Component

Vanadate(V), protonation/speciation dependent

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

32 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. Vanadate at concentrations that maximally stimulated glucose transport did not significantly increase Akt activity, whereas pervanadate and insulin did.

    Vanadate(V), protonation/speciation dependent → Rat Akt protein family, isoform unresolved source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Rat muscle-cell kinase assays.
    limitations
    Akt signal is not a surrogate for the complete glucose-transport response.
    nutrient_topic
    Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
    plain_language
    Chemical form changed signaling even when glucose transport increased.
    primary_references
    Tyrosine phosphatase inhibitors, vanadate and pervanadate, stimulate glucose transport and GLUT translocation in muscle cells by a mechanism independent of phosphatidylinositol 3-kinase and protein kinase C. · 1998 · https://pubmed.ncbi.nlm.nih.gov/9792535/ · DOI 10.2337/diabetes.47.11.1676

    Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 70–76

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Rat muscle-cell kinase assays. · source_derived_draft · unverified_draft

    ## vanadium-akt-difference Chemical form changed signaling even when glucose transport increased. Vanadate at concentrations that maximally stimulated glucose transport did not significantly increase Akt activity, whereas pervanadate and insulin did. Model: Rat muscle-cell kinase assays. Limitations: Akt signal is not a surrogate for the complete glucose-transport response. Evidence access: Primary abstract Tyrosine phosphatase inhibitors, vanadate and pervanadate, stimulate glucose transport and GLUT translocation in muscle cells by a mechanism independent of phosphatidylinositol 3-kinase and protein kinase C. · 1998 · https://pubmed.ncbi.nlm.nih.gov/9792535/ · DOI 10.2337/diabetes.47.11.1676
    Complete structured claim and evidence

  2. Vanadate increased NO release above 50 micromolar in the tested rat UMR106 and mouse MC3T3-E1 osteoblast-like cultures, with a biphasic concentration response.

    Vanadate(V), protonation/speciation dependent → NO production in vanadate-exposed osteoblast-like cells source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Rodent osteoblast-like cell cultures; 2.5–100 micromolar vanadate.
    limitations
    Mixed cell models are named explicitly; NO is a proposed mediator, not proven sole cause of growth effects.
    nutrient_topic
    Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
    plain_language
    A growth-related exposure can engage nitrosative signaling at higher concentrations.
    primary_references
    Vanadate-induced nitric oxide production: role in osteoblast growth and differentiation. · 2000 · https://pubmed.ncbi.nlm.nih.gov/10988345/ · DOI 10.1016/s0014-2999(00)00356-3

    Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 326–332

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Rodent osteoblast-like cell cultures; 2.5–100 micromolar vanadate. · source_derived_draft · unverified_draft

    ## vanadium-bone-no A growth-related exposure can engage nitrosative signaling at higher concentrations. Vanadate increased NO release above 50 micromolar in the tested rat UMR106 and mouse MC3T3-E1 osteoblast-like cultures, with a biphasic concentration response. Model: Rodent osteoblast-like cell cultures; 2.5–100 micromolar vanadate. Limitations: Mixed cell models are named explicitly; NO is a proposed mediator, not proven sole cause of growth effects. Evidence access: Primary abstract Vanadate-induced nitric oxide production: role in osteoblast growth and differentiation. · 2000 · https://pubmed.ncbi.nlm.nih.gov/10988345/ · DOI 10.1016/s0014-2999(00)00356-3
    Complete structured claim and evidence

  3. Vanadate exposure depleted intracellular nonprotein sulfhydryls while increasing extracellular glutathione in human erythrocytes.

    Vanadate(V), protonation/speciation dependent → Glutathione efflux from vanadate-exposed human erythrocytes source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Isolated human erythrocytes; millimolar vanadate exposures up to four hours.
    limitations
    High ex-vivo concentrations; nonprotein sulfhydryl assays are not exclusively glutathione measurements.
    nutrient_topic
    Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
    plain_language
    Loss of an intracellular thiol pool can include export rather than only oxidation.
    primary_references
    Efflux of glutathione and glutathione complexes from human erythrocytes in response to vanadate. · 2013 · https://pubmed.ncbi.nlm.nih.gov/22824382/ · DOI 10.1016/j.bcmd.2012.07.001

    Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 158–164

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Isolated human erythrocytes; millimolar vanadate exposures up to four hours. · source_derived_draft · unverified_draft

    ## vanadium-erythrocyte-gsh Loss of an intracellular thiol pool can include export rather than only oxidation. Vanadate exposure depleted intracellular nonprotein sulfhydryls while increasing extracellular glutathione in human erythrocytes. Model: Isolated human erythrocytes; millimolar vanadate exposures up to four hours. Limitations: High ex-vivo concentrations; nonprotein sulfhydryl assays are not exclusively glutathione measurements. Evidence access: Primary abstract Efflux of glutathione and glutathione complexes from human erythrocytes in response to vanadate. · 2013 · https://pubmed.ncbi.nlm.nih.gov/22824382/ · DOI 10.1016/j.bcmd.2012.07.001
    Complete structured claim and evidence

  4. Vanadate crystallization of rat-liver F1 ATP synthase captured an ADP–vanadate–Mg transition-like state with remodeling of the catalytic P-loop region.

