Component

Human transferrin receptor 1 / TFRC

Human transferrin receptor 1 / TFRC. Species, exposure and limitations are retained in each linked claim.

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 it acts on

  1. Binding of chromium-loaded transferrin to soluble transferrin receptor accelerated chromium release from both sites at acidic pH.

    Human transferrin receptor 1 / TFRC → Chromium release from transferrin source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/chromium-research/31669693.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "bdb962ff7838d36dfbc2cd2df4eed4e07c81ebd824c6e95096c5d7069ec32835", "start_char": 0, "end_char": 1635, "text_sha256": "bdb962ff7838d36dfbc2cd2df4eed4e07c81ebd824c6e95096c5d7069ec32835"}
    experimental_model
    Purified human transferrin release kinetics and soluble receptor interaction
    exposure
    pH 4.5 and 5.5; weak/tight binding sites; biological chelators and soluble transferrin receptor
    limitations
    The study establishes release kinetics, not the entire in-vivo pathway. The molecular route from the endosomal lumen to cytosol remains unresolved.
    nutrient_topic
    Chromium research collection; topical membership is not evidence of a direct dietary effect. · Chromium
    organism
    Human proteins in vitro
    plain_language
    The receptor changed the carrier’s behavior and helped it release chromium in this assay.
    primary_references
    [chromium-p31669693] Release of trivalent chromium from serum transferrin is sufficiently rapid to be physiologically relevant. (2020). https://pubmed.ncbi.nlm.nih.gov/31669693/ DOI: 10.1016/j.jinorgbio.2019.110901
    tissue_or_cell_type
    Endosome-mimicking solution

    Chromium: transport, insulin signaling, nutrient interactions and essentiality debate (2026-09-17) · lines 172–183

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified human transferrin release kinetics and soluble receptor interaction · source_derived_draft · unverified_draft

    ### chromium-receptor-accelerated-release Binding of chromium-loaded transferrin to soluble transferrin receptor accelerated chromium release from both sites at acidic pH. Condition category: normal nutrient_topic: Chromium research collection; topical membership is not evidence of a direct dietary effect. plain_language: The receptor changed the carrier’s behavior and helped it release chromium in this assay. organism: Human proteins in vitro tissue_or_cell_type: Endosome-mimicking solution experimental_model: Purified human transferrin release kinetics and soluble receptor interaction limitations: The study establishes release kinetics, not the entire in-vivo pathway. The molecular route from the endosomal lumen to cytosol remains unresolved. exposure: pH 4.5 and 5.5; weak/tight binding sites; biological chelators and soluble transferrin receptor evidence_span: {"source_cache": "artifacts/chromium-research/31669693.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "bdb962ff7838d36dfbc2cd2df4eed4e07c81ebd824c6e95096c5d7069ec32835", "start_char": 0, "end_char": 1635, "text_sha256": "bdb962ff7838d36dfbc2cd2df4eed4e07c81ebd824c6e95096c5d7069ec32835"} [chromium-p31669693] Release of trivalent chromium from serum transferrin is sufficiently rapid to be physiologically relevant. (2020). https://pubmed.ncbi.nlm.nih.gov/31669693/ DOI: 10.1016/j.jinorgbio.2019.110901
    Complete structured claim and evidence

  2. Apotransferrin bound receptors at pH 5.4 but dissociated rapidly when pH was raised to 7.0.

    Human transferrin receptor 1 / TFRC → Transferrin and transferrin-receptor recycling source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/iron-research/6300903.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "29d23cdaaacd30003c1f3e70935d7ab5ccbb1612379d6e650d356d1235438852", "start_char": 0, "end_char": 906, "text_sha256": "29d23cdaaacd30003c1f3e70935d7ab5ccbb1612379d6e650d356d1235438852"}
    experimental_model
    Receptor binding at controlled pH and transferrin cycle analysis
    exposure
    Apotransferrin and diferric transferrin binding at acidic versus neutral pH
    limitations
    The indexed abstract does not identify the cell line; its experiments support a pH-dependent trafficking model, not direct measures of whole-body iron turnover.
    nutrient_topic
    Iron research collection; topical membership is not evidence of a direct dietary effect. · Iron
    organism
    Cultured-cell transferrin receptor system
    plain_language
    Returning to the neutral cell surface allows the empty carrier to detach.
    primary_references
    [iron-p6300903] pH and the recycling of transferrin during receptor-mediated endocytosis. (1983). https://pubmed.ncbi.nlm.nih.gov/6300903/ DOI: 10.1073/pnas.80.8.2258
    tissue_or_cell_type
    Cell surface and endosomal recycling model

    Iron: absorption, trafficking, iron-dependent enzymes and nutrient interactions (2026-09-17) · lines 433–444

