Component
Gamma-tocopherol
Gamma tocopherol congener; stereochemistry is retained in individual experimental contexts where specified.
7 recorded relationships. Experimental role, claim status and evidence remain attached to each record.
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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.
Other things that act on it
Enzymes, hormones, genes, and other components with a recorded effect. These are not nutrients, so they do not count toward the arrows above. Each finding names the chapter that recorded it.
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.
What it acts on
Gamma-tocopherol inhibited human recombinant COX-1 in a prostaglandin-product assay, with the tested non-alpha vitamin E forms showing IC50 values of 1–2.5 µM. Parent vitamin E forms did not significantly inhibit COX-2 in the same system.
Experimental context and source evidence
- cross_nutrient
- false
- experimental_model
- Recombinant human COX enzyme assay; PGF2alpha readout after chemical reduction
- exposure
- 10 min compound preincubation; arachidonic acid 5 µM for 2 min; stannous chloride converted PG intermediates to PGF2alpha for ELISA.
- limitations
- This assay differs from older ovine COX-1/oxygen-electrode work; species and substrate differences preclude labeling every potency discrepancy as a contradiction.
- nutrient_topic
- Vitamin E research collection; topical membership is not evidence of a direct dietary effect. · Vitamin E
- organism
- Homo sapiens
- plain_language
- Gamma-tocopherol reduced activity of purified human COX-1 under these assay conditions.
- primary_references
- [park2022] Different forms of vitamin E and metabolite 13'-carboxychromanols inhibit cyclooxygenase-1 and its catalyzed thromboxane in platelets, and tocotrienols and 13'-carboxychromanols are competitive inhibitors of 5-lipoxygenase. (2022). https://pubmed.ncbi.nlm.nih.gov/34710615/ DOI: 10.1016/j.jnutbio.2021.108884
- tissue_or_cell_type
- Cell-free enzyme
Vitamin E: transport, membrane protection and nutrient interactions (2026-09-17) · lines 1089–1100
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant human COX enzyme assay; PGF2alpha readout after chemical reduction · source_derived_draft · unverified_draft
### e-sig-gamma-human-cox1 Gamma-tocopherol inhibited human recombinant COX-1 in a prostaglandin-product assay, with the tested non-alpha vitamin E forms showing IC50 values of 1–2.5 µM. Parent vitamin E forms did not significantly inhibit COX-2 in the same system. Condition category: normal nutrient_topic: Vitamin E research collection; topical membership is not evidence of a direct dietary effect. plain_language: Gamma-tocopherol reduced activity of purified human COX-1 under these assay conditions. organism: Homo sapiens tissue_or_cell_type: Cell-free enzyme experimental_model: Recombinant human COX enzyme assay; PGF2alpha readout after chemical reduction limitations: This assay differs from older ovine COX-1/oxygen-electrode work; species and substrate differences preclude labeling every potency discrepancy as a contradiction. exposure: 10 min compound preincubation; arachidonic acid 5 µM for 2 min; stannous chloride converted PG intermediates to PGF2alpha for ELISA. cross_nutrient: false [park2022] Different forms of vitamin E and metabolite 13'-carboxychromanols inhibit cyclooxygenase-1 and its catalyzed thromboxane in platelets, and tocotrienols and 13'-carboxychromanols are competitive inhibitors of 5-lipoxygenase. (2022). https://pubmed.ncbi.nlm.nih.gov/34710615/ DOI: 10.1016/j.jnutbio.2021.108884
Complete structured claim and evidenceGamma-tocopherol reduced LPS-stimulated PGE2 in mouse RAW264.7 macrophages with an apparent IC50 of 7.5 µM. COX-2 protein expression was not reduced in the tested 10 and 40 µM groups.
Experimental context and source evidence
- cross_nutrient
- false
- experimental_model
- Stimulated RAW264.7 culture; PGE2 assay and immunoblot
- exposure
- 8–14 h tocopherol pretreatment in 0.5% FBS-DMEM, then 0.1 µg/mL LPS for 14 h.
- limitations
- A cellular product endpoint does not establish direct parent-vitamin binding to COX-2, exclude metabolism, or predict human supplement benefit.
- nutrient_topic
- Vitamin E research collection; topical membership is not evidence of a direct dietary effect. · Vitamin E
- organism
- Mus musculus
- plain_language
- Gamma-tocopherol lowered this inflammatory lipid signal in cultured mouse immune cells without reducing the measured amount of COX-2 protein.