    Vanadate(V), protonation/speciation dependent → Rat liver F1 ATP synthase catalytic unit source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Rat liver F1 crystallography.
    limitations
    A captured structure is not proof that a given oral dose suppresses mitochondrial ATP production.
    nutrient_topic
    Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
    plain_language
    Another ATP-handling enzyme can bind the phosphate analogue.
    primary_references
    Mitochondrial ATP synthase. Crystal structure of the catalytic F1 unit in a vanadate-induced transition-like state and implications for mechanism. · 2006 · https://pubmed.ncbi.nlm.nih.gov/16531409/ · DOI 10.1074/jbc.M513369200

    Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 262–268

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Rat liver F1 crystallography. · source_derived_draft · unverified_draft

    ## vanadium-f1-transition Another ATP-handling enzyme can bind the phosphate analogue. Vanadate crystallization of rat-liver F1 ATP synthase captured an ADP–vanadate–Mg transition-like state with remodeling of the catalytic P-loop region. Model: Rat liver F1 crystallography. Limitations: A captured structure is not proof that a given oral dose suppresses mitochondrial ATP production. Evidence access: Primary abstract Mitochondrial ATP synthase. Crystal structure of the catalytic F1 unit in a vanadate-induced transition-like state and implications for mechanism. · 2006 · https://pubmed.ncbi.nlm.nih.gov/16531409/ · DOI 10.1074/jbc.M513369200
    Complete structured claim and evidence

  5. Vanadate and pervanadate stimulated glucose transport and GLUT movement to the plasma membrane in rat L6 myotubes.

    Vanadate(V), protonation/speciation dependent → Glucose transport in vanadate-treated rat L6 myotubes source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Rat L6 myotubes; related rat H9c2 experiments used tagged GLUT4.
    limitations
    GLUT isoforms in the L6 result are not all resolved in the accessed abstract.
    nutrient_topic
    Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
    plain_language
    More transporters at the surface can increase glucose entry.
    primary_references
    Tyrosine phosphatase inhibitors, vanadate and pervanadate, stimulate glucose transport and GLUT translocation in muscle cells by a mechanism independent of phosphatidylinositol 3-kinase and protein kinase C. · 1998 · https://pubmed.ncbi.nlm.nih.gov/9792535/ · DOI 10.2337/diabetes.47.11.1676

    Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 54–60

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Rat L6 myotubes; related rat H9c2 experiments used tagged GLUT4. · source_derived_draft · unverified_draft

    ## vanadium-l6-transport More transporters at the surface can increase glucose entry. Vanadate and pervanadate stimulated glucose transport and GLUT movement to the plasma membrane in rat L6 myotubes. Model: Rat L6 myotubes; related rat H9c2 experiments used tagged GLUT4. Limitations: GLUT isoforms in the L6 result are not all resolved in the accessed abstract. Evidence access: Primary abstract Tyrosine phosphatase inhibitors, vanadate and pervanadate, stimulate glucose transport and GLUT translocation in muscle cells by a mechanism independent of phosphatidylinositol 3-kinase and protein kinase C. · 1998 · https://pubmed.ncbi.nlm.nih.gov/9792535/ · DOI 10.2337/diabetes.47.11.1676
    Complete structured claim and evidence

  6. 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

  7. Vanadate competitively inhibited PTP1B with a reported Ki of 0.38 ± 0.02 micromolar.

    Vanadate(V), protonation/speciation dependent → PTP1B preparation in the 1997 vanadate inhibition study source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Recombinant-enzyme kinetic study; construct species not resolved from accessed primary abstract.
    limitations
    Assay affinity is not a dietary threshold, and PTP1B is not the only phosphatase inhibited.
    nutrient_topic
    Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
    plain_language
    A phosphate-like inhibitor can occupy a phosphatase’s catalytic machinery.
    primary_references
    Mechanism of inhibition of protein-tyrosine phosphatases by vanadate and pervanadate. · 1997 · https://pubmed.ncbi.nlm.nih.gov/8995372/ · DOI 10.1074/jbc.272.2.843

    Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 14–20

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Recombinant-enzyme kinetic study; construct species not resolved from accessed primary abstract. · source_derived_draft · unverified_draft

    ## vanadium-ptp-competitive A phosphate-like inhibitor can occupy a phosphatase’s catalytic machinery. Vanadate competitively inhibited PTP1B with a reported Ki of 0.38 ± 0.02 micromolar. Model: Recombinant-enzyme kinetic study; construct species not resolved from accessed primary abstract. Limitations: Assay affinity is not a dietary threshold, and PTP1B is not the only phosphatase inhibited. Evidence access: Primary abstract Mechanism of inhibition of protein-tyrosine phosphatases by vanadate and pervanadate. · 1997 · https://pubmed.ncbi.nlm.nih.gov/8995372/ · DOI 10.1074/jbc.272.2.843
    Complete structured claim and evidence

  8. Vanadate occupied the catalytic site of calcium-free SERCA as planar VO3 with water and magnesium in a dephosphorylation-transition-like conformation.