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Receptor binding at controlled pH and transferrin cycle analysis · source_derived_draft · unverified_draft

    ### iron-tf-recycling Apotransferrin bound receptors at pH 5.4 but dissociated rapidly when pH was raised to 7.0. Condition category: normal nutrient_topic: Iron research collection; topical membership is not evidence of a direct dietary effect. plain_language: Returning to the neutral cell surface allows the empty carrier to detach. organism: Cultured-cell transferrin receptor system tissue_or_cell_type: Cell surface and endosomal recycling model experimental_model: Receptor binding at controlled pH and transferrin cycle analysis limitations: The indexed abstract does not identify the cell line; its experiments support a pH-dependent trafficking model, not direct measures of whole-body iron turnover. exposure: Apotransferrin and diferric transferrin binding at acidic versus neutral pH evidence_span: {"source_cache": "artifacts/iron-research/6300903.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "29d23cdaaacd30003c1f3e70935d7ab5ccbb1612379d6e650d356d1235438852", "start_char": 0, "end_char": 906, "text_sha256": "29d23cdaaacd30003c1f3e70935d7ab5ccbb1612379d6e650d356d1235438852"} [iron-p6300903] pH and the recycling of transferrin during receptor-mediated endocytosis. (1983). https://pubmed.ncbi.nlm.nih.gov/6300903/ DOI: 10.1073/pnas.80.8.2258
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Vanadium binding did not increase transferrin affinity for TfR1 at pH 7.4, but disrupted conformational changes at pH 5.6 with citrate in the transferrin-cycle model.

    Human transferrin bound to vanadium(V/IV) → Endosome-like conformational change of vanadium-bound human transferrin source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Biolayer interferometry and electrophoretic model of the human transferrin cycle.
    limitations
    Return of undissociated V–transferrin to the surface is the authors’ proposed explanation, not directly imaged trafficking.
    nutrient_topic
    Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
    plain_language
    Receptor recognition and release during endosomal processing are different steps.
    primary_references
    Vanadium(V/IV)-Transferrin Binding Disrupts the Transferrin Cycle and Reduces Vanadium Uptake and Antiproliferative Activity in Human Lung Cancer Cells. · 2020 · https://pubmed.ncbi.nlm.nih.gov/32578416/ · DOI 10.1021/acs.inorgchem.0c00926

    Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 206–212

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Biolayer interferometry and electrophoretic model of the human transferrin cycle. · source_derived_draft · unverified_draft

    ## vanadium-tf-cycle Receptor recognition and release during endosomal processing are different steps. Vanadium binding did not increase transferrin affinity for TfR1 at pH 7.4, but disrupted conformational changes at pH 5.6 with citrate in the transferrin-cycle model. Model: Biolayer interferometry and electrophoretic model of the human transferrin cycle. Limitations: Return of undissociated V–transferrin to the surface is the authors’ proposed explanation, not directly imaged trafficking. Evidence access: Primary abstract Vanadium(V/IV)-Transferrin Binding Disrupts the Transferrin Cycle and Reduces Vanadium Uptake and Antiproliferative Activity in Human Lung Cancer Cells. · 2020 · https://pubmed.ncbi.nlm.nih.gov/32578416/ · DOI 10.1021/acs.inorgchem.0c00926
    Complete structured claim and evidence

  2. The vanadium adduct retained an open N-lobe and closed iron-containing C-lobe with little overall structural change.

    Human C-lobe-ferric transferrin Tyr188-linked divanadate(V) adduct → Open N-lobe conformation of monoferric human transferrin source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text
    experimental_model
    Human transferrin crystal comparison.
    limitations
    Compatibility with receptor recognition is a structural interpretation, not a completed cellular uptake cycle; not a contradiction of the A549 transport study.
    nutrient_topic
    Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
    plain_language
    A binding structure alone does not demonstrate successful cellular delivery.
    primary_references
    First crystal structure of an adduct formed upon reaction of a vanadium compound with human serum transferrin. · 2026 · https://pubmed.ncbi.nlm.nih.gov/41545537/ · DOI 10.1038/s42004-026-01891-1

    Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 222–228

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human transferrin crystal comparison. · source_derived_draft · unverified_draft

    ## vanadium-tf-open-lobe A binding structure alone does not demonstrate successful cellular delivery. The vanadium adduct retained an open N-lobe and closed iron-containing C-lobe with little overall structural change. Model: Human transferrin crystal comparison. Limitations: Compatibility with receptor recognition is a structural interpretation, not a completed cellular uptake cycle; not a contradiction of the A549 transport study. Evidence access: Primary full text First crystal structure of an adduct formed upon reaction of a vanadium compound with human serum transferrin. · 2026 · https://pubmed.ncbi.nlm.nih.gov/41545537/ · DOI 10.1038/s42004-026-01891-1
    Complete structured claim and evidence

