Component

Mammalian ferritin protein complexes

Ferritin detected without assigning a heavy/light-subunit composition or a single species protein sequence.

5 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. Ferritin staining increased in activated microglia and vessels within selectively vulnerable regions of depleted mice and rats.

    Thiamine (vitamin B1) → Mammalian ferritin protein complexes source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    nutrient_deficiency Imported condition classification; unverified.
    cross_nutrient
    Local iron storage changes accompany severe thiamine disruption; this is not evidence of systemic iron deficiency or overload.
    evidence_location
    Results: Ferritin, Iron, and Microglial Responses to TD; Figures 5-6
    evidence_span
    intense ferritin immunoreactivity
    experimental_model
    Adult male C57BL/6 mice and Fischer 344 Brown Norway F1 rats; thiamine-deficient diet plus pyrithiamine 0.5 mg/kg/day intraperitoneally; staged brain histochemistry.
    exposure
    Dietary thiamine removal plus daily pyrithiamine in mice or rats
    limitations
    Staining does not distinguish ferritin subunits or prove ferritin causes injury; serum ferritin was not measured.
    nutrient_topic
    Thiamine research collection; topical membership is not evidence of a direct dietary effect. · Thiamine (vitamin B1)
    organism
    Mus musculus; Rattus norvegicus
    plain_language
    Iron-storage protein accumulated locally alongside the iron signal.
    primary_references
    [calingasan-1998-bbb-iron-nos] Induction of nitric oxide synthase and microglial responses precede selective cell death induced by chronic impairment of oxidative metabolism (1998). https://pmc.ncbi.nlm.nih.gov/articles/PMC1852979/ DOI: 10.1016/S0002-9440(10)65602-7
    tissue_or_cell_type
    Vulnerable brain microglia and microvessels
    trigger_kind
    nutrient_deficiency Imported condition classification; unverified.

    Thiamine: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 1240–1253

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Adult male C57BL/6 mice and Fischer 344 Brown Norway F1 rats; thiamine-deficient diet plus pyrithiamine 0.5 mg/kg/day intraperitoneally; staged brain histochemistry. · source_derived_draft · unverified_draft

    ### thiamine-def-ferritin-regional-increase Ferritin staining increased in activated microglia and vessels within selectively vulnerable regions of depleted mice and rats. Condition category: nutrient_deficiency nutrient_topic: Thiamine research collection; topical membership is not evidence of a direct dietary effect. plain_language: Iron-storage protein accumulated locally alongside the iron signal. organism: Mus musculus; Rattus norvegicus tissue_or_cell_type: Vulnerable brain microglia and microvessels experimental_model: Adult male C57BL/6 mice and Fischer 344 Brown Norway F1 rats; thiamine-deficient diet plus pyrithiamine 0.5 mg/kg/day intraperitoneally; staged brain histochemistry. limitations: Staining does not distinguish ferritin subunits or prove ferritin causes injury; serum ferritin was not measured. evidence_location: Results: Ferritin, Iron, and Microglial Responses to TD; Figures 5-6 evidence_span: intense ferritin immunoreactivity cross_nutrient: Local iron storage changes accompany severe thiamine disruption; this is not evidence of systemic iron deficiency or overload. exposure: Dietary thiamine removal plus daily pyrithiamine in mice or rats [calingasan-1998-bbb-iron-nos] Induction of nitric oxide synthase and microglial responses precede selective cell death induced by chronic impairment of oxidative metabolism (1998). https://pmc.ncbi.nlm.nih.gov/articles/PMC1852979/ DOI: 10.1016/S0002-9440(10)65602-7
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Thirty minutes after iron dosing, riboflavin-deficient rats had less mucosal 59Fe but unchanged relative partition between ferritin and transferrin.

    Riboflavin (vitamin B2) → Intestinal mucosal iron partition source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    nutrient_deficiency Imported condition classification; unverified.
    cross_nutrient
    Constrains the proposed B2-iron mechanism.
    evidence_location
    Abstract
    experimental_model
    Dietary riboflavin-deficient male rats versus age-/weight-matched controls; intragastric 59Fe and mucosal brush-border vesicles.
    exposure
    Dietary riboflavin deficiency; 30-minute tracer endpoint
    limitations
    Only the reported pools and time point were compared.
    nutrient_topic
    Riboflavin research collection; topical membership is not evidence of a direct dietary effect. · Riboflavin (vitamin B2)
    organism
    Rattus norvegicus
    plain_language
    The uptake decrease was not explained by the tested redistribution hypothesis.
    primary_references
    [butler1993] Comparison of changes in the uptake and mucosal processing of iron in riboflavin-deficient rats. (1993). https://pubmed.ncbi.nlm.nih.gov/8358336/
    tissue_or_cell_type
    Intestinal mucosa
    trigger_kind
    nutrient_deficiency Imported condition classification; unverified.