    Vanadate(V), protonation/speciation dependent → Rabbit SERCA1a / ATP2A1 source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract and RCSB PDB 5A3Q author deposition
    experimental_model
    Rabbit SERCA structure, deposition 5A3Q; primary abstract plus author-deposited structure identity.
    limitations
    Structure used nucleotide analogues and thapsigargin; not a measured human intracellular calcium effect.
    nutrient_topic
    Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
    plain_language
    A phosphate analogue can trap a calcium pump in a catalytic state.
    primary_references
    Crystal Structure of the Vanadate-Inhibited Ca(2+)-ATPase. · 2016 · https://pubmed.ncbi.nlm.nih.gov/27050689/ · DOI 10.1016/j.str.2016.02.018

    Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 254–260

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Rabbit SERCA structure, deposition 5A3Q; primary abstract plus author-deposited structure identity. · source_derived_draft · unverified_draft

    ## vanadium-serca-transition A phosphate analogue can trap a calcium pump in a catalytic state. Vanadate occupied the catalytic site of calcium-free SERCA as planar VO3 with water and magnesium in a dephosphorylation-transition-like conformation. Model: Rabbit SERCA structure, deposition 5A3Q; primary abstract plus author-deposited structure identity. Limitations: Structure used nucleotide analogues and thapsigargin; not a measured human intracellular calcium effect. Evidence access: Primary abstract and RCSB PDB 5A3Q author deposition Crystal Structure of the Vanadate-Inhibited Ca(2+)-ATPase. · 2016 · https://pubmed.ncbi.nlm.nih.gov/27050689/ · DOI 10.1016/j.str.2016.02.018
    Complete structured claim and evidence

  9. In the vanadate-inhibited human ARSB structure, vanadate replaced sulfate at the active site and was covalently linked to the modified catalytic residue.

    Vanadate(V), protonation/speciation dependent → Human N-acetylgalactosamine-4-sulfatase / ARSB source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Human lysosomal sulfatase crystallography.
    limitations
    Structural inhibition is not evidence that oral vanadium causes mucopolysaccharidosis.
    nutrient_topic
    Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
    plain_language
    Vanadium’s targets extend beyond insulin signaling and ATPases.
    primary_references
    Structure of a human lysosomal sulfatase. · 1997 · https://pubmed.ncbi.nlm.nih.gov/9032078/ · DOI 10.1016/s0969-2126(97)00185-8

    Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 270–276

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

    ## vanadium-sulfatase-binding Vanadium’s targets extend beyond insulin signaling and ATPases. In the vanadate-inhibited human ARSB structure, vanadate replaced sulfate at the active site and was covalently linked to the modified catalytic residue. Model: Human lysosomal sulfatase crystallography. Limitations: Structural inhibition is not evidence that oral vanadium causes mucopolysaccharidosis. Evidence access: Primary abstract Structure of a human lysosomal sulfatase. · 1997 · https://pubmed.ncbi.nlm.nih.gov/9032078/ · DOI 10.1016/s0969-2126(97)00185-8
    Complete structured claim and evidence

  10. 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

What acts on it

  1. Dithiothreitol rapidly converted pervanadate to vanadate under the phosphatase assay conditions.

    Dithiothreitol / DTT → Vanadate(V), protonation/speciation dependent source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Cell-free reducing-agent experiment.
    limitations
    DTT is a laboratory reagent; glutathione cannot automatically be assigned identical kinetics.
    nutrient_topic
    Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
    plain_language
    The reducing environment can change which inhibitor is actually present.
    primary_references
    Mechanism of inhibition of protein-tyrosine phosphatases by vanadate and pervanadate. · 1997 · https://pubmed.ncbi.nlm.nih.gov/8995372/ · DOI 10.1074/jbc.272.2.843

    Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 38–44

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

    ## vanadium-dtt-speciation The reducing environment can change which inhibitor is actually present. Dithiothreitol rapidly converted pervanadate to vanadate under the phosphatase assay conditions. Model: Cell-free reducing-agent experiment. Limitations: DTT is a laboratory reagent; glutathione cannot automatically be assigned identical kinetics. Evidence access: Primary abstract Mechanism of inhibition of protein-tyrosine phosphatases by vanadate and pervanadate. · 1997 · https://pubmed.ncbi.nlm.nih.gov/8995372/ · DOI 10.1074/jbc.272.2.843
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Cytochalasin D-mediated actin disassembly blocked glucose-transport stimulation by vanadate, pervanadate and insulin.

