Component

Luteolin 3′-O-glucuronide

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. Luteolin 3′-O-glucuronide strongly inhibited OATP1B1 in vitro.

    Luteolin 3′-O-glucuronide → Human OATP1B1 / SLCO1B1 source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Human transporter interaction assays.
    limitations
    No clinical drug-exposure change was measured.
    nutrient_topic
    Luteolin collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Luteolin / 3′,4′,5,7-tetrahydroxyflavone
    plain_language
    A transported metabolite can also compete with uptake.
    primary_references
    Interaction of luteolin, naringenin, and their sulfate and glucuronide conjugates with human serum albumin, cytochrome P450 (CYP2C9, CYP2C19, and CYP3A4) enzymes and organic anion transporting polypeptide (OATP1B1 and OATP2B1) transporters. · 2023 · https://pubmed.ncbi.nlm.nih.gov/36481402/ · DOI 10.1016/j.biopha.2022.114078

    Luteolin: metabolism, immune signaling, redox chemistry and cross-nutrient mechanisms (2026-09-19) · lines 228–234

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Human transporter interaction assays. · source_derived_draft · unverified_draft

    ## luteolin-oatp1b1-inhibition-glucuronide A transported metabolite can also compete with uptake. Luteolin 3′-O-glucuronide strongly inhibited OATP1B1 in vitro. Model: Human transporter interaction assays. Limitations: No clinical drug-exposure change was measured. Evidence access: Primary abstract Interaction of luteolin, naringenin, and their sulfate and glucuronide conjugates with human serum albumin, cytochrome P450 (CYP2C9, CYP2C19, and CYP3A4) enzymes and organic anion transporting polypeptide (OATP1B1 and OATP2B1) transporters. · 2023 · https://pubmed.ncbi.nlm.nih.gov/36481402/ · DOI 10.1016/j.biopha.2022.114078
    Complete structured claim and evidence

What acts on it

  1. Human SLCO1B1 transported Luteolin 3′-O-glucuronide in the fluorescence-based uptake assay.

    Human OATP1B1 / SLCO1B1 → Luteolin 3′-O-glucuronide source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Living-cell uptake using 2-APB fluorescence enhancement.
    limitations
    Transport capacity is not clinical efficacy or net organ flux.
    nutrient_topic
    Luteolin collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Luteolin / 3′,4′,5,7-tetrahydroxyflavone
    plain_language
    A circulating conjugate has a route into cells.
    primary_references
    The 2-aminoethyl diphenylborinate-based fluorescent method identifies quercetin and luteolin metabolites as substrates of Organic anion transporting polypeptides, OATP1B1 and OATP2B1. · 2024 · https://pubmed.ncbi.nlm.nih.gov/38437885/ · DOI 10.1016/j.ejps.2024.106740
    transport_effect
    raises Measured in a fluorescence-based uptake assay.
    transport_pool
    the hepatocyte-model cell in the uptake assay Measured in a fluorescence-based uptake assay.

    Luteolin: metabolism, immune signaling, redox chemistry and cross-nutrient mechanisms (2026-09-19) · lines 172–178

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Living-cell uptake using 2-APB fluorescence enhancement. · source_derived_draft · unverified_draft

    ## luteolin-slco1b1-3g A circulating conjugate has a route into cells. Human SLCO1B1 transported Luteolin 3′-O-glucuronide in the fluorescence-based uptake assay. Model: Living-cell uptake using 2-APB fluorescence enhancement. Limitations: Transport capacity is not clinical efficacy or net organ flux. Evidence access: Primary abstract The 2-aminoethyl diphenylborinate-based fluorescent method identifies quercetin and luteolin metabolites as substrates of Organic anion transporting polypeptides, OATP1B1 and OATP2B1. · 2024 · https://pubmed.ncbi.nlm.nih.gov/38437885/ · DOI 10.1016/j.ejps.2024.106740
    Complete structured claim and evidence

  2. Human SLCO2B1 transported Luteolin 3′-O-glucuronide in the fluorescence-based uptake assay.

    Human organic anion transporting polypeptide 2B1 / SLCO2B1 → Luteolin 3′-O-glucuronide source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Living-cell uptake using 2-APB fluorescence enhancement.
    limitations
    Transport capacity is not clinical efficacy or net organ flux.
    nutrient_topic
    Luteolin collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Luteolin / 3′,4′,5,7-tetrahydroxyflavone
    plain_language
    A circulating conjugate has a route into cells.
    primary_references
    The 2-aminoethyl diphenylborinate-based fluorescent method identifies quercetin and luteolin metabolites as substrates of Organic anion transporting polypeptides, OATP1B1 and OATP2B1. · 2024 · https://pubmed.ncbi.nlm.nih.gov/38437885/ · DOI 10.1016/j.ejps.2024.106740
    transport_effect
    raises Measured in a fluorescence-based uptake assay.
    transport_pool
    the expressing cell Measured in a fluorescence-based uptake assay.

