Human cytochrome P450 2C19

evidence_span

{"source_cache": "artifacts/dim-research/20478852.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0b04ad3560e6db88e29df6793283d7571c2e7bba1d499b30a5675e49bc17434e", "start_char": 0, "end_char": 1696, "text_sha256": "0b04ad3560e6db88e29df6793283d7571c2e7bba1d499b30a5675e49bc17434e"}

experimental_model

Microsomal metabolism and drug-interaction prediction

exposure

CYP1A2, CYP2C19 and CYP3A4 assays

limitations

In-vitro estimated shares vary by pathway and model. Fluvoxamine inhibits multiple routes; its large interaction cannot be inverted into a DIM prediction.

nutrient_topic

Diindolylmethane (DIM) research collection; topical membership is not evidence of a direct dietary effect. · 3,3'-Diindolylmethane / DIM

organism

Human liver and intestinal microsomes

plain_language

Ramelteon has several metabolic routes; none here measures a DIM interaction.

primary_references

[dim-p20478852] Metabolism of ramelteon in human liver microsomes and correlation with the effect of fluvoxamine on ramelteon pharmacokinetics. (2010). https://pubmed.ncbi.nlm.nih.gov/20478852/ DOI: 10.1124/dmd.110.034009

tissue_or_cell_type

Ramelteon metabolism

Diindolylmethane (DIM): formation, receptor signaling, metabolism and drug interactions (2026-09-17) · lines 883–894

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Microsomal metabolism and drug-interaction prediction · source_derived_draft · unverified_draft

### dim-ramelteon-cyp2c19 CYP2C19 catalyzed ramelteon metabolism in the tested microsomal/recombinant system. Condition category: normal nutrient_topic: Diindolylmethane (DIM) research collection; topical membership is not evidence of a direct dietary effect. plain_language: Ramelteon has several metabolic routes; none here measures a DIM interaction. organism: Human liver and intestinal microsomes tissue_or_cell_type: Ramelteon metabolism experimental_model: Microsomal metabolism and drug-interaction prediction limitations: In-vitro estimated shares vary by pathway and model. Fluvoxamine inhibits multiple routes; its large interaction cannot be inverted into a DIM prediction. exposure: CYP1A2, CYP2C19 and CYP3A4 assays evidence_span: {"source_cache": "artifacts/dim-research/20478852.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0b04ad3560e6db88e29df6793283d7571c2e7bba1d499b30a5675e49bc17434e", "start_char": 0, "end_char": 1696, "text_sha256": "0b04ad3560e6db88e29df6793283d7571c2e7bba1d499b30a5675e49bc17434e"} [dim-p20478852] Metabolism of ramelteon in human liver microsomes and correlation with the effect of fluvoxamine on ramelteon pharmacokinetics. (2010). https://pubmed.ncbi.nlm.nih.gov/20478852/ DOI: 10.1124/dmd.110.034009

evidence_span

{"source_cache": "artifacts/melatonin-research/15616152.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "482334074e10503323360f236e00b5b837c5b082a7cda4df000a23d491bff8a2", "start_char": 0, "end_char": 1733, "text_sha256": "482334074e10503323360f236e00b5b837c5b082a7cda4df000a23d491bff8a2"}

experimental_model

Recombinant P450 screen and mouse brain comparisons

exposure

Eleven P450 isozymes; NADPH-dependent 6-hydroxylation/O-demethylation

limitations

Catalytic capacity in an enzyme assay is not whole-body contribution. CYP1B1 is an extrahepatic route; human proteins are not substituted for mouse knockout identity.

nutrient_topic

Melatonin research collection; topical membership is not evidence of a direct dietary effect. · Melatonin

organism

Human recombinant enzymes; separate mouse knockout experiment

plain_language

Removing the methyl group returns a molecule with the identity of a synthetic precursor.

primary_references

[melatonin-p15616152] Metabolism of melatonin by human cytochromes p450. (2005). https://pubmed.ncbi.nlm.nih.gov/15616152/ DOI: 10.1124/dmd.104.002410

tissue_or_cell_type

Oxidative melatonin metabolism

Melatonin: synthesis, receptors, circadian timing and nutrient interactions (2026-09-17) · lines 604–615

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant P450 screen and mouse brain comparisons · source_derived_draft · unverified_draft