    Actin-network disruption in rat muscle cells → Glucose transport in vanadate-treated rat L6 myotubes source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_access
    Primary abstract
    experimental_model
    Rat L6 myotube cytoskeleton perturbation.
    limitations
    Experimental machinery loss, not dietary deficiency.
    nutrient_topic
    Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
    plain_language
    The transport response still needed an intact cellular scaffold.
    primary_references
    Tyrosine phosphatase inhibitors, vanadate and pervanadate, stimulate glucose transport and GLUT translocation in muscle cells by a mechanism independent of phosphatidylinositol 3-kinase and protein kinase C. · 1998 · https://pubmed.ncbi.nlm.nih.gov/9792535/ · DOI 10.2337/diabetes.47.11.1676
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 78–84

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Rat L6 myotube cytoskeleton perturbation. · source_derived_draft · unverified_draft

    ## vanadium-actin-block The transport response still needed an intact cellular scaffold. Cytochalasin D-mediated actin disassembly blocked glucose-transport stimulation by vanadate, pervanadate and insulin. Model: Rat L6 myotube cytoskeleton perturbation. Limitations: Experimental machinery loss, not dietary deficiency. Evidence access: Primary abstract Tyrosine phosphatase inhibitors, vanadate and pervanadate, stimulate glucose transport and GLUT translocation in muscle cells by a mechanism independent of phosphatidylinositol 3-kinase and protein kinase C. · 1998 · https://pubmed.ncbi.nlm.nih.gov/9792535/ · DOI 10.2337/diabetes.47.11.1676
    Complete structured claim and evidence

  2. DIDS inhibited the intracellular thiol decrease and extracellular increase during vanadate exposure, supporting an anion-transport-dependent step.

    Human erythrocyte anion exchanger 1 / SLC4A1 → Glutathione efflux from vanadate-exposed human erythrocytes source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_access
    Primary abstract
    experimental_model
    Human erythrocytes; DIDS pharmacological intervention.
    limitations
    DIDS is an inhibitor, not itself an exchanger; pharmacology does not establish a unique SLC4A1 transport substrate or route.
    nutrient_topic
    Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
    plain_language
    Membrane transport can gate the redox response.
    primary_references
    Efflux of glutathione and glutathione complexes from human erythrocytes in response to vanadate. · 2013 · https://pubmed.ncbi.nlm.nih.gov/22824382/ · DOI 10.1016/j.bcmd.2012.07.001
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 166–172

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human erythrocytes; DIDS pharmacological intervention. · source_derived_draft · unverified_draft

    ## vanadium-anion-exchanger-block Membrane transport can gate the redox response. DIDS inhibited the intracellular thiol decrease and extracellular increase during vanadate exposure, supporting an anion-transport-dependent step. Model: Human erythrocytes; DIDS pharmacological intervention. Limitations: DIDS is an inhibitor, not itself an exchanger; pharmacology does not establish a unique SLC4A1 transport substrate or route. Evidence access: Primary abstract Efflux of glutathione and glutathione complexes from human erythrocytes in response to vanadate. · 2013 · https://pubmed.ncbi.nlm.nih.gov/22824382/ · DOI 10.1016/j.bcmd.2012.07.001
    Complete structured claim and evidence

  3. Ascorbate initiated NADH oxidation at lower concentrations but inhibited it at higher concentrations in the same chemical system.

    L-Ascorbate → NADH oxidation in the vanadium chemical assay source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Cell-free concentration-response experiments.
    limitations
    Not an established supplement dose-response in humans.
    nutrient_topic
    Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
    plain_language
    The direction of an antioxidant’s effect can depend on concentration.
    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 134–140

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

    ## vanadium-ascorbate-concentration The direction of an antioxidant’s effect can depend on concentration. Ascorbate initiated NADH oxidation at lower concentrations but inhibited it at higher concentrations in the same chemical system. Model: Cell-free concentration-response experiments. Limitations: Not an established supplement dose-response in humans. 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

  4. 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

  5. The NO donor sodium nitroprusside reduced growth and alkaline-phosphatase activity, mimicking part of the vanadate phenotype.

    Sodium nitroprusside → Growth and alkaline-phosphatase activity in rodent osteoblast-like cells source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Rat UMR106 and mouse MC3T3-E1 culture program.
    limitations
    Mimicry is not equivalent to selective blockade and rescue of the proposed vanadate mechanism.
    nutrient_topic
    Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
    plain_language
    A donor experiment supports a possible downstream mediator.
    primary_references
    Vanadate-induced nitric oxide production: role in osteoblast growth and differentiation. · 2000 · https://pubmed.ncbi.nlm.nih.gov/10988345/ · DOI 10.1016/s0014-2999(00)00356-3

    Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 334–340

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Rat UMR106 and mouse MC3T3-E1 culture program. · source_derived_draft · unverified_draft

    ## vanadium-bone-no-donor A donor experiment supports a possible downstream mediator. The NO donor sodium nitroprusside reduced growth and alkaline-phosphatase activity, mimicking part of the vanadate phenotype. Model: Rat UMR106 and mouse MC3T3-E1 culture program. Limitations: Mimicry is not equivalent to selective blockade and rescue of the proposed vanadate mechanism. Evidence access: Primary abstract Vanadate-induced nitric oxide production: role in osteoblast growth and differentiation. · 2000 · https://pubmed.ncbi.nlm.nih.gov/10988345/ · DOI 10.1016/s0014-2999(00)00356-3
    Complete structured claim and evidence

  6. Catalase blocked the slow time-dependent inactivation seen under some vanadate conditions, supporting an in-situ peroxide/pervanadate contribution.

