Component

Diosmetin / 4′-O-methylluteolin

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 acts on it

  1. Human recombinant COMT and liver S9 favored 4′- over 3′-O-methylation of luteolin.

    Human catechol O-methyltransferase / COMT → Diosmetin / 4′-O-methylluteolin source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Human enzyme and liver-S9 kinetics.
    limitations
    Product formation is not identical to accumulation after further metabolism.
    nutrient_topic
    Luteolin collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Luteolin / 3′,4′,5,7-tetrahydroxyflavone
    plain_language
    The enzyme initially favored the diosmetin branch.
    primary_references
    Luteolin is a rare substrate of human catechol-O-methyltransferase favoring a para-methylation. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23386290/ · DOI 10.1002/mnfr.201200584

    Luteolin: metabolism, immune signaling, redox chemistry and cross-nutrient mechanisms (2026-09-19) · lines 92–98

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Human enzyme and liver-S9 kinetics. · source_derived_draft · unverified_draft

    ## luteolin-comt-para The enzyme initially favored the diosmetin branch. Human recombinant COMT and liver S9 favored 4′- over 3′-O-methylation of luteolin. Model: Human enzyme and liver-S9 kinetics. Limitations: Product formation is not identical to accumulation after further metabolism. Evidence access: Primary abstract Luteolin is a rare substrate of human catechol-O-methyltransferase favoring a para-methylation. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23386290/ · DOI 10.1002/mnfr.201200584
    Complete structured claim and evidence

  2. Human CYP1A2 demethylated diosmetin more readily than chrysoeriol in vitro.

    Human cytochrome P450 1A2 → Diosmetin / 4′-O-methylluteolin source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Recombinant human CYP comparison.
    limitations
    Explains a candidate source of urinary bias; not proof of drug induction.
    nutrient_topic
    Luteolin collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Luteolin / 3′,4′,5,7-tetrahydroxyflavone
    plain_language
    Downstream removal can reverse the apparent product preference.
    primary_references
    Luteolin is a rare substrate of human catechol-O-methyltransferase favoring a para-methylation. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23386290/ · DOI 10.1002/mnfr.201200584

    Luteolin: metabolism, immune signaling, redox chemistry and cross-nutrient mechanisms (2026-09-19) · lines 100–106

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

    ## luteolin-cyp1a2-demethylation Downstream removal can reverse the apparent product preference. Human CYP1A2 demethylated diosmetin more readily than chrysoeriol in vitro. Model: Recombinant human CYP comparison. Limitations: Explains a candidate source of urinary bias; not proof of drug induction. Evidence access: Primary abstract Luteolin is a rare substrate of human catechol-O-methyltransferase favoring a para-methylation. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23386290/ · DOI 10.1002/mnfr.201200584
    Complete structured claim and evidence

  3. Human CYP3A4 demethylated diosmetin more readily than chrysoeriol in vitro.

    Human cytochrome P450 3A4 → Diosmetin / 4′-O-methylluteolin source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Recombinant human CYP comparison.
    limitations
    Explains a candidate source of urinary bias; not proof of drug induction.
    nutrient_topic
    Luteolin collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Luteolin / 3′,4′,5,7-tetrahydroxyflavone
    plain_language
    Downstream removal can reverse the apparent product preference.
    primary_references
    Luteolin is a rare substrate of human catechol-O-methyltransferase favoring a para-methylation. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23386290/ · DOI 10.1002/mnfr.201200584

    Luteolin: metabolism, immune signaling, redox chemistry and cross-nutrient mechanisms (2026-09-19) · lines 108–114

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

    ## luteolin-cyp3a4-demethylation Downstream removal can reverse the apparent product preference. Human CYP3A4 demethylated diosmetin more readily than chrysoeriol in vitro. Model: Recombinant human CYP comparison. Limitations: Explains a candidate source of urinary bias; not proof of drug induction. Evidence access: Primary abstract Luteolin is a rare substrate of human catechol-O-methyltransferase favoring a para-methylation. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23386290/ · DOI 10.1002/mnfr.201200584
    Complete structured claim and evidence

