Component

Human cytochrome P450 2E1

Human cytochrome P450 2E1. Species, exposure and limitations are retained in each linked claim.

4 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 CYP2E1 catalyzed coumarin 3,4-epoxide formation.

    Human cytochrome P450 2E1 → Coumarin 3,4-epoxide source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/coumarin-research/11950775.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "98a03fafa68ef4d55593a3b725af646175a11b42ce02b1dfe02be84ff49d4861", "start_char": 0, "end_char": 1158, "text_sha256": "98a03fafa68ef4d55593a3b725af646175a11b42ce02b1dfe02be84ff49d4861"}
    experimental_model
    Recombinant CYP enzymes, immunoinhibition and mouse lung inhibitor experiments
    exposure
    CYP1A/2E antibody inhibition and 5-phenyl-pentyne lung experiments
    limitations
    Relative contributions depend on species and tissue; this is not a clinical drug-interaction study.
    nutrient_topic
    Coumarin research collection; topical membership is not evidence of a direct dietary effect. · Coumarin
    organism
    Human, rat and mouse; each claim specifies enzyme origin
    plain_language
    CYP2E1 also produces the reactive intermediate.
    primary_references
    [coumarin-p11950775] Identification of the cytochromes P450 that catalyze coumarin 3,4-epoxidation and 3-hydroxylation. (2002). https://pubmed.ncbi.nlm.nih.gov/11950775/ DOI: 10.1124/dmd.30.5.483
    tissue_or_cell_type
    Liver and lung microsomes

    Coumarin: metabolism, signaling and nutrient connections (2026-09-17) · lines 241–252

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant CYP enzymes, immunoinhibition and mouse lung inhibitor experiments · source_derived_draft · unverified_draft

    ### coumarin-2e1-epoxide Recombinant human CYP2E1 catalyzed coumarin 3,4-epoxide formation. Condition category: normal nutrient_topic: Coumarin research collection; topical membership is not evidence of a direct dietary effect. plain_language: CYP2E1 also produces the reactive intermediate. organism: Human, rat and mouse; each claim specifies enzyme origin tissue_or_cell_type: Liver and lung microsomes experimental_model: Recombinant CYP enzymes, immunoinhibition and mouse lung inhibitor experiments limitations: Relative contributions depend on species and tissue; this is not a clinical drug-interaction study. exposure: CYP1A/2E antibody inhibition and 5-phenyl-pentyne lung experiments evidence_span: {"source_cache": "artifacts/coumarin-research/11950775.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "98a03fafa68ef4d55593a3b725af646175a11b42ce02b1dfe02be84ff49d4861", "start_char": 0, "end_char": 1158, "text_sha256": "98a03fafa68ef4d55593a3b725af646175a11b42ce02b1dfe02be84ff49d4861"} [coumarin-p11950775] Identification of the cytochromes P450 that catalyze coumarin 3,4-epoxidation and 3-hydroxylation. (2002). https://pubmed.ncbi.nlm.nih.gov/11950775/ DOI: 10.1124/dmd.30.5.483
    Complete structured claim and evidence

  2. Fructose promoted leaky gut, endotoxaemia and liver fibrosis through ethanol-inducible cytochrome P450-2E1-mediated oxidative and nitrative stress.

    Human cytochrome P450 2E1 → Intestinal permeability to macromolecules source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/alcohol-research/30959577.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "1a80ad0b106d815118c6c4174ff22f9a86c4e41f549edb39e5d663c6efd7af3d", "start_char": 0, "end_char": 1961, "text_sha256": "1a80ad0b106d815118c6c4174ff22f9a86c4e41f549edb39e5d663c6efd7af3d"}
    experimental_model
    Fructose feeding in mice with CYP2E1 deletion and gut barrier measurement
    exposure
    Fructose feeding with and without CYP2E1
    limitations
    Recorded because it isolates the enzyme: the leak and fibrosis required CYP2E1, which ethanol induces. The driver here is fructose, not ethanol.
    nutrient_topic
    Alcohol research collection; topical membership is not evidence of a direct clinical effect, and ethanol is recorded separately from the acetaldehyde it becomes. · Ethanol
    organism
    Mouse
    plain_language
    The enzyme alcohol stabilises is itself enough to open the gut barrier.
    primary_references
    [alcohol-p30959577] Fructose Promotes Leaky Gut, Endotoxemia, and Liver Fibrosis Through Ethanol-Inducible Cytochrome P450-2E1-Mediated Oxidative and Nitrative Stress. (2021). https://pubmed.ncbi.nlm.nih.gov/30959577/ DOI: 10.1002/hep.30652
    tissue_or_cell_type
    Intestine and liver

    Alcohol: ethanol clearance, acetaldehyde, the channels it binds, organ injury and nutrient collisions (2026-09-21) · lines 501–512