    Catalase-treated PTP1B assay → Slow time-dependent PTP1B inactivation in vanadate assays source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    PTP1B time-course experiments with catalase.
    limitations
    Catalase rescue supports peroxide involvement; it does not identify every species in living cells.
    nutrient_topic
    Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
    plain_language
    An assay can generate a second inhibitor while it runs.
    primary_references
    Mechanism of inhibition of protein-tyrosine phosphatases by vanadate and pervanadate. · 1997 · https://pubmed.ncbi.nlm.nih.gov/8995372/ · DOI 10.1074/jbc.272.2.843

    Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 46–52

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · PTP1B time-course experiments with catalase. · source_derived_draft · unverified_draft

    ## vanadium-catalase-artifact An assay can generate a second inhibitor while it runs. Catalase blocked the slow time-dependent inactivation seen under some vanadate conditions, supporting an in-situ peroxide/pervanadate contribution. Model: PTP1B time-course experiments with catalase. Limitations: Catalase rescue supports peroxide involvement; it does not identify every species in living cells. Evidence access: Primary abstract Mechanism of inhibition of protein-tyrosine phosphatases by vanadate and pervanadate. · 1997 · https://pubmed.ncbi.nlm.nih.gov/8995372/ · DOI 10.1074/jbc.272.2.843
    Complete structured claim and evidence

  7. Decavanadate inhibited isolated Sparus aurata heart mitochondrial oxygen consumption more potently than monomeric vanadate in the reported assay.

    Decavanadate(V) → Respiration of isolated Sparus aurata heart mitochondria source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Fish cardiac mitochondria; IC50 400 nM V10 versus 23 micromolar V1 as reported.
    limitations
    Species and concentration basis matter; compare ten V atoms per decamer before inferring a per-atom potency ratio.
    nutrient_topic
    Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
    plain_language
    Oligomeric form changed potency in an isolated organelle.
    primary_references
    Mitochondria as a target for decavanadate toxicity in Sparus aurata heart. · 2007 · https://pubmed.ncbi.nlm.nih.gov/17420061/ · DOI 10.1016/j.aquatox.2007.03.005

    Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 310–316

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Fish cardiac mitochondria; IC50 400 nM V10 versus 23 micromolar V1 as reported. · source_derived_draft · unverified_draft

    ## vanadium-fish-decamer-potency Oligomeric form changed potency in an isolated organelle. Decavanadate inhibited isolated Sparus aurata heart mitochondrial oxygen consumption more potently than monomeric vanadate in the reported assay. Model: Fish cardiac mitochondria; IC50 400 nM V10 versus 23 micromolar V1 as reported. Limitations: Species and concentration basis matter; compare ten V atoms per decamer before inferring a per-atom potency ratio. Evidence access: Primary abstract Mitochondria as a target for decavanadate toxicity in Sparus aurata heart. · 2007 · https://pubmed.ncbi.nlm.nih.gov/17420061/ · DOI 10.1016/j.aquatox.2007.03.005
    Complete structured claim and evidence

  8. Glutathione and catalase reversed vanadate sensitivity in the susceptible cell line studied.

    GSH → Viability in the vanadate-sensitive cell-line experiment source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Two cell lines with different susceptibilities; identities not provided in accessed abstract.
    limitations
    The proposed intracellular peroxovanadium sequence was not established as a universal mechanism.
    nutrient_topic
    Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
    plain_language
    Available reducing or peroxide-removing capacity changed the toxicity response.
    primary_references
    Mechanisms of vanadate-induced cellular toxicity: role of cellular glutathione and NADPH. · 2002 · https://pubmed.ncbi.nlm.nih.gov/12234491/ · DOI 10.1016/s0003-9861(02)00408-3

    Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 142–148

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Two cell lines with different susceptibilities; identities not provided in accessed abstract. · source_derived_draft · unverified_draft

    ## vanadium-gsh-cell-rescue Available reducing or peroxide-removing capacity changed the toxicity response. Glutathione and catalase reversed vanadate sensitivity in the susceptible cell line studied. Model: Two cell lines with different susceptibilities; identities not provided in accessed abstract. Limitations: The proposed intracellular peroxovanadium sequence was not established as a universal mechanism. Evidence access: Primary abstract Mechanisms of vanadate-induced cellular toxicity: role of cellular glutathione and NADPH. · 2002 · https://pubmed.ncbi.nlm.nih.gov/12234491/ · DOI 10.1016/s0003-9861(02)00408-3
    Complete structured claim and evidence

  9. DMSA treatment of erythrocyte supernatants increased measured glutathione, consistent with release from metal-associated forms.