  4. Human CYP3A5 demethylated diosmetin more readily than chrysoeriol in vitro.

    Human cytochrome P450 3A5 → Diosmetin / 4′-O-methylluteolin source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Recombinant human CYP comparison.
    limitations
    Explains a candidate source of urinary bias; not proof of drug induction.
    nutrient_topic
    Luteolin collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Luteolin / 3′,4′,5,7-tetrahydroxyflavone
    plain_language
    Downstream removal can reverse the apparent product preference.
    primary_references
    Luteolin is a rare substrate of human catechol-O-methyltransferase favoring a para-methylation. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23386290/ · DOI 10.1002/mnfr.201200584

    Luteolin: metabolism, immune signaling, redox chemistry and cross-nutrient mechanisms (2026-09-19) · lines 116–122

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

    ## luteolin-cyp3a5-demethylation Downstream removal can reverse the apparent product preference. Human CYP3A5 demethylated diosmetin more readily than chrysoeriol in vitro. Model: Recombinant human CYP comparison. Limitations: Explains a candidate source of urinary bias; not proof of drug induction. Evidence access: Primary abstract Luteolin is a rare substrate of human catechol-O-methyltransferase favoring a para-methylation. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23386290/ · DOI 10.1002/mnfr.201200584
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Entacapone coadministration reduced methylated luteolin products and increased circulating luteolin in rats.

    Rat catechol O-methyltransferase → Luteolin / 3′,4′,5,7-tetrahydroxyflavone source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_access
    Primary abstract
    experimental_model
    Rat intravenous luteolin with COMT inhibition.
    limitations
    Not a measured human oral drug interaction.
    nutrient_topic
    Luteolin collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Luteolin / 3′,4′,5,7-tetrahydroxyflavone
    plain_language
    Blocking one metabolic exit increased parent exposure.
    primary_references
    Role of catechol-O-methyltransferase in the disposition of luteolin in rats. · 2011 · https://pubmed.ncbi.nlm.nih.gov/21209248/ · DOI 10.1124/dmd.110.037333
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Luteolin: metabolism, immune signaling, redox chemistry and cross-nutrient mechanisms (2026-09-19) · lines 132–138

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Rat intravenous luteolin with COMT inhibition. · source_derived_draft · unverified_draft

    ## luteolin-rat-comt-blockade Blocking one metabolic exit increased parent exposure. Entacapone coadministration reduced methylated luteolin products and increased circulating luteolin in rats. Model: Rat intravenous luteolin with COMT inhibition. Limitations: Not a measured human oral drug interaction. Evidence access: Primary abstract Role of catechol-O-methyltransferase in the disposition of luteolin in rats. · 2011 · https://pubmed.ncbi.nlm.nih.gov/21209248/ · DOI 10.1124/dmd.110.037333
    Complete structured claim and evidence

  2. Human urine favored the 3′-methylated product despite the opposite initial COMT preference.

    Luteolin / 3′,4′,5,7-tetrahydroxyflavone → Chrysoeriol / 3′-O-methylluteolin source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Volunteers receiving a luteolin-containing formulation.
    limitations
    Different measurement levels, not an unresolved contradiction.
    nutrient_topic
    Luteolin collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Luteolin / 3′,4′,5,7-tetrahydroxyflavone
    plain_language
    A urine ratio reflects formation plus subsequent clearance.
    primary_references
    Luteolin is a rare substrate of human catechol-O-methyltransferase favoring a para-methylation. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23386290/ · DOI 10.1002/mnfr.201200584

    Luteolin: metabolism, immune signaling, redox chemistry and cross-nutrient mechanisms (2026-09-19) · lines 124–130

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Volunteers receiving a luteolin-containing formulation. · source_derived_draft · unverified_draft

    ## luteolin-urinary-methyl-bias A urine ratio reflects formation plus subsequent clearance. Human urine favored the 3′-methylated product despite the opposite initial COMT preference. Model: Volunteers receiving a luteolin-containing formulation. Limitations: Different measurement levels, not an unresolved contradiction. Evidence access: Primary abstract Luteolin is a rare substrate of human catechol-O-methyltransferase favoring a para-methylation. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23386290/ · DOI 10.1002/mnfr.201200584
    Complete structured claim and evidence

In the sources

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

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

    Evidence, AI assistance and curation standards