_span
    {"source_cache": "artifacts/iron-research/15124018.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "f2ed307ef57c255917685bb7bfb1f02f3a6481c732cc2ee41ad1f338e2a2a830", "start_char": 0, "end_char": 578, "text_sha256": "f2ed307ef57c255917685bb7bfb1f02f3a6481c732cc2ee41ad1f338e2a2a830"}
    experimental_model
    Human liver-cell, mouse and human-volunteer inflammation experiments
    exposure
    IL-6 and inflammatory stimulation
    limitations
    IL-6 dependence applies to the tested inflammatory models, not every possible inflammatory iron pathway.
    nutrient_topic
    Iron research collection; topical membership is not evidence of a direct dietary effect. · Iron
    organism
    Humans and mice
    plain_language
    Low blood iron during inflammation is a distribution response, not by itself proof of low total-body stores.
    primary_references
    [iron-p15124018] IL-6 mediates hypoferremia of inflammation by inducing the synthesis of the iron regulatory hormone hepcidin. (2004). https://pubmed.ncbi.nlm.nih.gov/15124018/ DOI: 10.1172/jci20945
    tissue_or_cell_type
    Liver and circulation
    trigger_kind
    biomarker_context Imported condition classification; unverified.

    Iron: absorption, trafficking, iron-dependent enzymes and nutrient interactions (2026-09-17) · lines 888–899

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human liver-cell, mouse and human-volunteer inflammation experiments · source_derived_draft · unverified_draft

    ### iron-inflammatory-low-serum The IL-6–hepcidin axis mediated inflammation-associated hypoferremia in the studied systems. Condition category: biomarker_context nutrient_topic: Iron research collection; topical membership is not evidence of a direct dietary effect. plain_language: Low blood iron during inflammation is a distribution response, not by itself proof of low total-body stores. organism: Humans and mice tissue_or_cell_type: Liver and circulation experimental_model: Human liver-cell, mouse and human-volunteer inflammation experiments limitations: IL-6 dependence applies to the tested inflammatory models, not every possible inflammatory iron pathway. exposure: IL-6 and inflammatory stimulation evidence_span: {"source_cache": "artifacts/iron-research/15124018.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "f2ed307ef57c255917685bb7bfb1f02f3a6481c732cc2ee41ad1f338e2a2a830", "start_char": 0, "end_char": 578, "text_sha256": "f2ed307ef57c255917685bb7bfb1f02f3a6481c732cc2ee41ad1f338e2a2a830"} [iron-p15124018] IL-6 mediates hypoferremia of inflammation by inducing the synthesis of the iron regulatory hormone hepcidin. (2004). https://pubmed.ncbi.nlm.nih.gov/15124018/ DOI: 10.1172/jci20945
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Vitamin A-deficient rats showed lower hepatic Hamp transcripts despite increased Bmp6 and Hfe2 transcripts.

    Vitamin A → HAMP mRNA source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    nutrient_deficiency Imported condition classification; unverified.
    cross_nutrient
    Vitamin A/iron -> hepcidin regulation.
    experimental_model
    Dietary comparison; hepatic mRNA.
    limitations
    Not a direct demonstration of BMP signaling flux or circulating hepcidin.
    nutrient_topic
    Vitamin A research collection; topical membership is not evidence of a direct dietary effect. · Vitamin A
    organism
    Rattus norvegicus
    plain_language
    The measured regulatory signals did not all move in the same direction.
    primary_references
    [va-cunha2016] Vitamin A deficiency modulates iron metabolism independent of hemojuvelin (Hfe2) and bone morphogenetic protein 6 (Bmp6) transcript levels (2016). https://pubmed.ncbi.nlm.nih.gov/27551308/ DOI: 10.1186/s12263-016-0519-4
    tissue_or_cell_type
    Liver
    trigger_kind
    nutrient_deficiency Imported condition classification; unverified.