### melatonin-cyp-2c19-demethylation Human CYP2C19 catalyzed melatonin O-demethylation. Condition category: normal nutrient_topic: Melatonin research collection; topical membership is not evidence of a direct dietary effect. plain_language: Removing the methyl group returns a molecule with the identity of a synthetic precursor. organism: Human recombinant enzymes; separate mouse knockout experiment tissue_or_cell_type: Oxidative melatonin metabolism experimental_model: Recombinant P450 screen and mouse brain comparisons limitations: Catalytic capacity in an enzyme assay is not whole-body contribution. CYP1B1 is an extrahepatic route; human proteins are not substituted for mouse knockout identity. exposure: Eleven P450 isozymes; NADPH-dependent 6-hydroxylation/O-demethylation evidence_span: {"source_cache": "artifacts/melatonin-research/15616152.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "482334074e10503323360f236e00b5b837c5b082a7cda4df000a23d491bff8a2", "start_char": 0, "end_char": 1733, "text_sha256": "482334074e10503323360f236e00b5b837c5b082a7cda4df000a23d491bff8a2"} [melatonin-p15616152] Metabolism of melatonin by human cytochromes p450. (2005). https://pubmed.ncbi.nlm.nih.gov/15616152/ DOI: 10.1124/dmd.104.002410

evidence_span

{"source_cache": "artifacts/melatonin-research/15616152.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "482334074e10503323360f236e00b5b837c5b082a7cda4df000a23d491bff8a2", "start_char": 0, "end_char": 1733, "text_sha256": "482334074e10503323360f236e00b5b837c5b082a7cda4df000a23d491bff8a2"}

experimental_model

Recombinant P450 screen and mouse brain comparisons

exposure

Eleven P450 isozymes; NADPH-dependent 6-hydroxylation/O-demethylation

limitations

Catalytic capacity in an enzyme assay is not whole-body contribution. CYP1B1 is an extrahepatic route; human proteins are not substituted for mouse knockout identity.

nutrient_topic

Melatonin research collection; topical membership is not evidence of a direct dietary effect. · Melatonin

organism

Human recombinant enzymes; separate mouse knockout experiment

plain_language

Melatonin has multiple metabolic routes whose importance depends on enzyme and tissue.

primary_references

[melatonin-p15616152] Metabolism of melatonin by human cytochromes p450. (2005). https://pubmed.ncbi.nlm.nih.gov/15616152/ DOI: 10.1124/dmd.104.002410

tissue_or_cell_type

Oxidative melatonin metabolism

Melatonin: synthesis, receptors, circadian timing and nutrient interactions (2026-09-17) · lines 591–602

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant P450 screen and mouse brain comparisons · source_derived_draft · unverified_draft

### melatonin-cyp-2c19-hydroxylation Recombinant human CYP2C19 catalyzed melatonin 6-hydroxylation to a minor extent in this screen. Condition category: normal nutrient_topic: Melatonin research collection; topical membership is not evidence of a direct dietary effect. plain_language: Melatonin has multiple metabolic routes whose importance depends on enzyme and tissue. organism: Human recombinant enzymes; separate mouse knockout experiment tissue_or_cell_type: Oxidative melatonin metabolism experimental_model: Recombinant P450 screen and mouse brain comparisons limitations: Catalytic capacity in an enzyme assay is not whole-body contribution. CYP1B1 is an extrahepatic route; human proteins are not substituted for mouse knockout identity. exposure: Eleven P450 isozymes; NADPH-dependent 6-hydroxylation/O-demethylation evidence_span: {"source_cache": "artifacts/melatonin-research/15616152.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "482334074e10503323360f236e00b5b837c5b082a7cda4df000a23d491bff8a2", "start_char": 0, "end_char": 1733, "text_sha256": "482334074e10503323360f236e00b5b837c5b082a7cda4df000a23d491bff8a2"} [melatonin-p15616152] Metabolism of melatonin by human cytochromes p450. (2005). https://pubmed.ncbi.nlm.nih.gov/15616152/ DOI: 10.1124/dmd.104.002410

evidence_access

Primary full text PMC3513969, CYP methods and results

experimental_model

Human liver microsomes; product concentrations normalized to 0.5–25 micromolar lovastatin, with an NADPH-generating system.

limitations

In-vitro inhibition is not a measured interaction with every drug using this enzyme; the additional responsible constituent was not identified.

nutrient_topic

Red yeast rice collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Red yeast rice

plain_language

The mixture changed an enzyme assay beyond its lovastatin content.