    Dimercaptosuccinic acid / DMSA → Recoverable extracellular glutathione after vanadate exposure source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Ex-vivo supernatant treatment.
    limitations
    This supports but does not structurally identify every GSH–vanadium complex; not clinical chelation guidance.
    nutrient_topic
    Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
    plain_language
    An assay can detect additional glutathione after a complex is disrupted.
    primary_references
    Efflux of glutathione and glutathione complexes from human erythrocytes in response to vanadate. · 2013 · https://pubmed.ncbi.nlm.nih.gov/22824382/ · DOI 10.1016/j.bcmd.2012.07.001

    Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 182–188

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Ex-vivo supernatant treatment. · source_derived_draft · unverified_draft

    ## vanadium-gsh-complex-recovery An assay can detect additional glutathione after a complex is disrupted. DMSA treatment of erythrocyte supernatants increased measured glutathione, consistent with release from metal-associated forms. Model: Ex-vivo supernatant treatment. Limitations: This supports but does not structurally identify every GSH–vanadium complex; not clinical chelation guidance. Evidence access: Primary abstract Efflux of glutathione and glutathione complexes from human erythrocytes in response to vanadate. · 2013 · https://pubmed.ncbi.nlm.nih.gov/22824382/ · DOI 10.1016/j.bcmd.2012.07.001
    Complete structured claim and evidence

  10. MK571 reduced glutathione efflux during erythrocyte vanadate exposure, suggesting involvement of an MRP-family exporter.

    MRP-inhibitor experiment in human erythrocytes → Glutathione efflux from vanadate-exposed human erythrocytes source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_access
    Primary abstract
    experimental_model
    Human erythrocyte inhibitor experiment.
    limitations
    The accessed study does not identify a specific ABCC isoform; no invented transporter assignment.
    nutrient_topic
    Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
    plain_language
    An exporter can contribute to loss of cellular glutathione.
    primary_references
    Efflux of glutathione and glutathione complexes from human erythrocytes in response to vanadate. · 2013 · https://pubmed.ncbi.nlm.nih.gov/22824382/ · DOI 10.1016/j.bcmd.2012.07.001
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 174–180

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

    ## vanadium-mrp-efflux-block An exporter can contribute to loss of cellular glutathione. MK571 reduced glutathione efflux during erythrocyte vanadate exposure, suggesting involvement of an MRP-family exporter. Model: Human erythrocyte inhibitor experiment. Limitations: The accessed study does not identify a specific ABCC isoform; no invented transporter assignment. Evidence access: Primary abstract Efflux of glutathione and glutathione complexes from human erythrocytes in response to vanadate. · 2013 · https://pubmed.ncbi.nlm.nih.gov/22824382/ · DOI 10.1016/j.bcmd.2012.07.001
    Complete structured claim and evidence

  11. NADPH sensitized vanadate-resistant cells and increased phosphotyrosine signals and Ras expression in the reported experiment.

    NADPH → Vanadate sensitization of a resistant cell line source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Cell-line NADPH intervention.
    limitations
    Changes support redox-dependent signaling but do not directly demonstrate each proposed vanadium intermediate.
    nutrient_topic
    Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
    plain_language
    More reducing power did not necessarily protect against this metal exposure.
    primary_references
    Mechanisms of vanadate-induced cellular toxicity: role of cellular glutathione and NADPH. · 2002 · https://pubmed.ncbi.nlm.nih.gov/12234491/ · DOI 10.1016/s0003-9861(02)00408-3

    Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 150–156

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Cell-line NADPH intervention. · source_derived_draft · unverified_draft

    ## vanadium-nadph-sensitization More reducing power did not necessarily protect against this metal exposure. NADPH sensitized vanadate-resistant cells and increased phosphotyrosine signals and Ras expression in the reported experiment. Model: Cell-line NADPH intervention. Limitations: Changes support redox-dependent signaling but do not directly demonstrate each proposed vanadium intermediate. Evidence access: Primary abstract Mechanisms of vanadate-induced cellular toxicity: role of cellular glutathione and NADPH. · 2002 · https://pubmed.ncbi.nlm.nih.gov/12234491/ · DOI 10.1016/s0003-9861(02)00408-3
    Complete structured claim and evidence

  12. 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

  13. Wortmannin inhibited measured PI3K signaling but did not block vanadate/pervanadate-stimulated glucose transport; it did block insulin-stimulated transport.

    Wortmannin-sensitive PI3K inhibition in rat muscle cells → Glucose transport in vanadate-treated rat L6 myotubes source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Rat L6 and H9c2 cell inhibitor experiments.
    limitations
    Pharmacological context-specific result, not universal PI3K independence in every vanadium study.
    nutrient_topic
    Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
    plain_language
    The same transport outcome could be reached despite blocking a usual insulin pathway.
    primary_references
    Tyrosine phosphatase inhibitors, vanadate and pervanadate, stimulate glucose transport and GLUT translocation in muscle cells by a mechanism independent of phosphatidylinositol 3-kinase and protein kinase C. · 1998 · https://pubmed.ncbi.nlm.nih.gov/9792535/ · DOI 10.2337/diabetes.47.11.1676

    Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 62–68

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Rat L6 and H9c2 cell inhibitor experiments. · source_derived_draft · unverified_draft