- primary_references
- [jiang2000] gamma-tocopherol and its major metabolite, in contrast to alpha-tocopherol, inhibit cyclooxygenase activity in macrophages and epithelial cells. (2000). https://pubmed.ncbi.nlm.nih.gov/11005841/ DOI: 10.1073/pnas.200357097
- tissue_or_cell_type
- Macrophage cell line
Vitamin E: transport, membrane protection and nutrient interactions (2026-09-17) · lines 829–840
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Stimulated RAW264.7 culture; PGE2 assay and immunoblot · source_derived_draft · unverified_draft
### e-sig-gamma-macrophage-pge2 Gamma-tocopherol reduced LPS-stimulated PGE2 in mouse RAW264.7 macrophages with an apparent IC50 of 7.5 µM. COX-2 protein expression was not reduced in the tested 10 and 40 µM groups. Condition category: normal nutrient_topic: Vitamin E research collection; topical membership is not evidence of a direct dietary effect. plain_language: Gamma-tocopherol lowered this inflammatory lipid signal in cultured mouse immune cells without reducing the measured amount of COX-2 protein. organism: Mus musculus tissue_or_cell_type: Macrophage cell line experimental_model: Stimulated RAW264.7 culture; PGE2 assay and immunoblot limitations: A cellular product endpoint does not establish direct parent-vitamin binding to COX-2, exclude metabolism, or predict human supplement benefit. exposure: 8–14 h tocopherol pretreatment in 0.5% FBS-DMEM, then 0.1 µg/mL LPS for 14 h. cross_nutrient: false [jiang2000] gamma-tocopherol and its major metabolite, in contrast to alpha-tocopherol, inhibit cyclooxygenase activity in macrophages and epithelial cells. (2000). https://pubmed.ncbi.nlm.nih.gov/11005841/ DOI: 10.1073/pnas.200357097
Complete structured claim and evidenceSIN-1 exposure converted gamma-tocopherol to 5-nitro-gamma-tocopherol in soybean phosphatidylcholine liposomes and isolated human LDL. Product yields were approximately 50% and 75%, respectively; alpha-tocopherol did not prevent gamma nitration.
Experimental context and source evidence
- cross_nutrient
- false
- experimental_model
- HPLC analysis of tocopherols and nitration products
- exposure
- Liposomes: 20 mM phosphatidylcholine, 20 µM tocopherol and 1 mM SIN-1 at 37°C. LDL: 0.2 mM SIN-1; Figure 3 initial gamma-tocopherol 0.98 µM.
- limitations
- This identifies a stable nitration product, not every reactive intermediate or clinical anti-inflammatory efficacy. Liposome-versus-LDL antioxidant rankings differed.
- nutrient_topic
- Vitamin E research collection; topical membership is not evidence of a direct dietary effect. · Vitamin E
- organism
- Cell-free and Homo sapiens-derived LDL
- plain_language
- Gamma-tocopherol captured nitrating chemistry as a measurable nitrogen-containing product in artificial membranes and isolated blood lipoproteins.
- primary_references
- [christen1997] gamma-tocopherol traps mutagenic electrophiles such as NO(X) and complements alpha-tocopherol: physiological implications. (1997). https://pubmed.ncbi.nlm.nih.gov/9096373/ DOI: 10.1073/pnas.94.7.3217
- tissue_or_cell_type
- Soybean phosphatidylcholine liposomes; isolated plasma LDL
Vitamin E: transport, membrane protection and nutrient interactions (2026-09-17) · lines 816–827
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · HPLC analysis of tocopherols and nitration products · source_derived_draft · unverified_draft
### e-sig-gamma-nitro-product SIN-1 exposure converted gamma-tocopherol to 5-nitro-gamma-tocopherol in soybean phosphatidylcholine liposomes and isolated human LDL. Product yields were approximately 50% and 75%, respectively; alpha-tocopherol did not prevent gamma nitration. Condition category: normal nutrient_topic: Vitamin E research collection; topical membership is not evidence of a direct dietary effect. plain_language: Gamma-tocopherol captured nitrating chemistry as a measurable nitrogen-containing product in artificial membranes and isolated blood lipoproteins. organism: Cell-free and Homo sapiens-derived LDL tissue_or_cell_type: Soybean phosphatidylcholine liposomes; isolated plasma LDL experimental_model: HPLC analysis of tocopherols and nitration products limitations: This identifies a stable nitration product, not every reactive intermediate or clinical anti-inflammatory efficacy. Liposome-versus-LDL antioxidant rankings differed. exposure: Liposomes: 20 mM phosphatidylcholine, 20 µM tocopherol and 1 mM SIN-1 at 37°C. LDL: 0.2 mM SIN-1; Figure 3 initial gamma-tocopherol 0.98 µM. cross_nutrient: false [christen1997] gamma-tocopherol traps mutagenic electrophiles such as NO(X) and complements alpha-tocopherol: physiological implications. (1997). https://pubmed.ncbi.nlm.nih.gov/9096373/ DOI: 10.1073/pnas.94.7.3217
Complete structured claim and evidenceHepG2 cultures exposed to gamma-tocopherol produced side-chain oxidation/shortening intermediates culminating in gamma-CEHC, identified by GC-MS.
