Component

Human UDP-glucuronosyltransferase 1A1 / UGT1A1

Human UDP-glucuronosyltransferase 1A1 / UGT1A1. Species, exposure and limitations are retained in each linked claim.

5 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. Recombinant human UGT1A1 efficiently glucuronidated luteolin in the isoenzyme comparison.

    Human UDP-glucuronosyltransferase 1A1 / UGT1A1 → Luteolin / 3′,4′,5,7-tetrahydroxyflavone source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Human recombinant UGT comparison and microsomes.
    limitations
    Relative activity depends on tissue and conjugation position. Not a claim of equal in-vivo contribution.
    nutrient_topic
    Luteolin collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Luteolin / 3′,4′,5,7-tetrahydroxyflavone
    plain_language
    A specific enzyme can attach a glucuronide group.
    primary_references
    Regioselectivity of phase II metabolism of luteolin and quercetin by UDP-glucuronosyl transferases. · 2002 · https://pubmed.ncbi.nlm.nih.gov/12018987/ · DOI 10.1021/tx0101705

    Luteolin: metabolism, immune signaling, redox chemistry and cross-nutrient mechanisms (2026-09-19) · lines 28–34

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

    ## luteolin-ugt1a1-formation A specific enzyme can attach a glucuronide group. Recombinant human UGT1A1 efficiently glucuronidated luteolin in the isoenzyme comparison. Model: Human recombinant UGT comparison and microsomes. Limitations: Relative activity depends on tissue and conjugation position. Not a claim of equal in-vivo contribution. Evidence access: Primary abstract Regioselectivity of phase II metabolism of luteolin and quercetin by UDP-glucuronosyl transferases. · 2002 · https://pubmed.ncbi.nlm.nih.gov/12018987/ · DOI 10.1021/tx0101705
    Complete structured claim and evidence

  2. Human UGT1A1 predominantly formed the 3-O glucuronide of trans-resveratrol in microsomal/recombinant experiments; reported Km was 149 micromolar.

    Human UDP-glucuronosyltransferase 1A1 / UGT1A1 → Resveratrol 3-O-glucuronide source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Human liver/intestine microsomes and recombinant UGTs.
    limitations
    Predominant contribution is not exclusive specificity; Km is not a human plasma target.
    nutrient_topic
    Resveratrol collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Resveratrol
    plain_language
    An independently named enzyme produces an independently named metabolite.
    primary_references
    Glucuronidation of trans-resveratrol by human liver and intestinal microsomes and UGT isoforms. · 2006 · https://pubmed.ncbi.nlm.nih.gov/16597364/ · DOI 10.1211/jpp.58.4.0006

    Resveratrol: metabolites, target selectivity 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 · Human liver/intestine microsomes and recombinant UGTs. · source_derived_draft · unverified_draft

    ## resveratrol-ugt1a1 An independently named enzyme produces an independently named metabolite. Human UGT1A1 predominantly formed the 3-O glucuronide of trans-resveratrol in microsomal/recombinant experiments; reported Km was 149 micromolar. Model: Human liver/intestine microsomes and recombinant UGTs. Limitations: Predominant contribution is not exclusive specificity; Km is not a human plasma target. Evidence access: Primary abstract Glucuronidation of trans-resveratrol by human liver and intestinal microsomes and UGT isoforms. · 2006 · https://pubmed.ncbi.nlm.nih.gov/16597364/ · DOI 10.1211/jpp.58.4.0006
    Complete structured claim and evidence

What acts on it

  1. At 250 micrograms/mL, mangiferin reduced UGT1A1 activity by about 55 percent.

    Mangiferin → Human UDP-glucuronosyltransferase 1A1 / UGT1A1 source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/mangiferin-research/22815239.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e85ebd0af89f030dbeda45ed922e93a8a616c51f5ce1b64badc44d90791716c0", "start_char": 0, "end_char": 1728, "text_sha256": "e85ebd0af89f030dbeda45ed922e93a8a616c51f5ce1b64badc44d90791716c0"}
    experimental_model
    Primary human hepatocyte exposure
    exposure
    Mangiferin 50-250 micrograms/mL for 48 hours
    limitations
    High in vitro concentrations; decreased enzyme activity is not proof of human drug-level changes. Extract and isolated mangiferin are distinct.
    nutrient_topic
    Mangiferin research collection; topical membership is not evidence of a direct dietary effect. · Mangiferin
    organism
    Homo sapiens
    plain_language
    A conjugation pathway also responded in vitro.
    primary_references
    [mangiferin-p22815239] Mangifera indica L. extract and mangiferin modulate cytochrome P450 and UDP-glucuronosyltransferase enzymes in primary cultures of human hepatocytes. (2013). https://pubmed.ncbi.nlm.nih.gov/22815239/ DOI: 10.1002/ptr.4782
    tissue_or_cell_type
    Cultured hepatocytes