  3. Transferrin binding reduced vanadium uptake and antiproliferative activity in human A549 cells.

    Human transferrin bound to vanadium(V/IV) → Vanadium uptake in human A549 cells source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Human lung-cancer cell uptake and proliferation assays.
    limitations
    Does not establish every tissue’s uptake route or clinical efficacy.
    nutrient_topic
    Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
    plain_language
    Binding to a carrier protein can reduce delivery rather than improve it.
    primary_references
    Vanadium(V/IV)-Transferrin Binding Disrupts the Transferrin Cycle and Reduces Vanadium Uptake and Antiproliferative Activity in Human Lung Cancer Cells. · 2020 · https://pubmed.ncbi.nlm.nih.gov/32578416/ · DOI 10.1021/acs.inorgchem.0c00926

    Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 198–204

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human lung-cancer cell uptake and proliferation assays. · source_derived_draft · unverified_draft

    ## vanadium-tf-uptake-reduction Binding to a carrier protein can reduce delivery rather than improve it. Transferrin binding reduced vanadium uptake and antiproliferative activity in human A549 cells. Model: Human lung-cancer cell uptake and proliferation assays. Limitations: Does not establish every tissue’s uptake route or clinical efficacy. Evidence access: Primary abstract Vanadium(V/IV)-Transferrin Binding Disrupts the Transferrin Cycle and Reduces Vanadium Uptake and Antiproliferative Activity in Human Lung Cancer Cells. · 2020 · https://pubmed.ncbi.nlm.nih.gov/32578416/ · DOI 10.1021/acs.inorgchem.0c00926
    Complete structured claim and evidence

  4. The transferrin-cycle model supported by the binding experiments releases iron in acidified endosomes while apotransferrin remains receptor-bound.

    Human serum transferrin / TF → Transferrin-dependent endosomal iron delivery to cytosol source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/iron-research/6300903.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "29d23cdaaacd30003c1f3e70935d7ab5ccbb1612379d6e650d356d1235438852", "start_char": 0, "end_char": 906, "text_sha256": "29d23cdaaacd30003c1f3e70935d7ab5ccbb1612379d6e650d356d1235438852"}
    experimental_model
    Receptor binding at controlled pH and transferrin cycle analysis
    exposure
    Apotransferrin and diferric transferrin binding at acidic versus neutral pH
    limitations
    The indexed abstract does not identify the cell line; its experiments support a pH-dependent trafficking model, not direct measures of whole-body iron turnover.
    nutrient_topic
    Iron research collection; topical membership is not evidence of a direct dietary effect. · Iron
    organism
    Cultured-cell transferrin receptor system
    plain_language
    The carrier gives up its iron inside an acidic compartment but stays attached to its return transport.
    primary_references
    [iron-p6300903] pH and the recycling of transferrin during receptor-mediated endocytosis. (1983). https://pubmed.ncbi.nlm.nih.gov/6300903/ DOI: 10.1073/pnas.80.8.2258
    tissue_or_cell_type
    Cell surface and endosomal recycling model

    Iron: absorption, trafficking, iron-dependent enzymes and nutrient interactions (2026-09-17) · lines 420–431

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Receptor binding at controlled pH and transferrin cycle analysis · source_derived_draft · unverified_draft

    ### iron-tf-acidic-release The transferrin-cycle model supported by the binding experiments releases iron in acidified endosomes while apotransferrin remains receptor-bound. Condition category: normal nutrient_topic: Iron research collection; topical membership is not evidence of a direct dietary effect. plain_language: The carrier gives up its iron inside an acidic compartment but stays attached to its return transport. organism: Cultured-cell transferrin receptor system tissue_or_cell_type: Cell surface and endosomal recycling model experimental_model: Receptor binding at controlled pH and transferrin cycle analysis limitations: The indexed abstract does not identify the cell line; its experiments support a pH-dependent trafficking model, not direct measures of whole-body iron turnover. exposure: Apotransferrin and diferric transferrin binding at acidic versus neutral pH evidence_span: {"source_cache": "artifacts/iron-research/6300903.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "29d23cdaaacd30003c1f3e70935d7ab5ccbb1612379d6e650d356d1235438852", "start_char": 0, "end_char": 906, "text_sha256": "29d23cdaaacd30003c1f3e70935d7ab5ccbb1612379d6e650d356d1235438852"} [iron-p6300903] pH and the recycling of transferrin during receptor-mediated endocytosis. (1983). https://pubmed.ncbi.nlm.nih.gov/6300903/ DOI: 10.1073/pnas.80.8.2258
    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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