Experimental context and source evidence
- cross_nutrient
- false
- experimental_model
- HepG2 metabolite profiling
- exposure
- 50 µM gamma-tocopherol; primary Figure 1.
- limitations
- Pathway-level conversion; not a one-step CYP4F2 reaction or a human excretion-rate estimate.
- nutrient_topic
- Vitamin E research collection; topical membership is not evidence of a direct dietary effect. · Vitamin E
- organism
- Homo sapiens
- plain_language
- Several metabolic steps convert gamma-tocopherol into a shorter-chain product.
- primary_references
- [sontag2002] Cytochrome P450 omega-hydroxylase pathway of tocopherol catabolism. Novel mechanism of regulation of vitamin E status. (2002). https://pubmed.ncbi.nlm.nih.gov/11997390/ DOI: 10.1074/jbc.m201466200
- tissue_or_cell_type
- Hepatoma cells
Vitamin E: transport, membrane protection and nutrient interactions (2026-09-17) · lines 428–439
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · HepG2 metabolite profiling · source_derived_draft · unverified_draft
### ve-transport-gamma-multistep-cehc HepG2 cultures exposed to gamma-tocopherol produced side-chain oxidation/shortening intermediates culminating in gamma-CEHC, identified by GC-MS. Condition category: normal nutrient_topic: Vitamin E research collection; topical membership is not evidence of a direct dietary effect. plain_language: Several metabolic steps convert gamma-tocopherol into a shorter-chain product. organism: Homo sapiens tissue_or_cell_type: Hepatoma cells experimental_model: HepG2 metabolite profiling limitations: Pathway-level conversion; not a one-step CYP4F2 reaction or a human excretion-rate estimate. exposure: 50 µM gamma-tocopherol; primary Figure 1. cross_nutrient: false [sontag2002] Cytochrome P450 omega-hydroxylase pathway of tocopherol catabolism. Novel mechanism of regulation of vitamin E status. (2002). https://pubmed.ncbi.nlm.nih.gov/11997390/ DOI: 10.1074/jbc.m201466200
Complete structured claim and evidence
What acts on it
In a rat alpha-TTP membrane-transfer competition assay, gamma-tocopherol had relative affinity 8.9% of RRR-alpha-tocopherol (100%).
Experimental context and source evidence
- cross_nutrient
- false
- experimental_model
- Purified rat liver protein and membrane-transfer competition
- exposure
- 37 °C, 30 min; Table 1 competition-derived affinity.
- limitations
- Relative transfer competition, not a direct Kd or human clinical efficacy ratio.
- nutrient_topic
- Vitamin E research collection; topical membership is not evidence of a direct dietary effect. · Vitamin E
- organism
- Rattus norvegicus
- plain_language
- Rat alpha-TTP distinguished this form from RRR-alpha-tocopherol.
- primary_references
- [hosomi1997] Affinity for alpha-tocopherol transfer protein as a determinant of the biological activities of vitamin E analogs. (1997). https://pubmed.ncbi.nlm.nih.gov/9199513/ DOI: 10.1016/s0014-5793(97)00499-7
- tissue_or_cell_type
- Liver protein/liposomes
Vitamin E: transport, membrane protection and nutrient interactions (2026-09-17) · lines 155–166
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified rat liver protein and membrane-transfer competition · source_derived_draft · unverified_draft
### ve-transport-rat-ttp-affinity-gamma-tocopherol In a rat alpha-TTP membrane-transfer competition assay, gamma-tocopherol had relative affinity 8.9% of RRR-alpha-tocopherol (100%). Condition category: normal nutrient_topic: Vitamin E research collection; topical membership is not evidence of a direct dietary effect. plain_language: Rat alpha-TTP distinguished this form from RRR-alpha-tocopherol. organism: Rattus norvegicus tissue_or_cell_type: Liver protein/liposomes experimental_model: Purified rat liver protein and membrane-transfer competition limitations: Relative transfer competition, not a direct Kd or human clinical efficacy ratio. exposure: 37 °C, 30 min; Table 1 competition-derived affinity. cross_nutrient: false [hosomi1997] Affinity for alpha-tocopherol transfer protein as a determinant of the biological activities of vitamin E analogs. (1997). https://pubmed.ncbi.nlm.nih.gov/9199513/ DOI: 10.1016/s0014-5793(97)00499-7
Complete structured claim and evidence
Where it participates (unsigned role)
Recombinant human CYP4F2 catalyzed terminal side-chain hydroxylation of gamma-tocopherol to its 13′-hydroxy product.