    Vitamin A: forms, mechanisms, deficiency and excess (2026-09-17) · lines 1766–1776

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Dietary comparison; hepatic mRNA. · source_derived_draft · unverified_draft

    ### va-deficiency-hepcidin-transcript Vitamin A-deficient rats showed lower hepatic Hamp transcripts despite increased Bmp6 and Hfe2 transcripts. Condition category: nutrient_deficiency nutrient_topic: Vitamin A research collection; topical membership is not evidence of a direct dietary effect. plain_language: The measured regulatory signals did not all move in the same direction. organism: Rattus norvegicus tissue_or_cell_type: Liver experimental_model: Dietary comparison; hepatic mRNA. limitations: Not a direct demonstration of BMP signaling flux or circulating hepcidin. cross_nutrient: Vitamin A/iron -> hepcidin regulation. [va-cunha2016] Vitamin A deficiency modulates iron metabolism independent of hemojuvelin (Hfe2) and bone morphogenetic protein 6 (Bmp6) transcript levels (2016). https://pubmed.ncbi.nlm.nih.gov/27551308/ DOI: 10.1186/s12263-016-0519-4
    Complete structured claim and evidence

  2. IL-6 induced hepcidin in the tested human liver-cell, mouse and volunteer systems.

    IL6 → Hepcidin expression source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    biomarker_context Imported condition classification; unverified.
    evidence_span
    {"source_cache": "artifacts/iron-research/15124018.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "f2ed307ef57c255917685bb7bfb1f02f3a6481c732cc2ee41ad1f338e2a2a830", "start_char": 0, "end_char": 578, "text_sha256": "f2ed307ef57c255917685bb7bfb1f02f3a6481c732cc2ee41ad1f338e2a2a830"}
    experimental_model
    Human liver-cell, mouse and human-volunteer inflammation experiments
    exposure
    IL-6 and inflammatory stimulation
    limitations
    IL-6 dependence applies to the tested inflammatory models, not every possible inflammatory iron pathway.
    nutrient_topic
    Iron research collection; topical membership is not evidence of a direct dietary effect. · Iron
    organism
    Humans and mice
    plain_language
    Inflammation can turn up the hormone that restricts iron release.
    primary_references
    [iron-p15124018] IL-6 mediates hypoferremia of inflammation by inducing the synthesis of the iron regulatory hormone hepcidin. (2004). https://pubmed.ncbi.nlm.nih.gov/15124018/ DOI: 10.1172/jci20945
    tissue_or_cell_type
    Liver and circulation
    trigger_kind
    biomarker_context Imported condition classification; unverified.

    Iron: absorption, trafficking, iron-dependent enzymes and nutrient interactions (2026-09-17) · lines 875–886

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human liver-cell, mouse and human-volunteer inflammation experiments · source_derived_draft · unverified_draft

    ### iron-il6-hepcidin IL-6 induced hepcidin in the tested human liver-cell, mouse and volunteer systems. Condition category: biomarker_context nutrient_topic: Iron research collection; topical membership is not evidence of a direct dietary effect. plain_language: Inflammation can turn up the hormone that restricts iron release. organism: Humans and mice tissue_or_cell_type: Liver and circulation experimental_model: Human liver-cell, mouse and human-volunteer inflammation experiments limitations: IL-6 dependence applies to the tested inflammatory models, not every possible inflammatory iron pathway. exposure: IL-6 and inflammatory stimulation evidence_span: {"source_cache": "artifacts/iron-research/15124018.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "f2ed307ef57c255917685bb7bfb1f02f3a6481c732cc2ee41ad1f338e2a2a830", "start_char": 0, "end_char": 578, "text_sha256": "f2ed307ef57c255917685bb7bfb1f02f3a6481c732cc2ee41ad1f338e2a2a830"} [iron-p15124018] IL-6 mediates hypoferremia of inflammation by inducing the synthesis of the iron regulatory hormone hepcidin. (2004). https://pubmed.ncbi.nlm.nih.gov/15124018/ DOI: 10.1172/jci20945
    Complete structured claim and evidence