primary_references

[23227093] Interaction between Red Yeast Rice and CYP450 Enzymes/P-Glycoprotein and Its Implication for the Clinical Pharmacokinetics of Lovastatin. · 2012 · https://pubmed.ncbi.nlm.nih.gov/23227093/ · DOI 10.1155/2012/127043

Red yeast rice: constituents, mevalonate, CoQ and product-specific interactions (2026-09-20) · lines 116–122

AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human liver microsomes; product concentrations normalized to 0.5–25 micromolar lovastatin, with an NADPH-generating system. · source_derived_draft · unverified_draft

## red-yeast-rice-extract-cyp2c19 The mixture changed an enzyme assay beyond its lovastatin content. The three 2012 red yeast rice product extracts inhibited human microsomal CYP2C19 more potently than pure lovastatin at matched nominal lovastatin concentrations. Model: Human liver microsomes; product concentrations normalized to 0.5–25 micromolar lovastatin, with an NADPH-generating system. Limitations: In-vitro inhibition is not a measured interaction with every drug using this enzyme; the additional responsible constituent was not identified. Evidence access: Primary full text PMC3513969, CYP methods and results [23227093] Interaction between Red Yeast Rice and CYP450 Enzymes/P-Glycoprotein and Its Implication for the Clinical Pharmacokinetics of Lovastatin. · 2012 · https://pubmed.ncbi.nlm.nih.gov/23227093/ · DOI 10.1155/2012/127043

evidence_span

{"source_cache": "artifacts/curcumin-research/18480186.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "c1155ca38a767b3c3fa7bd494d0ad5590eed70a47812b7a6f3d977b43aa8a922", "start_char": 0, "end_char": 1788, "text_sha256": "c1155ca38a767b3c3fa7bd494d0ad5590eed70a47812b7a6f3d977b43aa8a922"}

experimental_model

Human microsomal/cytosolic and recombinant enzyme inhibition assays

exposure

Curcuminoid mixture, purified curcuminoids and piperine; micromolar concentrations

limitations

In-vitro inhibition does not automatically predict human drug levels. Extract, isolated curcumin and piperine are separate interventions.

nutrient_topic

Curcumin research collection; topical membership is not evidence of a direct dietary effect. · Curcumin

organism

Human enzyme systems

plain_language

The extract inhibited one drug-metabolizing enzyme in vitro.

primary_references

[curcumin-p18480186] Curcuminoids inhibit multiple human cytochromes P450, UDP-glucuronosyltransferase, and sulfotransferase enzymes, whereas piperine is a relatively selective CYP3A4 inhibitor. (2008). https://pubmed.ncbi.nlm.nih.gov/18480186/ DOI: 10.1124/dmd.108.020552

tissue_or_cell_type

Drug metabolism assays

Curcumin: metabolism, signaling and nutrient connections (2026-09-17) · lines 840–851

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human microsomal/cytosolic and recombinant enzyme inhibition assays · source_derived_draft · unverified_draft

### curcumin-extract-cyp2c19 The mixture inhibited CYP2C19 with mixed inhibition kinetics. Condition category: normal nutrient_topic: Curcumin research collection; topical membership is not evidence of a direct dietary effect. plain_language: The extract inhibited one drug-metabolizing enzyme in vitro. organism: Human enzyme systems tissue_or_cell_type: Drug metabolism assays experimental_model: Human microsomal/cytosolic and recombinant enzyme inhibition assays limitations: In-vitro inhibition does not automatically predict human drug levels. Extract, isolated curcumin and piperine are separate interventions. exposure: Curcuminoid mixture, purified curcuminoids and piperine; micromolar concentrations evidence_span: {"source_cache": "artifacts/curcumin-research/18480186.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "c1155ca38a767b3c3fa7bd494d0ad5590eed70a47812b7a6f3d977b43aa8a922", "start_char": 0, "end_char": 1788, "text_sha256": "c1155ca38a767b3c3fa7bd494d0ad5590eed70a47812b7a6f3d977b43aa8a922"} [curcumin-p18480186] Curcuminoids inhibit multiple human cytochromes P450, UDP-glucuronosyltransferase, and sulfotransferase enzymes, whereas piperine is a relatively selective CYP3A4 inhibitor. (2008). https://pubmed.ncbi.nlm.nih.gov/18480186/ DOI: 10.1124/dmd.108.020552

evidence_access

Primary full text

experimental_model

Recombinant human enzymes; 5 micromolar substrate.