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Fructose feeding in mice with CYP2E1 deletion and gut barrier measurement · source_derived_draft · unverified_draft

    ### alcohol-cyp2e1-leaky-gut Fructose promoted leaky gut, endotoxaemia and liver fibrosis through ethanol-inducible cytochrome P450-2E1-mediated oxidative and nitrative stress. Condition category: normal nutrient_topic: Alcohol research collection; topical membership is not evidence of a direct clinical effect, and ethanol is recorded separately from the acetaldehyde it becomes. plain_language: The enzyme alcohol stabilises is itself enough to open the gut barrier. organism: Mouse tissue_or_cell_type: Intestine and liver experimental_model: Fructose feeding in mice with CYP2E1 deletion and gut barrier measurement limitations: Recorded because it isolates the enzyme: the leak and fibrosis required CYP2E1, which ethanol induces. The driver here is fructose, not ethanol. exposure: Fructose feeding with and without CYP2E1 evidence_span: {"source_cache": "artifacts/alcohol-research/30959577.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "1a80ad0b106d815118c6c4174ff22f9a86c4e41f549edb39e5d663c6efd7af3d", "start_char": 0, "end_char": 1961, "text_sha256": "1a80ad0b106d815118c6c4174ff22f9a86c4e41f549edb39e5d663c6efd7af3d"} [alcohol-p30959577] Fructose Promotes Leaky Gut, Endotoxemia, and Liver Fibrosis Through Ethanol-Inducible Cytochrome P450-2E1-Mediated Oxidative and Nitrative Stress. (2021). https://pubmed.ncbi.nlm.nih.gov/30959577/ DOI: 10.1002/hep.30652
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Acetaminophen produced a biphasic response in the N-acyl ethanolamide and PPAR alpha system, with decreased PPAR alpha expression after 6 hours followed by a generalised increase of system components including PPAR alpha, NAPE-PLD and fatty acid amide hydrolase and of the N-acyl ethanolamides after 24 hours, confirmed in mice where gene expression of PPAR alpha and fatty acid amide hydrolase fell at 6 hours and rose by 24 hours, repeated administration decreased both and increased liver N-acyl ethanolamides with complete restoration after 15 days of rest, immunohistochemistry in a human case of acetaminophen hepatotoxicity confirmed the decrements, and damage-related alterations after repeated administration were aggravated in PPAR alpha-deficient mice.

    Paracetamol → The N-acyl ethanolamide and PPAR alpha anti-inflammatory system source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/paracetamol-research/29056914.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "2ca7517052bab3c774f315af85f3aa8cdf810e43dc44444724bff46e2f1bdab3", "start_char": 0, "end_char": 2081, "text_sha256": "2ca7517052bab3c774f315af85f3aa8cdf810e43dc44444724bff46e2f1bdab3"}
    experimental_model
    Human HepG2 cells and mice given acute and repeated doses, with PPAR-alpha-deficient animals and a human case
    exposure
    0.5 to 20 millimolar in cells and 750 milligrams per kilogram in mice, acute and repeated over four days
    limitations
    Follows a lipid signalling system across cells, mice, knockouts and one human case. The biphasic time course is the informative part and complicates any single-timepoint reading.
    nutrient_topic
    Paracetamol research collection; topical membership is not evidence of a direct clinical effect, and the drug is recorded separately from the metabolites NAPQI and AM404. · Paracetamol
    organism
    Human cells, mouse and human
    plain_language
    The same lipid system that makes the painkilling metabolite is knocked down by an overdose and then rebounds, and animals lacking it fare worse.
    primary_references
    [apap-p29056914] Acetaminophen-Induced Liver Injury Alters the Acyl Ethanolamine-Based Anti-Inflammatory Signaling System in Liver. (2017). https://pubmed.ncbi.nlm.nih.gov/29056914/ DOI: 10.3389/fphar.2017.00705
    tissue_or_cell_type
    Liver

    Paracetamol: the enzyme it reduces rather than blocks, the isoform that turned out not to exist, the metabolite that carries the analgesia, and the metabolite that destroys the liver (2026-09-22) · lines 441–452

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human HepG2 cells and mice given acute and repeated doses, with PPAR-alpha-deficient animals and a human case · source_derived_draft · unverified_draft