    Luteolin: metabolism, immune signaling, redox chemistry and cross-nutrient mechanisms (2026-09-19) · lines 196–202

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Living-cell uptake using 2-APB fluorescence enhancement. · source_derived_draft · unverified_draft

    ## luteolin-slco2b1-3g A circulating conjugate has a route into cells. Human SLCO2B1 transported Luteolin 3′-O-glucuronide in the fluorescence-based uptake assay. Model: Living-cell uptake using 2-APB fluorescence enhancement. Limitations: Transport capacity is not clinical efficacy or net organ flux. Evidence access: Primary abstract The 2-aminoethyl diphenylborinate-based fluorescent method identifies quercetin and luteolin metabolites as substrates of Organic anion transporting polypeptides, OATP1B1 and OATP2B1. · 2024 · https://pubmed.ncbi.nlm.nih.gov/38437885/ · DOI 10.1016/j.ejps.2024.106740
    Complete structured claim and evidence

  3. Human UGT1A9 formed Luteolin 3′-O-glucuronide in the luteolin-conjugation study.

    Human UDP-glucuronosyltransferase 1A9 / UGT1A9 → Luteolin 3′-O-glucuronide source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Recombinant enzymes and UGT1A9-expressing HeLa cells.
    limitations
    Engineered expression; not a human organ concentration.
    nutrient_topic
    Luteolin collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Luteolin / 3′,4′,5,7-tetrahydroxyflavone
    plain_language
    The conjugation position defines a distinct product.
    primary_references
    Breast cancer resistance protein-mediated efflux of luteolin glucuronides in HeLa cells overexpressing UDP-glucuronosyltransferase 1A9. · 2014 · https://pubmed.ncbi.nlm.nih.gov/24092055/ · DOI 10.1007/s11095-013-1207-0

    Luteolin: metabolism, immune signaling, redox chemistry and cross-nutrient mechanisms (2026-09-19) · lines 52–58

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Recombinant enzymes and UGT1A9-expressing HeLa cells. · source_derived_draft · unverified_draft

    ## luteolin-ugt1a9-3g The conjugation position defines a distinct product. Human UGT1A9 formed Luteolin 3′-O-glucuronide in the luteolin-conjugation study. Model: Recombinant enzymes and UGT1A9-expressing HeLa cells. Limitations: Engineered expression; not a human organ concentration. Evidence access: Primary abstract Breast cancer resistance protein-mediated efflux of luteolin glucuronides in HeLa cells overexpressing UDP-glucuronosyltransferase 1A9. · 2014 · https://pubmed.ncbi.nlm.nih.gov/24092055/ · DOI 10.1007/s11095-013-1207-0
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Ko143 inhibition of ABCG2 reduced luteolin-monoglucuronide efflux and increased intracellular retention.

    Human ABCG2 / breast cancer resistance protein → Luteolin monoglucuronides, position unresolved in study source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_access
    Primary abstract
    experimental_model
    UGT1A9-expressing human HeLa cells.
    limitations
    Pharmacological inhibition; diglucuronide compensation was proposed, not proven in patients.
    nutrient_topic
    Luteolin collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Luteolin / 3′,4′,5,7-tetrahydroxyflavone
    plain_language
    Blocking export changes where metabolites accumulate.
    primary_references
    Breast cancer resistance protein-mediated efflux of luteolin glucuronides in HeLa cells overexpressing UDP-glucuronosyltransferase 1A9. · 2014 · https://pubmed.ncbi.nlm.nih.gov/24092055/ · DOI 10.1007/s11095-013-1207-0
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Luteolin: metabolism, immune signaling, redox chemistry and cross-nutrient mechanisms (2026-09-19) · lines 84–90

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · UGT1A9-expressing human HeLa cells. · source_derived_draft · unverified_draft

    ## luteolin-abcg2-blockade Blocking export changes where metabolites accumulate. Ko143 inhibition of ABCG2 reduced luteolin-monoglucuronide efflux and increased intracellular retention. Model: UGT1A9-expressing human HeLa cells. Limitations: Pharmacological inhibition; diglucuronide compensation was proposed, not proven in patients. Evidence access: Primary abstract Breast cancer resistance protein-mediated efflux of luteolin glucuronides in HeLa cells overexpressing UDP-glucuronosyltransferase 1A9. · 2014 · https://pubmed.ncbi.nlm.nih.gov/24092055/ · DOI 10.1007/s11095-013-1207-0
    Complete structured claim and evidence

  2. Tested luteolin conjugates had no or weak inhibition of CYP2C9, CYP2C19 and CYP3A4.

    Luteolin 3′-O-sulfate → Human CYP2C9/CYP2C19/CYP3A4 assay panel source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Human CYP assays.
    limitations
    Restricted enzyme panel; not a blanket absence of interactions.
    nutrient_topic
    Luteolin collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Luteolin / 3′,4′,5,7-tetrahydroxyflavone
    plain_language
    The parent’s effects cannot simply be assigned to every metabolite.
    primary_references
    Interaction of luteolin, naringenin, and their sulfate and glucuronide conjugates with human serum albumin, cytochrome P450 (CYP2C9, CYP2C19, and CYP3A4) enzymes and organic anion transporting polypeptide (OATP1B1 and OATP2B1) transporters. · 2023 · https://pubmed.ncbi.nlm.nih.gov/36481402/ · DOI 10.1016/j.biopha.2022.114078

    Luteolin: metabolism, immune signaling, redox chemistry and cross-nutrient mechanisms (2026-09-19) · lines 244–250

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Human CYP assays. · source_derived_draft · unverified_draft

    ## luteolin-conjugate-cyp The parent’s effects cannot simply be assigned to every metabolite. Tested luteolin conjugates had no or weak inhibition of CYP2C9, CYP2C19 and CYP3A4. Model: Human CYP assays. Limitations: Restricted enzyme panel; not a blanket absence of interactions. Evidence access: Primary abstract Interaction of luteolin, naringenin, and their sulfate and glucuronide conjugates with human serum albumin, cytochrome P450 (CYP2C9, CYP2C19, and CYP3A4) enzymes and organic anion transporting polypeptide (OATP1B1 and OATP2B1) transporters. · 2023 · https://pubmed.ncbi.nlm.nih.gov/36481402/ · DOI 10.1016/j.biopha.2022.114078
    Complete structured claim and evidence

In the sources

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

    This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.

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