    ## vanadium-pi3k-not-required The same transport outcome could be reached despite blocking a usual insulin pathway. Wortmannin inhibited measured PI3K signaling but did not block vanadate/pervanadate-stimulated glucose transport; it did block insulin-stimulated transport. Model: Rat L6 and H9c2 cell inhibitor experiments. Limitations: Pharmacological context-specific result, not universal PI3K independence in every vanadium study. Evidence access: Primary abstract Tyrosine phosphatase inhibitors, vanadate and pervanadate, stimulate glucose transport and GLUT translocation in muscle cells by a mechanism independent of phosphatidylinositol 3-kinase and protein kinase C. · 1998 · https://pubmed.ncbi.nlm.nih.gov/9792535/ · DOI 10.2337/diabetes.47.11.1676
    Complete structured claim and evidence

  14. PKC inhibition or downregulation, alone or combined with wortmannin, failed to block vanadate/pervanadate-stimulated glucose transport.

    PKC inhibition or downregulation in rat muscle cells → Glucose transport in vanadate-treated rat L6 myotubes source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Rat L6 inhibitor and prolonged-PMA experiments.
    limitations
    No conclusion about every PKC isoform in other cell types.
    nutrient_topic
    Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
    plain_language
    Blocking another signaling family did not remove the effect in these cells.
    primary_references
    Tyrosine phosphatase inhibitors, vanadate and pervanadate, stimulate glucose transport and GLUT translocation in muscle cells by a mechanism independent of phosphatidylinositol 3-kinase and protein kinase C. · 1998 · https://pubmed.ncbi.nlm.nih.gov/9792535/ · DOI 10.2337/diabetes.47.11.1676

    Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 86–92

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Rat L6 inhibitor and prolonged-PMA experiments. · source_derived_draft · unverified_draft

    ## vanadium-pkc-block-null Blocking another signaling family did not remove the effect in these cells. PKC inhibition or downregulation, alone or combined with wortmannin, failed to block vanadate/pervanadate-stimulated glucose transport. Model: Rat L6 inhibitor and prolonged-PMA experiments. Limitations: No conclusion about every PKC isoform in other cell types. Evidence access: Primary abstract Tyrosine phosphatase inhibitors, vanadate and pervanadate, stimulate glucose transport and GLUT translocation in muscle cells by a mechanism independent of phosphatidylinositol 3-kinase and protein kinase C. · 1998 · https://pubmed.ncbi.nlm.nih.gov/9792535/ · DOI 10.2337/diabetes.47.11.1676
    Complete structured claim and evidence

  15. Adding EDTA immediately and completely reversed vanadate inhibition of PTP1B in the assay.

    EDTA → PTP1B preparation in the 1997 vanadate inhibition study source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Enzyme assay with a vanadate-chelating reagent.
    limitations
    Biochemical reversal, not a clinical chelation treatment.
    nutrient_topic
    Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
    plain_language
    Removing available inhibitor restored activity in this preparation.
    primary_references
    Mechanism of inhibition of protein-tyrosine phosphatases by vanadate and pervanadate. · 1997 · https://pubmed.ncbi.nlm.nih.gov/8995372/ · DOI 10.1074/jbc.272.2.843

    Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 22–28

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Enzyme assay with a vanadate-chelating reagent. · source_derived_draft · unverified_draft

    ## vanadium-ptp-edta-reversal Removing available inhibitor restored activity in this preparation. Adding EDTA immediately and completely reversed vanadate inhibition of PTP1B in the assay. Model: Enzyme assay with a vanadate-chelating reagent. Limitations: Biochemical reversal, not a clinical chelation treatment. Evidence access: Primary abstract Mechanism of inhibition of protein-tyrosine phosphatases by vanadate and pervanadate. · 1997 · https://pubmed.ncbi.nlm.nih.gov/8995372/ · DOI 10.1074/jbc.272.2.843
    Complete structured claim and evidence

  16. Replacing 3 mM MgCl2 with MnCl2 lowered vanadate-binding Kd from 96 to 12 nM in the dog-kidney Na/K-ATPase preparation without changing binding capacity.

    Mn2+ → Dog kidney sodium/potassium ATPase preparation source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Dog kidney particulate-enzyme radiovanadate binding assay.
    limitations
    Assay concentrations and enzyme state matter; not a manganese supplementation interaction in humans.
    nutrient_topic
    Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
    plain_language
    The supporting divalent ion changed inhibitor affinity.
    primary_references
    Vanadate binding to the (Na + K)-ATPase. · 1981 · https://pubmed.ncbi.nlm.nih.gov/6277881/ · DOI 10.1007/BF00743200

    Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 230–236

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Dog kidney particulate-enzyme radiovanadate binding assay. · source_derived_draft · unverified_draft

    ## vanadium-pump-mg-mn The supporting divalent ion changed inhibitor affinity. Replacing 3 mM MgCl2 with MnCl2 lowered vanadate-binding Kd from 96 to 12 nM in the dog-kidney Na/K-ATPase preparation without changing binding capacity. Model: Dog kidney particulate-enzyme radiovanadate binding assay. Limitations: Assay concentrations and enzyme state matter; not a manganese supplementation interaction in humans. Evidence access: Primary abstract Vanadate binding to the (Na + K)-ATPase. · 1981 · https://pubmed.ncbi.nlm.nih.gov/6277881/ · DOI 10.1007/BF00743200
    Complete structured claim and evidence

  17. In magnesium-containing medium, potassium increased vanadate binding and lowered its Kd to about 11 nM without changing maximum binding.