    Riboflavin: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 1430–1442

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Dietary riboflavin-deficient male rats versus age-/weight-matched controls; intragastric 59Fe and mucosal brush-border vesicles. · source_derived_draft · unverified_draft

    ### b2-rat-iron-partition-preserved Thirty minutes after iron dosing, riboflavin-deficient rats had less mucosal 59Fe but unchanged relative partition between ferritin and transferrin. Condition category: nutrient_deficiency nutrient_topic: Riboflavin research collection; topical membership is not evidence of a direct dietary effect. plain_language: The uptake decrease was not explained by the tested redistribution hypothesis. organism: Rattus norvegicus tissue_or_cell_type: Intestinal mucosa experimental_model: Dietary riboflavin-deficient male rats versus age-/weight-matched controls; intragastric 59Fe and mucosal brush-border vesicles. limitations: Only the reported pools and time point were compared. exposure: Dietary riboflavin deficiency; 30-minute tracer endpoint cross_nutrient: Constrains the proposed B2-iron mechanism. evidence_location: Abstract [butler1993] Comparison of changes in the uptake and mucosal processing of iron in riboflavin-deficient rats. (1993). https://pubmed.ncbi.nlm.nih.gov/8358336/
    Complete structured claim and evidence

  2. Ferritin-heavy-chain overexpression in H1299 cells lowered labile iron and increased clonogenic survival after pharmacological ascorbate, supporting a protective role of intracellular iron sequestration in this setting.

    Ferritin heavy chain → Cancer-cell clonogenic survival source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    true
    evidence_location
    Figure 6I–L
    experimental_model
    H1299 adenoviral ferritin-heavy-chain versus empty-vector cultures; calcein/BIP and clonogenic assays
    exposure
    20-MOI ferritin-heavy-chain expression 36 h before experiment; 5 pmol/cell (approximately 2–3 mM) ascorbate for 1 h.
    limitations
    Engineered overexpression is not dietary iron deficiency or ordinary ferritin concentration; serum ferritin does not measure this intracellular intervention.
    nutrient_topic
    Vitamin C research collection; topical membership is not evidence of a direct dietary effect. · Vitamin C
    organism
    Homo sapiens
    plain_language
    Locking more iron into ferritin protected these lung cancer cells from the exposure.
    primary_references
    [c-reg-schoenfeld] O2⋅- and H2O2-Mediated Disruption of Fe Metabolism Causes the Differential Susceptibility of NSCLC and GBM Cancer Cells to Pharmacological Ascorbate. (2017). https://pubmed.ncbi.nlm.nih.gov/28366679/ DOI: 10.1016/j.ccell.2017.02.018
    tissue_or_cell_type
    NSCLC cells

    Vitamin C: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 1369–1381

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · H1299 adenoviral ferritin-heavy-chain versus empty-vector cultures; calcein/BIP and clonogenic assays · source_derived_draft · unverified_draft

    ### c-reg-ferritin-heavy-protects Ferritin-heavy-chain overexpression in H1299 cells lowered labile iron and increased clonogenic survival after pharmacological ascorbate, supporting a protective role of intracellular iron sequestration in this setting. Condition category: normal nutrient_topic: Vitamin C research collection; topical membership is not evidence of a direct dietary effect. plain_language: Locking more iron into ferritin protected these lung cancer cells from the exposure. organism: Homo sapiens tissue_or_cell_type: NSCLC cells experimental_model: H1299 adenoviral ferritin-heavy-chain versus empty-vector cultures; calcein/BIP and clonogenic assays limitations: Engineered overexpression is not dietary iron deficiency or ordinary ferritin concentration; serum ferritin does not measure this intracellular intervention. exposure: 20-MOI ferritin-heavy-chain expression 36 h before experiment; 5 pmol/cell (approximately 2–3 mM) ascorbate for 1 h. cross_nutrient: true evidence_location: Figure 6I–L [c-reg-schoenfeld] O2⋅- and H2O2-Mediated Disruption of Fe Metabolism Causes the Differential Susceptibility of NSCLC and GBM Cancer Cells to Pharmacological Ascorbate. (2017). https://pubmed.ncbi.nlm.nih.gov/28366679/ DOI: 10.1016/j.ccell.2017.02.018
    Complete structured claim and evidence

