Component

Pervanadate / peroxovanadium(V) assay species

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

8 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. Pervanadate irreversibly inhibited PTP1B by oxidation of its catalytic cysteine, supported by mass spectrometry.

    Pervanadate / peroxovanadium(V) assay species → PTP1B preparation in the 1997 vanadate inhibition study source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Purified PTP1B kinetic and mass-spectrometric experiments.
    limitations
    Do not assign this irreversible oxidation to all vanadate exposures or dietary vanadium.
    nutrient_topic
    Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
    plain_language
    The peroxide-containing species disables the enzyme through a different mechanism.
    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 30–36

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Purified PTP1B kinetic and mass-spectrometric experiments. · source_derived_draft · unverified_draft

    ## vanadium-pervanadate-cysteine The peroxide-containing species disables the enzyme through a different mechanism. Pervanadate irreversibly inhibited PTP1B by oxidation of its catalytic cysteine, supported by mass spectrometry. Model: Purified PTP1B kinetic and mass-spectrometric experiments. Limitations: Do not assign this irreversible oxidation to all vanadate exposures or dietary vanadium. 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. 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

  3. 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

  4. 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

  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. 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

  7. 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

In the sources

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