  3. Iron increased hepcidin affinity for ferroportin approximately 80-fold in the measured binding system.

    Ferrous iron → Ferroportin / SLC40A1 source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/iron-research/32814342.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "8de67bc7ca2250cfab2f2cb71c2da16b4806c05cf5d4b6e648b191596b6e0da0", "start_char": 0, "end_char": 1365, "text_sha256": "8de67bc7ca2250cfab2f2cb71c2da16b4806c05cf5d4b6e648b191596b6e0da0"}
    experimental_model
    Cryo-EM in lipid nanodiscs and binding/transport analysis
    exposure
    Apo state, hepcidin and cobalt mimetic; iron-dependent affinity measurements
    limitations
    Metal sites include a cobalt-bound structural preparation; the degradation-selectivity model is an interpretation, not proof that only loaded molecules are ever degraded.
    nutrient_topic
    Iron research collection; topical membership is not evidence of a direct dietary effect. · Iron
    organism
    Human ferroportin
    plain_language
    The exporter’s metal-loading state changes how strongly the regulator binds.
    primary_references
    [iron-p32814342] Structure of hepcidin-bound ferroportin reveals iron homeostatic mechanisms. (2020). https://pubmed.ncbi.nlm.nih.gov/32814342/ DOI: 10.1038/s41586-020-2668-z
    tissue_or_cell_type
    Purified membrane transporter

    Iron: absorption, trafficking, iron-dependent enzymes and nutrient interactions (2026-09-17) · lines 758–769

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Cryo-EM in lipid nanodiscs and binding/transport analysis · source_derived_draft · unverified_draft

    ### iron-iron-hepcidin-affinity Iron increased hepcidin affinity for ferroportin approximately 80-fold in the measured binding system. Condition category: normal nutrient_topic: Iron research collection; topical membership is not evidence of a direct dietary effect. plain_language: The exporter’s metal-loading state changes how strongly the regulator binds. organism: Human ferroportin tissue_or_cell_type: Purified membrane transporter experimental_model: Cryo-EM in lipid nanodiscs and binding/transport analysis limitations: Metal sites include a cobalt-bound structural preparation; the degradation-selectivity model is an interpretation, not proof that only loaded molecules are ever degraded. exposure: Apo state, hepcidin and cobalt mimetic; iron-dependent affinity measurements evidence_span: {"source_cache": "artifacts/iron-research/32814342.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "8de67bc7ca2250cfab2f2cb71c2da16b4806c05cf5d4b6e648b191596b6e0da0", "start_char": 0, "end_char": 1365, "text_sha256": "8de67bc7ca2250cfab2f2cb71c2da16b4806c05cf5d4b6e648b191596b6e0da0"} [iron-p32814342] Structure of hepcidin-bound ferroportin reveals iron homeostatic mechanisms. (2020). https://pubmed.ncbi.nlm.nih.gov/32814342/ DOI: 10.1038/s41586-020-2668-z
    Complete structured claim and evidence

  4. Doses of at least 60 mg raised hepcidin at 24 hours and reduced fractional absorption of subsequent iron by 35–45%.

    Ferrous sulfate → Circulating hepcidin concentration source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/iron-research/26289639.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "67eb8d47c0df5398c03a2a73fdd7698efc0467e85db72cfdcc829fab72b90096", "start_char": 0, "end_char": 1708, "text_sha256": "67eb8d47c0df5398c03a2a73fdd7698efc0467e85db72cfdcc829fab72b90096"}
    experimental_model
    Stable-isotope dose studies
    exposure
    40–240 mg oral labeled ferrous sulfate; successive or twice-daily doses
    limitations
    Short-term fractional absorption is not equivalent to long-term hemoglobin recovery; dose values describe the experiment.
    nutrient_topic
    Iron research collection; topical membership is not evidence of a direct dietary effect. · Iron
    organism
    54 nonanemic iron-depleted young women
    plain_language
    An iron dose can temporarily make the next dose harder to absorb.
    primary_references
    [iron-p26289639] Oral iron supplements increase hepcidin and decrease iron absorption from daily or twice-daily doses in iron-depleted young women. (2015). https://pubmed.ncbi.nlm.nih.gov/26289639/ DOI: 10.1182/blood-2015-05-642223
    tissue_or_cell_type
    Iron absorption and circulating hepcidin

    Iron: absorption, trafficking, iron-dependent enzymes and nutrient interactions (2026-09-17) · lines 1278–1289

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Stable-isotope dose studies · source_derived_draft · unverified_draft