  3. PCBP1 depletion inhibited ferritin iron loading and increased cytosolic iron pools in human cells.

    Human poly(rC)-binding protein 1 / PCBP1 → Cellular labile iron pool source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_span
    {"source_cache": "artifacts/iron-research/18511687.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d8000e5c5f59dc72e9697d5aac77ce5070a1c92f6cada7e863088ec917684c68", "start_char": 0, "end_char": 703, "text_sha256": "d8000e5c5f59dc72e9697d5aac77ce5070a1c92f6cada7e863088ec917684c68"}
    experimental_model
    Yeast expression, in-vitro binding/loading and human-cell depletion
    exposure
    PCBP1 expression and depletion
    limitations
    Chaperone-mediated distribution is distinct from total cellular iron.
    nutrient_topic
    Iron research collection; topical membership is not evidence of a direct dietary effect. · Iron
    organism
    Human PCBP1 and ferritin in yeast and human cells
    plain_language
    Less iron in storage can coexist with more potentially reactive iron outside the store.
    primary_references
    [iron-p18511687] A cytosolic iron chaperone that delivers iron to ferritin. (2008). https://pubmed.ncbi.nlm.nih.gov/18511687/ DOI: 10.1126/science.1157643
    tissue_or_cell_type
    Cytosol
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Iron: absorption, trafficking, iron-dependent enzymes and nutrient interactions (2026-09-17) · lines 602–613

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Yeast expression, in-vitro binding/loading and human-cell depletion · source_derived_draft · unverified_draft

    ### iron-pcbp-depletion PCBP1 depletion inhibited ferritin iron loading and increased cytosolic iron pools in human cells. Condition category: machinery_impairment nutrient_topic: Iron research collection; topical membership is not evidence of a direct dietary effect. plain_language: Less iron in storage can coexist with more potentially reactive iron outside the store. organism: Human PCBP1 and ferritin in yeast and human cells tissue_or_cell_type: Cytosol experimental_model: Yeast expression, in-vitro binding/loading and human-cell depletion limitations: Chaperone-mediated distribution is distinct from total cellular iron. exposure: PCBP1 expression and depletion evidence_span: {"source_cache": "artifacts/iron-research/18511687.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d8000e5c5f59dc72e9697d5aac77ce5070a1c92f6cada7e863088ec917684c68", "start_char": 0, "end_char": 703, "text_sha256": "d8000e5c5f59dc72e9697d5aac77ce5070a1c92f6cada7e863088ec917684c68"} [iron-p18511687] A cytosolic iron chaperone that delivers iron to ferritin. (2008). https://pubmed.ncbi.nlm.nih.gov/18511687/ DOI: 10.1126/science.1157643
    Complete structured claim and evidence

  4. PCBP1 bound iron and ferritin and facilitated iron loading into ferritin in vitro and in cellular systems.

    Human poly(rC)-binding protein 1 / PCBP1 → Iron loading into cellular ferritin source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/iron-research/18511687.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d8000e5c5f59dc72e9697d5aac77ce5070a1c92f6cada7e863088ec917684c68", "start_char": 0, "end_char": 703, "text_sha256": "d8000e5c5f59dc72e9697d5aac77ce5070a1c92f6cada7e863088ec917684c68"}
    experimental_model
    Yeast expression, in-vitro binding/loading and human-cell depletion
    exposure
    PCBP1 expression and depletion
    limitations
    Chaperone-mediated distribution is distinct from total cellular iron.
    nutrient_topic
    Iron research collection; topical membership is not evidence of a direct dietary effect. · Iron
    organism
    Human PCBP1 and ferritin in yeast and human cells
    plain_language
    Iron has a delivery protein for safe storage, rather than simply drifting into every target.
    primary_references
    [iron-p18511687] A cytosolic iron chaperone that delivers iron to ferritin. (2008). https://pubmed.ncbi.nlm.nih.gov/18511687/ DOI: 10.1126/science.1157643
    tissue_or_cell_type
    Cytosol

    Iron: absorption, trafficking, iron-dependent enzymes and nutrient interactions (2026-09-17) · lines 589–600

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Yeast expression, in-vitro binding/loading and human-cell depletion · source_derived_draft · unverified_draft

    ### iron-pcbp-loads-ferritin PCBP1 bound iron and ferritin and facilitated iron loading into ferritin in vitro and in cellular systems. Condition category: normal nutrient_topic: Iron research collection; topical membership is not evidence of a direct dietary effect. plain_language: Iron has a delivery protein for safe storage, rather than simply drifting into every target. organism: Human PCBP1 and ferritin in yeast and human cells tissue_or_cell_type: Cytosol experimental_model: Yeast expression, in-vitro binding/loading and human-cell depletion limitations: Chaperone-mediated distribution is distinct from total cellular iron. exposure: PCBP1 expression and depletion evidence_span: {"source_cache": "artifacts/iron-research/18511687.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d8000e5c5f59dc72e9697d5aac77ce5070a1c92f6cada7e863088ec917684c68", "start_char": 0, "end_char": 703, "text_sha256": "d8000e5c5f59dc72e9697d5aac77ce5070a1c92f6cada7e863088ec917684c68"} [iron-p18511687] A cytosolic iron chaperone that delivers iron to ferritin. (2008). https://pubmed.ncbi.nlm.nih.gov/18511687/ DOI: 10.1126/science.1157643
    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.

    Evidence, AI assistance and curation standards