    Potassium ion → Dog kidney sodium/potassium ATPase preparation source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Dog kidney Na/K-ATPase binding experiments.
    limitations
    Effect was not appreciable under the manganese condition; not evidence that dietary potassium necessarily increases toxicity.
    nutrient_topic
    Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
    plain_language
    Potassium can shift the pump toward an inhibitor-sensitive state.
    primary_references
    Vanadate binding to the (Na + K)-ATPase. · 1981 · https://pubmed.ncbi.nlm.nih.gov/6277881/ · DOI 10.1007/BF00743200

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    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Dog kidney Na/K-ATPase binding experiments. · source_derived_draft · unverified_draft

    ## vanadium-pump-potassium Potassium can shift the pump toward an inhibitor-sensitive state. In magnesium-containing medium, potassium increased vanadate binding and lowered its Kd to about 11 nM without changing maximum binding. Model: Dog kidney Na/K-ATPase binding experiments. Limitations: Effect was not appreciable under the manganese condition; not evidence that dietary potassium necessarily increases toxicity. Evidence access: Primary abstract Vanadate binding to the (Na + K)-ATPase. · 1981 · https://pubmed.ncbi.nlm.nih.gov/6277881/ · DOI 10.1007/BF00743200
    Complete structured claim and evidence

  18. Sodium decreased vanadate binding in magnesium-containing medium, whereas sodium and potassium had little effect in the manganese condition.

    Sodium ion → Dog kidney sodium/potassium ATPase preparation source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Dog kidney enzyme binding assay.
    limitations
    No human dietary sodium recommendation follows.
    nutrient_topic
    Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
    plain_language
    The ionic environment changes how vanadate interacts with the pump.
    primary_references
    Vanadate binding to the (Na + K)-ATPase. · 1981 · https://pubmed.ncbi.nlm.nih.gov/6277881/ · DOI 10.1007/BF00743200

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    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Dog kidney enzyme binding assay. · source_derived_draft · unverified_draft

    ## vanadium-pump-sodium The ionic environment changes how vanadate interacts with the pump. Sodium decreased vanadate binding in magnesium-containing medium, whereas sodium and potassium had little effect in the manganese condition. Model: Dog kidney enzyme binding assay. Limitations: No human dietary sodium recommendation follows. Evidence access: Primary abstract Vanadate binding to the (Na + K)-ATPase. · 1981 · https://pubmed.ncbi.nlm.nih.gov/6277881/ · DOI 10.1007/BF00743200
    Complete structured claim and evidence

  19. Superoxide dismutase inhibited NADH oxidation in the vanadate/ascorbate/phosphate system, whereas catalase and ethanol did not.

    Superoxide-dismutase-treated vanadium redox assay → NADH oxidation in the vanadium chemical assay source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Cell-free scavenger comparison.
    limitations
    Does not imply catalase is irrelevant to all vanadium toxicity.
    nutrient_topic
    Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
    plain_language
    The scavenger comparison points to a superoxide-dependent step in this particular 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 126–132

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

    ## vanadium-sod-redox-rescue The scavenger comparison points to a superoxide-dependent step in this particular reaction. Superoxide dismutase inhibited NADH oxidation in the vanadate/ascorbate/phosphate system, whereas catalase and ethanol did not. Model: Cell-free scavenger comparison. Limitations: Does not imply catalase is irrelevant to all vanadium toxicity. 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

  20. Human ARSB crystallography identified calcium coordinated in the sulfate-containing catalytic site and an essential modified Cys91 residue.

    Calcium ion → Human N-acetylgalactosamine-4-sulfatase / ARSB source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Human lysosomal sulfatase structure.
    limitations
    Does not show calcium supplementation reverses vanadate inhibition.
    nutrient_topic
    Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
    plain_language
    Calcium and enzyme maturation define the machinery that the inhibitor encounters.
    primary_references
    Structure of a human lysosomal sulfatase. · 1997 · https://pubmed.ncbi.nlm.nih.gov/9032078/ · DOI 10.1016/s0969-2126(97)00185-8

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

    ## vanadium-sulfatase-calcium Calcium and enzyme maturation define the machinery that the inhibitor encounters. Human ARSB crystallography identified calcium coordinated in the sulfate-containing catalytic site and an essential modified Cys91 residue. Model: Human lysosomal sulfatase structure. Limitations: Does not show calcium supplementation reverses vanadate inhibition. Evidence access: Primary abstract Structure of a human lysosomal sulfatase. · 1997 · https://pubmed.ncbi.nlm.nih.gov/9032078/ · DOI 10.1016/s0969-2126(97)00185-8
    Complete structured claim and evidence

  21. 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

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