Component

Human transferrin bound to vanadium(V/IV)

Context-specific entity; species, compartment and exposure are stated on each claim.

3 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. 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. 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

Where it participates (unsigned role)

  1. V(V) and V(IV) bound vacant transferrin iron-binding sites in culture medium even with a 20-fold molar excess of albumin, without displacing already-bound Fe(III) under those conditions.

    Vanadate(V), protonation/speciation dependent → Human serum transferrin / TF source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Human transferrin binding experiments under normoxic conditions.
    limitations
    Does not establish systemic iron deficiency or competition magnitude at dietary exposures.
    nutrient_topic
    Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
    plain_language
    Vanadium can occupy available metal-binding sites without stripping out all bound iron.
    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 190–196

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human transferrin binding experiments under normoxic conditions. · source_derived_draft · unverified_draft

    ## vanadium-tf-binding Vanadium can occupy available metal-binding sites without stripping out all bound iron. V(V) and V(IV) bound vacant transferrin iron-binding sites in culture medium even with a 20-fold molar excess of albumin, without displacing already-bound Fe(III) under those conditions. Model: Human transferrin binding experiments under normoxic conditions. Limitations: Does not establish systemic iron deficiency or competition magnitude at dietary exposures. 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

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