    Mangiferin: metabolism, signaling and nutrient connections (2026-09-17) · lines 835–846

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Primary human hepatocyte exposure · source_derived_draft · unverified_draft

    ### mangiferin-ugt1a1-activity At 250 micrograms/mL, mangiferin reduced UGT1A1 activity by about 55 percent. Condition category: normal nutrient_topic: Mangiferin research collection; topical membership is not evidence of a direct dietary effect. plain_language: A conjugation pathway also responded in vitro. organism: Homo sapiens tissue_or_cell_type: Cultured hepatocytes experimental_model: Primary human hepatocyte exposure limitations: High in vitro concentrations; decreased enzyme activity is not proof of human drug-level changes. Extract and isolated mangiferin are distinct. exposure: Mangiferin 50-250 micrograms/mL for 48 hours evidence_span: {"source_cache": "artifacts/mangiferin-research/22815239.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e85ebd0af89f030dbeda45ed922e93a8a616c51f5ce1b64badc44d90791716c0", "start_char": 0, "end_char": 1728, "text_sha256": "e85ebd0af89f030dbeda45ed922e93a8a616c51f5ce1b64badc44d90791716c0"} [mangiferin-p22815239] Mangifera indica L. extract and mangiferin modulate cytochrome P450 and UDP-glucuronosyltransferase enzymes in primary cultures of human hepatocytes. (2013). https://pubmed.ncbi.nlm.nih.gov/22815239/ DOI: 10.1002/ptr.4782
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Overall lymphocyte GST and bilirubin-based UGT1A1 indices changed minimally after resveratrol, with larger changes reported in low-baseline subgroups.

    Resveratrol → Human phase-II enzyme indices after resveratrol source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Same four-week volunteer study.
    limitations
    Bilirubin was a surrogate; this was not a direct hepatic UGT flux measurement.
    nutrient_topic
    Resveratrol collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Resveratrol
    plain_language
    A subgroup signal is not a universal detoxification effect.
    primary_references
    Resveratrol modulates drug- and carcinogen-metabolizing enzymes in a healthy volunteer study. · 2010 · https://pubmed.ncbi.nlm.nih.gov/20716633/ · DOI 10.1158/1940-6207.CAPR-09-0155

    Resveratrol: metabolites, target selectivity and cross-nutrient mechanisms (2026-09-19) · lines 446–452

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Same four-week volunteer study. · source_derived_draft · unverified_draft

    ## resveratrol-human-phase2 A subgroup signal is not a universal detoxification effect. Overall lymphocyte GST and bilirubin-based UGT1A1 indices changed minimally after resveratrol, with larger changes reported in low-baseline subgroups. Model: Same four-week volunteer study. Limitations: Bilirubin was a surrogate; this was not a direct hepatic UGT flux measurement. Evidence access: Primary abstract Resveratrol modulates drug- and carcinogen-metabolizing enzymes in a healthy volunteer study. · 2010 · https://pubmed.ncbi.nlm.nih.gov/20716633/ · DOI 10.1158/1940-6207.CAPR-09-0155
    Complete structured claim and evidence

  2. Trans-resveratrol inhibited SN-38 glucuronidation in human enzyme experiments (Ki 6.2 ± 2.1 micromolar), while bilirubin glucuronidation showed no major change.

    trans-Resveratrol → SN-38 source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Human microsomal/recombinant assays.
    limitations
    Not demonstrated irinotecan toxicity or a clinical dose-adjustment rule.
    nutrient_topic
    Resveratrol collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Resveratrol
    plain_language
    The interaction depends on the enzyme substrate.
    primary_references
    Glucuronidation of trans-resveratrol by human liver and intestinal microsomes and UGT isoforms. · 2006 · https://pubmed.ncbi.nlm.nih.gov/16597364/ · DOI 10.1211/jpp.58.4.0006

    Resveratrol: metabolites, target selectivity 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 · Human microsomal/recombinant assays. · source_derived_draft · unverified_draft

    ## resveratrol-ugt-substrate-selectivity The interaction depends on the enzyme substrate. Trans-resveratrol inhibited SN-38 glucuronidation in human enzyme experiments (Ki 6.2 ± 2.1 micromolar), while bilirubin glucuronidation showed no major change. Model: Human microsomal/recombinant assays. Limitations: Not demonstrated irinotecan toxicity or a clinical dose-adjustment rule. Evidence access: Primary abstract Glucuronidation of trans-resveratrol by human liver and intestinal microsomes and UGT isoforms. · 2006 · https://pubmed.ncbi.nlm.nih.gov/16597364/ · DOI 10.1211/jpp.58.4.0006
    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