    ### iron-oral-iron-hepcidin Doses of at least 60 mg raised hepcidin at 24 hours and reduced fractional absorption of subsequent iron by 35–45%. Condition category: normal nutrient_topic: Iron research collection; topical membership is not evidence of a direct dietary effect. plain_language: An iron dose can temporarily make the next dose harder to absorb. organism: 54 nonanemic iron-depleted young women tissue_or_cell_type: Iron absorption and circulating hepcidin experimental_model: Stable-isotope dose studies limitations: Short-term fractional absorption is not equivalent to long-term hemoglobin recovery; dose values describe the experiment. exposure: 40–240 mg oral labeled ferrous sulfate; successive or twice-daily doses evidence_span: {"source_cache": "artifacts/iron-research/26289639.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "67eb8d47c0df5398c03a2a73fdd7698efc0467e85db72cfdcc829fab72b90096", "start_char": 0, "end_char": 1708, "text_sha256": "67eb8d47c0df5398c03a2a73fdd7698efc0467e85db72cfdcc829fab72b90096"} [iron-p26289639] Oral iron supplements increase hepcidin and decrease iron absorption from daily or twice-daily doses in iron-depleted young women. (2015). https://pubmed.ncbi.nlm.nih.gov/26289639/ DOI: 10.1182/blood-2015-05-642223
    Complete structured claim and evidence

  5. Germline TMPRSS6 mutations caused iron-deficiency anemia refractory to oral iron therapy in the studied families.

    Human matriptase-2 / TMPRSS6 → Microcytic anemia refractory to oral iron in genetic iron-handling disorders source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_span
    {"source_cache": "artifacts/iron-research/18408718.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "26d5ec56d21c4675127615cc14ef1b167eef0d8c5e2fe7d69a5b316f4e06011e", "start_char": 0, "end_char": 468, "text_sha256": "26d5ec56d21c4675127615cc14ef1b167eef0d8c5e2fe7d69a5b316f4e06011e"}
    experimental_model
    Family genetic investigation
    exposure
    Germline TMPRSS6 variants
    limitations
    Rare inherited disorder; not an explanation for every failure of oral iron.
    nutrient_topic
    Iron research collection; topical membership is not evidence of a direct dietary effect. · Iron
    organism
    Humans with refractory iron-deficiency anemia
    plain_language
    The problem can be the body’s control of iron availability, rather than simply too little iron supplied.
    primary_references
    [iron-p18408718] Mutations in TMPRSS6 cause iron-refractory iron deficiency anemia (IRIDA). (2008). https://pubmed.ncbi.nlm.nih.gov/18408718/ DOI: 10.1038/ng.130
    tissue_or_cell_type
    Systemic iron regulation
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Iron: absorption, trafficking, iron-dependent enzymes and nutrient interactions (2026-09-17) · lines 1018–1029

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Family genetic investigation · source_derived_draft · unverified_draft

    ### iron-tmprss6-irida Germline TMPRSS6 mutations caused iron-deficiency anemia refractory to oral iron therapy in the studied families. Condition category: machinery_impairment nutrient_topic: Iron research collection; topical membership is not evidence of a direct dietary effect. plain_language: The problem can be the body’s control of iron availability, rather than simply too little iron supplied. organism: Humans with refractory iron-deficiency anemia tissue_or_cell_type: Systemic iron regulation experimental_model: Family genetic investigation limitations: Rare inherited disorder; not an explanation for every failure of oral iron. exposure: Germline TMPRSS6 variants evidence_span: {"source_cache": "artifacts/iron-research/18408718.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "26d5ec56d21c4675127615cc14ef1b167eef0d8c5e2fe7d69a5b316f4e06011e", "start_char": 0, "end_char": 468, "text_sha256": "26d5ec56d21c4675127615cc14ef1b167eef0d8c5e2fe7d69a5b316f4e06011e"} [iron-p18408718] Mutations in TMPRSS6 cause iron-refractory iron deficiency anemia (IRIDA). (2008). https://pubmed.ncbi.nlm.nih.gov/18408718/ DOI: 10.1038/ng.130
    Complete structured claim and evidence

In the sources

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    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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