limitations

Restricted substrate, concentration and preparation; earlier CYP2C9 assays gave different potency.

nutrient_topic

Myricetin collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Myricetin

plain_language

A transporter interaction does not imply strong CYP inhibition.

primary_references

Interaction of myricetin, ampelopsin (dihydromyricetin), and their sulfate metabolites with serum albumin, cytochrome P450 (CYP2C9, 2C19, and 3A4) enzymes, and organic anion-transporting polypeptides (OATP1B1 and OATP2B1). · 2024 · https://pubmed.ncbi.nlm.nih.gov/39344282/ · DOI 10.1002/prp2.70021

Myricetin: metabolism, immune signaling, redox chemistry and cross-nutrient mechanisms (2026-09-19) · lines 140–146

AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Recombinant human enzymes; 5 micromolar substrate. · source_derived_draft · unverified_draft

## myricetin-parent-cyp2c19 A transporter interaction does not imply strong CYP inhibition. At 20 micromolar, the parent did not significantly inhibit mephenytoin hydroxylation in the human CYP2C19 assay. Model: Recombinant human enzymes; 5 micromolar substrate. Limitations: Restricted substrate, concentration and preparation; earlier CYP2C9 assays gave different potency. Evidence access: Primary full text Interaction of myricetin, ampelopsin (dihydromyricetin), and their sulfate metabolites with serum albumin, cytochrome P450 (CYP2C9, 2C19, and 3A4) enzymes, and organic anion-transporting polypeptides (OATP1B1 and OATP2B1). · 2024 · https://pubmed.ncbi.nlm.nih.gov/39344282/ · DOI 10.1002/prp2.70021

evidence_access

Primary full text

experimental_model

Recombinant human enzymes; 5 micromolar substrate.

limitations

Restricted substrate, concentration and preparation; earlier CYP2C9 assays gave different potency.

nutrient_topic

Myricetin collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Myricetin

plain_language

A transporter interaction does not imply strong CYP inhibition.

primary_references

Interaction of myricetin, ampelopsin (dihydromyricetin), and their sulfate metabolites with serum albumin, cytochrome P450 (CYP2C9, 2C19, and 3A4) enzymes, and organic anion-transporting polypeptides (OATP1B1 and OATP2B1). · 2024 · https://pubmed.ncbi.nlm.nih.gov/39344282/ · DOI 10.1002/prp2.70021

Myricetin: metabolism, immune signaling, redox chemistry and cross-nutrient mechanisms (2026-09-19) · lines 188–194

AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Recombinant human enzymes; 5 micromolar substrate. · source_derived_draft · unverified_draft

## myricetin-sulfate-cyp2c19 A transporter interaction does not imply strong CYP inhibition. At 20 micromolar, the sulfate did not significantly inhibit mephenytoin hydroxylation in the human CYP2C19 assay. Model: Recombinant human enzymes; 5 micromolar substrate. Limitations: Restricted substrate, concentration and preparation; earlier CYP2C9 assays gave different potency. Evidence access: Primary full text Interaction of myricetin, ampelopsin (dihydromyricetin), and their sulfate metabolites with serum albumin, cytochrome P450 (CYP2C9, 2C19, and 3A4) enzymes, and organic anion-transporting polypeptides (OATP1B1 and OATP2B1). · 2024 · https://pubmed.ncbi.nlm.nih.gov/39344282/ · DOI 10.1002/prp2.70021

evidence_access

Primary abstract

experimental_model

In-vitro CYP panel and exposure comparison in the primary study.

limitations

An inhibition assay differs from hepatocyte induction; neither establishes a clinically important interaction at ordinary oral exposures.

nutrient_topic

Astaxanthin collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Astaxanthin

plain_language

An enzyme effect required concentrations above reported human blood exposure.

primary_references

Inhibitory effects of astaxanthin, β-cryptoxanthin, canthaxanthin, lutein, and zeaxanthin on cytochrome P450 enzyme activities. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23669408/ · DOI 10.1016/j.fct.2013.04.053

Astaxanthin: transport, membrane chemistry, signaling and nutrient interactions (2026-09-19) · lines 142–148

AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · In-vitro CYP panel and exposure comparison in the primary study. · source_derived_draft · unverified_draft

