Component

Ferroportin / SLC40A1

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

6 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. 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

  2. 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

  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

Where it participates (unsigned role)

  1. Vitamin A deficiency reduced intestinal Fpn1 transcripts in the same rat study.

    Vitamin A → SLC40A1 mRNA source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    nutrient_deficiency Imported condition classification; unverified.
    experimental_model
    Intestinal mRNA assay.
    limitations
    Does not quantify ferroportin membrane protein or iron-export flux.
    nutrient_topic
    Vitamin A research collection; topical membership is not evidence of a direct dietary effect. · Vitamin A
    organism
    Rattus norvegicus
    plain_language
    Expression of an iron-export component changed alongside systemic signals.
    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
    Small intestine
    trigger_kind
    nutrient_deficiency Imported condition classification; unverified.

    Vitamin A: forms, mechanisms, deficiency and excess (2026-09-17) · lines 1778–1787

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

    ### va-deficiency-ferroportin-transcript Vitamin A deficiency reduced intestinal Fpn1 transcripts in the same rat study. Condition category: nutrient_deficiency nutrient_topic: Vitamin A research collection; topical membership is not evidence of a direct dietary effect. plain_language: Expression of an iron-export component changed alongside systemic signals. organism: Rattus norvegicus tissue_or_cell_type: Small intestine experimental_model: Intestinal mRNA assay. limitations: Does not quantify ferroportin membrane protein or iron-export flux. [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. 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

  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

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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