    ### apap-the-lipid-brake-fails-then-rebounds Acetaminophen produced a biphasic response in the N-acyl ethanolamide and PPAR alpha system, with decreased PPAR alpha expression after 6 hours followed by a generalised increase of system components including PPAR alpha, NAPE-PLD and fatty acid amide hydrolase and of the N-acyl ethanolamides after 24 hours, confirmed in mice where gene expression of PPAR alpha and fatty acid amide hydrolase fell at 6 hours and rose by 24 hours, repeated administration decreased both and increased liver N-acyl ethanolamides with complete restoration after 15 days of rest, immunohistochemistry in a human case of acetaminophen hepatotoxicity confirmed the decrements, and damage-related alterations after repeated administration were aggravated in PPAR alpha-deficient mice. Condition category: normal nutrient_topic: Paracetamol research collection; topical membership is not evidence of a direct clinical effect, and the drug is recorded separately from the metabolites NAPQI and AM404. plain_language: The same lipid system that makes the painkilling metabolite is knocked down by an overdose and then rebounds, and animals lacking it fare worse. organism: Human cells, mouse and human tissue_or_cell_type: Liver experimental_model: Human HepG2 cells and mice given acute and repeated doses, with PPAR-alpha-deficient animals and a human case limitations: Follows a lipid signalling system across cells, mice, knockouts and one human case. The biphasic time course is the informative part and complicates any single-timepoint reading. exposure: 0.5 to 20 millimolar in cells and 750 milligrams per kilogram in mice, acute and repeated over four days evidence_span: {"source_cache": "artifacts/paracetamol-research/29056914.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "2ca7517052bab3c774f315af85f3aa8cdf810e43dc44444724bff46e2f1bdab3", "start_char": 0, "end_char": 2081, "text_sha256": "2ca7517052bab3c774f315af85f3aa8cdf810e43dc44444724bff46e2f1bdab3"} [apap-p29056914] Acetaminophen-Induced Liver Injury Alters the Acyl Ethanolamine-Based Anti-Inflammatory Signaling System in Liver. (2017). https://pubmed.ncbi.nlm.nih.gov/29056914/ DOI: 10.3389/fphar.2017.00705
    Complete structured claim and evidence

  2. Ethanol induces CYP2E1 by protein stabilisation, slowing the ubiquitin-conjugation-dependent rapid degradation of the enzyme rather than raising its synthesis.

    Ethanol → CYP2E1 protein stability against ubiquitin-dependent degradation source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/alcohol-research/8530344.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "94e862c6432092ebcc448d94b25d00e1c2d9bd38197f2a7cd774202aeaebc689", "start_char": 0, "end_char": 909, "text_sha256": "94e862c6432092ebcc448d94b25d00e1c2d9bd38197f2a7cd774202aeaebc689"}
    experimental_model
    Ethanol treatment with ubiquitin conjugation and degradation assays
    exposure
    Ethanol exposure with measurement of CYP2E1 turnover
    limitations
    A protein-turnover mechanism rather than a transcriptional one. It explains why the second oxidation route appears quickly without new transcription.
    nutrient_topic
    Alcohol research collection; topical membership is not evidence of a direct clinical effect, and ethanol is recorded separately from the acetaldehyde it becomes. · Ethanol
    organism
    Rat and cell systems
    plain_language
    Alcohol does not make more of this enzyme; it stops the cell destroying it.
    primary_references
    [alcohol-p8530344] Ethanol induces CYP2E1 by protein stabilization. Role of ubiquitin conjugation in the rapid degradation of CYP2E1. (1995). https://pubmed.ncbi.nlm.nih.gov/8530344/ DOI: 10.1074/jbc.270.50.29632
    tissue_or_cell_type
    Hepatic microsomes

    Alcohol: ethanol clearance, acetaldehyde, the channels it binds, organ injury and nutrient collisions (2026-09-21) · lines 137–148

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Ethanol treatment with ubiquitin conjugation and degradation assays · source_derived_draft · unverified_draft

    ### alcohol-cyp2e1-stabilisation Ethanol induces CYP2E1 by protein stabilisation, slowing the ubiquitin-conjugation-dependent rapid degradation of the enzyme rather than raising its synthesis. Condition category: normal nutrient_topic: Alcohol research collection; topical membership is not evidence of a direct clinical effect, and ethanol is recorded separately from the acetaldehyde it becomes. plain_language: Alcohol does not make more of this enzyme; it stops the cell destroying it. organism: Rat and cell systems tissue_or_cell_type: Hepatic microsomes experimental_model: Ethanol treatment with ubiquitin conjugation and degradation assays limitations: A protein-turnover mechanism rather than a transcriptional one. It explains why the second oxidation route appears quickly without new transcription. exposure: Ethanol exposure with measurement of CYP2E1 turnover evidence_span: {"source_cache": "artifacts/alcohol-research/8530344.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "94e862c6432092ebcc448d94b25d00e1c2d9bd38197f2a7cd774202aeaebc689", "start_char": 0, "end_char": 909, "text_sha256": "94e862c6432092ebcc448d94b25d00e1c2d9bd38197f2a7cd774202aeaebc689"} [alcohol-p8530344] Ethanol induces CYP2E1 by protein stabilization. Role of ubiquitin conjugation in the rapid degradation of CYP2E1. (1995). https://pubmed.ncbi.nlm.nih.gov/8530344/ DOI: 10.1074/jbc.270.50.29632
    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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