## astaxanthin-cyp-inhibition An enzyme effect required concentrations above reported human blood exposure. Astaxanthin weakly inhibited CYP2C19 in the in-vitro enzyme panel, with IC50 16.2 micromolar and no time-dependent IC50 shift. Model: In-vitro CYP panel and exposure comparison in the primary study. Limitations: An inhibition assay differs from hepatocyte induction; neither establishes a clinically important interaction at ordinary oral exposures. Evidence access: Primary abstract Inhibitory effects of astaxanthin, β-cryptoxanthin, canthaxanthin, lutein, and zeaxanthin on cytochrome P450 enzyme activities. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23669408/ · DOI 10.1016/j.fct.2013.04.053

acting_entity

s-allylcysteine

dose

SAC 0.01–1 mM; N-acetyl-SAC 1 mM

duration

Probe-specific incubation

evidence_access

Primary full-text HTML, methods/results

experimental_comparison

Test compound versus probe reaction without compound

experimental_model

Pooled human liver microsomes; probe substrate metabolism

interpretation_status

Source-derived research curation; not independent primary verification

limitations

Microsomal assay; not a clinical interaction or induction study.

nutrient_topic

S-allylcysteine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · S-allyl-L-cysteine / SAC

organism

Human liver preparation

plain_language

A negative enzyme-interaction result is retained.

primary_references

[27725449] Evaluation of the Effects of S-Allyl-L-cysteine, S-Methyl-L-cysteine, trans-S-1-Propenyl-L-cysteine, and Their N-Acetylated and S-Oxidized Metabolites on Human CYP Activities. · 2016 · https://pubmed.ncbi.nlm.nih.gov/27725449/ · DOI 10.1248/bpb.b16-00449

route

In vitro

tissue_or_cell_type

Pooled human liver microsomes; probe substrate metabolism

S-allylcysteine: sulfur signaling, redox responses and cross-nutrient mechanisms (2026-09-20) · lines 401–408

AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Pooled human liver microsomes; probe substrate metabolism · source_derived_draft · unverified_draft

## s-allylcysteine-cyp-null-cyp2c19 A negative enzyme-interaction result is retained. SAC showed little effect on tested human CYP2C19 activity over 0.01–1 mM. Model: Pooled human liver microsomes; probe substrate metabolism Limitations: Microsomal assay; not a clinical interaction or induction study. Evidence access: Primary full-text HTML, methods/results [27725449] Evaluation of the Effects of S-Allyl-L-cysteine, S-Methyl-L-cysteine, trans-S-1-Propenyl-L-cysteine, and Their N-Acetylated and S-Oxidized Metabolites on Human CYP Activities. · 2016 · https://pubmed.ncbi.nlm.nih.gov/27725449/ · DOI 10.1248/bpb.b16-00449 Structured context: {"organism": "Human liver preparation", "tissue_or_cell_type": "Pooled human liver microsomes; probe substrate metabolism", "dose": "SAC 0.01–1 mM; N-acetyl-SAC 1 mM", "duration": "Probe-specific incubation", "route": "In vitro", "experimental_comparison": "Test compound versus probe reaction without compound", "acting_entity": "s-allylcysteine", "interpretation_status": "Source-derived research curation; not independent primary verification"}

evidence_span

{"source_cache": "artifacts/thc-research/38583809.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "29593807ef463cf784578c2920ed864667e6ef46a0125ac14757a38c6b331bb1", "start_char": 0, "end_char": 1645, "text_sha256": "29593807ef463cf784578c2920ed864667e6ef46a0125ac14757a38c6b331bb1"}

experimental_model

Recombinant enzyme metabolism of THC with and without liver fatty acid binding protein

exposure

THC metabolism by CYP2C9, CYP3A and CYP2C19 with FABP1

limitations

Adds a binding protein that changes apparent metabolism, which matters because THC is extremely lipophilic. It is a recombinant system.

nutrient_topic

THC research collection; topical membership is not evidence of a direct clinical effect, and THC is recorded separately from the endocannabinoids it imitates. · Delta-9-tetrahydrocannabinol / THC

organism

Human enzymes

plain_language

Three enzymes share the job, and a fat-carrying protein changes how fast they do it.

primary_references

[thc-p38583809] CYP2C9, CYP3A and CYP2C19 metabolize Δ9-tetrahydrocannabinol to multiple metabolites but metabolism is affected by human liver fatty acid binding protein (FABP1). (2024). https://pubmed.ncbi.nlm.nih.gov/38583809/ DOI: 10.1016/j.bcp.2024.116191

tissue_or_cell_type

Recombinant system

THC: the cannabinoid receptors, the endocannabinoid system it occupies, what the drug does, and the dietary fat it is built from (2026-09-21) · lines 543–554