Experimental context and source evidence
- cross_nutrient
- false
- experimental_model
- Recombinant human P450 enzyme comparison
- exposure
- gamma-Tocopherol substrate with NADPH; quantitative incubation details not assigned here.
- limitations
- Initial oxidation only; other enzymes perform subsequent side-chain shortening.
- nutrient_topic
- Vitamin E research collection; topical membership is not evidence of a direct dietary effect. · Vitamin E
- organism
- Human protein in recombinant microsomes
- plain_language
- CYP4F2 begins breakdown of this tocopherol form.
- primary_references
- [sontag2002] Cytochrome P450 omega-hydroxylase pathway of tocopherol catabolism. Novel mechanism of regulation of vitamin E status. (2002). https://pubmed.ncbi.nlm.nih.gov/11997390/ DOI: 10.1074/jbc.m201466200
- tissue_or_cell_type
- Microsomal enzyme preparation
Vitamin E: transport, membrane protection and nutrient interactions (2026-09-17) · lines 415–426
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant human P450 enzyme comparison · source_derived_draft · unverified_draft
### ve-transport-cyp4f2-gamma-hydroxylation Recombinant human CYP4F2 catalyzed terminal side-chain hydroxylation of gamma-tocopherol to its 13′-hydroxy product. Condition category: normal nutrient_topic: Vitamin E research collection; topical membership is not evidence of a direct dietary effect. plain_language: CYP4F2 begins breakdown of this tocopherol form. organism: Human protein in recombinant microsomes tissue_or_cell_type: Microsomal enzyme preparation experimental_model: Recombinant human P450 enzyme comparison limitations: Initial oxidation only; other enzymes perform subsequent side-chain shortening. exposure: gamma-Tocopherol substrate with NADPH; quantitative incubation details not assigned here. cross_nutrient: false [sontag2002] Cytochrome P450 omega-hydroxylase pathway of tocopherol catabolism. Novel mechanism of regulation of vitamin E status. (2002). https://pubmed.ncbi.nlm.nih.gov/11997390/ DOI: 10.1074/jbc.m201466200
Complete structured claim and evidenceRat liver microsomes formed initial alpha- and gamma-tocopherol side-chain oxidation products with NADPH but not without it.
Experimental context and source evidence
- cross_nutrient
- true
- experimental_model
- Cofactor omission/addition; Figure 6
- exposure
- 0.5 mM NADPH; reaction followed for 80 minutes.
- limitations
- Direct NADPH dependence; no dietary niacin or riboflavin shortage, universal supplement combination or magnesium requirement was tested.
- nutrient_topic
- Vitamin E research collection; topical membership is not evidence of a direct dietary effect. · Vitamin E
- organism
- Rattus norvegicus
- plain_language
- The initial microsomal oxidation required a reducing cofactor.
- primary_references
- [sontag2002] Cytochrome P450 omega-hydroxylase pathway of tocopherol catabolism. Novel mechanism of regulation of vitamin E status. (2002). https://pubmed.ncbi.nlm.nih.gov/11997390/ DOI: 10.1074/jbc.m201466200
- tissue_or_cell_type
- Liver microsomes
Vitamin E: transport, membrane protection and nutrient interactions (2026-09-17) · lines 441–452
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Cofactor omission/addition; Figure 6 · source_derived_draft · unverified_draft
### ve-transport-nadph-microsomal-oxidation Rat liver microsomes formed initial alpha- and gamma-tocopherol side-chain oxidation products with NADPH but not without it. Condition category: normal nutrient_topic: Vitamin E research collection; topical membership is not evidence of a direct dietary effect. plain_language: The initial microsomal oxidation required a reducing cofactor. organism: Rattus norvegicus tissue_or_cell_type: Liver microsomes experimental_model: Cofactor omission/addition; Figure 6 limitations: Direct NADPH dependence; no dietary niacin or riboflavin shortage, universal supplement combination or magnesium requirement was tested. exposure: 0.5 mM NADPH; reaction followed for 80 minutes. cross_nutrient: true [sontag2002] Cytochrome P450 omega-hydroxylase pathway of tocopherol catabolism. Novel mechanism of regulation of vitamin E status. (2002). https://pubmed.ncbi.nlm.nih.gov/11997390/ DOI: 10.1074/jbc.m201466200
Complete structured claim and evidence
The events it takes part in
A mechanism often involves more than two components. These are the full events, with every participant and its role.
Situations it appears in
Low-supply and faulty-machinery situations recorded in the chapters where this component plays a part.
In the sources
Preserved passages that mention this component, quoted exactly. Open one to read it in context.
Open hypotheses
Proposed ideas that involve this component. They are labeled as hypotheses and do not change any recorded statement.
This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.