Component

Oxovanadium(IV) / vanadyl

Context-specific entity; species, compartment and exposure are stated on each 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. V(IV) generated by ascorbate/vanadate chemistry produced hydroperoxide-derived radicals from cumene hydroperoxide.

    Oxovanadium(IV) / vanadyl → Radicals derived from hydroperoxide in vanadium assays source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Cell-free model-hydroperoxide assay.
    limitations
    Cumene hydroperoxide is a model reagent, not direct measurement of membrane injury in humans.
    nutrient_topic
    Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
    plain_language
    The same redox system can also react with a model lipid peroxide.
    primary_references
    One-electron reduction of vanadate by ascorbate and related free radical generation at physiological pH. · 1994 · https://pubmed.ncbi.nlm.nih.gov/8051539/ · DOI 10.1016/0162-0134(94)85032-1

    Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 110–116

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Cell-free model-hydroperoxide assay. · source_derived_draft · unverified_draft

    ## vanadium-lipid-peroxide-radicals The same redox system can also react with a model lipid peroxide. V(IV) generated by ascorbate/vanadate chemistry produced hydroperoxide-derived radicals from cumene hydroperoxide. Model: Cell-free model-hydroperoxide assay. Limitations: Cumene hydroperoxide is a model reagent, not direct measurement of membrane injury in humans. Evidence access: Primary abstract One-electron reduction of vanadate by ascorbate and related free radical generation at physiological pH. · 1994 · https://pubmed.ncbi.nlm.nih.gov/8051539/ · DOI 10.1016/0162-0134(94)85032-1
    Complete structured claim and evidence

  2. In phosphate/ascorbate mixtures with peroxide, reduced vanadium supported hydroxyl-radical generation; omitting phosphate sharply reduced the yield.

    Oxovanadium(IV) / vanadyl → Hydroxyl-radical generation in vanadium redox assays source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Cell-free ESR spin trapping.
    limitations
    Chemical mechanism under specified reagents; not proof that vitamin C supplementation causes this injury in people.
    nutrient_topic
    Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
    plain_language
    A reductant can enable pro-oxidant chemistry when peroxide is also present.
    primary_references
    One-electron reduction of vanadate by ascorbate and related free radical generation at physiological pH. · 1994 · https://pubmed.ncbi.nlm.nih.gov/8051539/ · DOI 10.1016/0162-0134(94)85032-1

    Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 102–108

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Cell-free ESR spin trapping. · source_derived_draft · unverified_draft

    ## vanadium-peroxide-radicals A reductant can enable pro-oxidant chemistry when peroxide is also present. In phosphate/ascorbate mixtures with peroxide, reduced vanadium supported hydroxyl-radical generation; omitting phosphate sharply reduced the yield. Model: Cell-free ESR spin trapping. Limitations: Chemical mechanism under specified reagents; not proof that vitamin C supplementation causes this injury in people. Evidence access: Primary abstract One-electron reduction of vanadate by ascorbate and related free radical generation at physiological pH. · 1994 · https://pubmed.ncbi.nlm.nih.gov/8051539/ · DOI 10.1016/0162-0134(94)85032-1
    Complete structured claim and evidence

What acts on it

  1. Ascorbate generated V(IV) from vanadate in phosphate buffer at pH 7.4, but not comparably in water or the tested cacodylate buffer.

    L-Ascorbate → Oxovanadium(IV) / vanadyl source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    ESR and spin-trapping chemistry; cell-free solutions.
    limitations
    Buffer-dependent chemistry does not establish a human depletion rate or clinical interaction.
    nutrient_topic
    Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
    plain_language
    Vitamin C and phosphate together changed vanadium’s oxidation state in this assay.
    primary_references
    One-electron reduction of vanadate by ascorbate and related free radical generation at physiological pH. · 1994 · https://pubmed.ncbi.nlm.nih.gov/8051539/ · DOI 10.1016/0162-0134(94)85032-1

    Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 94–100

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · ESR and spin-trapping chemistry; cell-free solutions. · source_derived_draft · unverified_draft

    ## vanadium-ascorbate-reduction Vitamin C and phosphate together changed vanadium’s oxidation state in this assay. Ascorbate generated V(IV) from vanadate in phosphate buffer at pH 7.4, but not comparably in water or the tested cacodylate buffer. Model: ESR and spin-trapping chemistry; cell-free solutions. Limitations: Buffer-dependent chemistry does not establish a human depletion rate or clinical interaction. Evidence access: Primary abstract One-electron reduction of vanadate by ascorbate and related free radical generation at physiological pH. · 1994 · https://pubmed.ncbi.nlm.nih.gov/8051539/ · DOI 10.1016/0162-0134(94)85032-1
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. A vanadate/ascorbate/phosphate system oxidized NADH, with similar results for NADPH, through a proposed superoxide-initiated chain reaction.

    Vanadate(V), protonation/speciation dependent → NADH source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Cell-free NADH/NADPH oxidation experiments.
    limitations
    Not evidence of a measured whole-body NAD shortage.
    nutrient_topic
    Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
    plain_language
    Reducing equivalents can be consumed by a metal-dependent reaction.
    primary_references
    Vanadate-mediated oxidation of NADH: description of an in vitro system requiring ascorbate and phosphate. · 1989 · https://pubmed.ncbi.nlm.nih.gov/2735768/ · DOI 10.1016/0003-9861(89)90196-3

    Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 118–124

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Cell-free NADH/NADPH oxidation experiments. · source_derived_draft · unverified_draft

    ## vanadium-nadh-oxidation Reducing equivalents can be consumed by a metal-dependent reaction. A vanadate/ascorbate/phosphate system oxidized NADH, with similar results for NADPH, through a proposed superoxide-initiated chain reaction. Model: Cell-free NADH/NADPH oxidation experiments. Limitations: Not evidence of a measured whole-body NAD shortage. Evidence access: Primary abstract Vanadate-mediated oxidation of NADH: description of an in vitro system requiring ascorbate and phosphate. · 1989 · https://pubmed.ncbi.nlm.nih.gov/2735768/ · DOI 10.1016/0003-9861(89)90196-3
    Complete structured claim and evidence

  2. 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

  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

In the sources

Preserved passages that mention this component, quoted exactly. Open one to read it in context.

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