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant enzyme metabolism of THC with and without liver fatty acid binding protein · source_derived_draft · unverified_draft

### thc-multiple-cyps CYP2C9, CYP3A and CYP2C19 metabolised THC to multiple metabolites, but the metabolism was affected by human liver fatty acid binding protein. Condition category: normal nutrient_topic: THC research collection; topical membership is not evidence of a direct clinical effect, and THC is recorded separately from the endocannabinoids it imitates. plain_language: Three enzymes share the job, and a fat-carrying protein changes how fast they do it. organism: Human enzymes tissue_or_cell_type: Recombinant system experimental_model: Recombinant enzyme metabolism of THC with and without liver fatty acid binding protein limitations: Adds a binding protein that changes apparent metabolism, which matters because THC is extremely lipophilic. It is a recombinant system. exposure: THC metabolism by CYP2C9, CYP3A and CYP2C19 with FABP1 evidence_span: {"source_cache": "artifacts/thc-research/38583809.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "29593807ef463cf784578c2920ed864667e6ef46a0125ac14757a38c6b331bb1", "start_char": 0, "end_char": 1645, "text_sha256": "29593807ef463cf784578c2920ed864667e6ef46a0125ac14757a38c6b331bb1"} [thc-p38583809] CYP2C9, CYP3A and CYP2C19 metabolize Δ9-tetrahydrocannabinol to multiple metabolites but metabolism is affected by human liver fatty acid binding protein (FABP1). (2024). https://pubmed.ncbi.nlm.nih.gov/38583809/ DOI: 10.1016/j.bcp.2024.116191

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

evidence_span

{"source_cache": "artifacts/berberine-research/21870106.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "12e465c3c0a8ce995697a6fb9bf77c079e38b413e82c8b4f2a82e45a3dbf8ae5", "start_char": 0, "end_char": 1817, "text_sha256": "12e465c3c0a8ce995697a6fb9bf77c079e38b413e82c8b4f2a82e45a3dbf8ae5"}

experimental_model

Two-phase randomized crossover enzyme-phenotyping study

exposure

Berberine 300 mg three times daily for 14 days versus placebo

limitations

Small short-term study. Probe metabolic ratios are not percentage inhibition of every substrate. No universal dose-adjustment rule; no statistically significant effect is not equivalence.

nutrient_topic

Berberine research collection; topical membership is not evidence of a direct dietary effect. · Berberine

organism

Healthy human male volunteers; 17 completed

plain_language

The CYP2C19 probe result was also negative under these conditions.

primary_references

[berberine-p21870106] Repeated administration of berberine inhibits cytochromes P450 in humans. (2012). https://pubmed.ncbi.nlm.nih.gov/21870106/ DOI: 10.1007/s00228-011-1108-2

tissue_or_cell_type

Oral probe pharmacokinetics and urinary metabolite ratios

Berberine: metabolism, nutrient connections and drug interactions (2026-09-17) · lines 688–699

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Two-phase randomized crossover enzyme-phenotyping study · source_derived_draft · unverified_draft

### berberine-human-cyp-2c19-null No statistically significant change in omeprazole probe pharmacokinetics was found after berberine. Condition category: normal nutrient_topic: Berberine research collection; topical membership is not evidence of a direct dietary effect. plain_language: The CYP2C19 probe result was also negative under these conditions. organism: Healthy human male volunteers; 17 completed tissue_or_cell_type: Oral probe pharmacokinetics and urinary metabolite ratios experimental_model: Two-phase randomized crossover enzyme-phenotyping study limitations: Small short-term study. Probe metabolic ratios are not percentage inhibition of every substrate. No universal dose-adjustment rule; no statistically significant effect is not equivalence. exposure: Berberine 300 mg three times daily for 14 days versus placebo evidence_span: {"source_cache": "artifacts/berberine-research/21870106.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "12e465c3c0a8ce995697a6fb9bf77c079e38b413e82c8b4f2a82e45a3dbf8ae5", "start_char": 0, "end_char": 1817, "text_sha256": "12e465c3c0a8ce995697a6fb9bf77c079e38b413e82c8b4f2a82e45a3dbf8ae5"} [berberine-p21870106] Repeated administration of berberine inhibits cytochromes P450 in humans. (2012). https://pubmed.ncbi.nlm.nih.gov/21870106/ DOI: 10.1007/s00228-011-1108-2