Glutathione reductase / GSR

cross_nutrient

B2-FAD supports GSH recycling; selenium-dependent GPX use of GSH is a separate reaction.

evidence_location

Results: NADPH binding; Fig 1 consensus cycle; GSH/GSSG complexes

experimental_model

Purified human glutathione reductase crystals with natural substrates, 0.95-1.1-A resolution, chemically reduced controls.

exposure

Purified-enzyme assay

limitations

GSR is not glutathione peroxidase; this record does not show that B2 improves selenium repletion.

nutrient_topic

Riboflavin research collection; topical membership is not evidence of a direct dietary effect. · Riboflavin (vitamin B2)

organism

Homo sapiens

plain_language

This enzyme recycles glutathione after oxidation.

primary_references

[berkholz2008] Catalytic cycle of human glutathione reductase near 1 A resolution. (2008). https://pubmed.ncbi.nlm.nih.gov/18638483/ DOI: 10.1016/j.jmb.2008.06.083

tissue_or_cell_type

Purified human GSR

Riboflavin: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 1332–1344

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified human glutathione reductase crystals with natural substrates, 0.95-1.1-A resolution, chemically reduced controls. · source_derived_draft · unverified_draft

### b2-gsr-gssg-to-gsh GSR reduces one glutathione-disulfide molecule to two reduced glutathione molecules using the NADPH/FAD catalytic relay. Condition category: normal nutrient_topic: Riboflavin research collection; topical membership is not evidence of a direct dietary effect. plain_language: This enzyme recycles glutathione after oxidation. organism: Homo sapiens tissue_or_cell_type: Purified human GSR experimental_model: Purified human glutathione reductase crystals with natural substrates, 0.95-1.1-A resolution, chemically reduced controls. limitations: GSR is not glutathione peroxidase; this record does not show that B2 improves selenium repletion. exposure: Purified-enzyme assay cross_nutrient: B2-FAD supports GSH recycling; selenium-dependent GPX use of GSH is a separate reaction. evidence_location: Results: NADPH binding; Fig 1 consensus cycle; GSH/GSSG complexes [berkholz2008] Catalytic cycle of human glutathione reductase near 1 A resolution. (2008). https://pubmed.ncbi.nlm.nih.gov/18638483/ DOI: 10.1016/j.jmb.2008.06.083

evidence_span

{"source_cache": "artifacts/ala-research/7632170.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "2ebbc851e5279e646bc7c892645c931a3fd2993830c3f4405379839cbbd6e707", "start_char": 0, "end_char": 1863, "text_sha256": "2ebbc851e5279e646bc7c892645c931a3fd2993830c3f4405379839cbbd6e707"}

experimental_model

Human erythrocytes, one G6PD-deficient donor and purified-enzyme assays

exposure

Lipoic acid with glucose/2-deoxyglucose and G6PD inhibition

limitations

The deficient-donor finding is small and mechanistic; it is not a clinical safety or efficacy trial in G6PD deficiency.

nutrient_topic

Alpha-lipoic acid research collection; topical membership is not evidence of a direct dietary effect. · Lipoic acid

organism

Human

plain_language

An enzyme associated with glutathione recycling can also reduce free lipoic acid.

primary_references

[ala-p7632170] Reduction and transport of lipoic acid by human erythrocytes. (1995). https://pubmed.ncbi.nlm.nih.gov/7632170/ DOI: 10.1016/0006-2952(95)00084-d

tissue_or_cell_type

Erythrocytes and glutathione reductase

Alpha-lipoic acid: cofactor assembly, redox signaling and nutrient interactions (2026-09-17) · lines 741–752

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human erythrocytes, one G6PD-deficient donor and purified-enzyme assays · source_derived_draft · unverified_draft

### ala-gsr-free-lipoate Purified human glutathione reductase reduced free lipoic acid to DHLA in vitro. Condition category: normal nutrient_topic: Alpha-lipoic acid research collection; topical membership is not evidence of a direct dietary effect. plain_language: An enzyme associated with glutathione recycling can also reduce free lipoic acid. organism: Human tissue_or_cell_type: Erythrocytes and glutathione reductase experimental_model: Human erythrocytes, one G6PD-deficient donor and purified-enzyme assays limitations: The deficient-donor finding is small and mechanistic; it is not a clinical safety or efficacy trial in G6PD deficiency. exposure: Lipoic acid with glucose/2-deoxyglucose and G6PD inhibition evidence_span: {"source_cache": "artifacts/ala-research/7632170.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "2ebbc851e5279e646bc7c892645c931a3fd2993830c3f4405379839cbbd6e707", "start_char": 0, "end_char": 1863, "text_sha256": "2ebbc851e5279e646bc7c892645c931a3fd2993830c3f4405379839cbbd6e707"} [ala-p7632170] Reduction and transport of lipoic acid by human erythrocytes. (1995). https://pubmed.ncbi.nlm.nih.gov/7632170/ DOI: 10.1016/0006-2952(95)00084-d

evidence_span

{"source_cache": "artifacts/sulforaphane-research/30595796.fulltext.txt", "locator": "Primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "13f25a5ca61ca9bdf80d4b24878682c90b414a5718a73b6a5b86ff20a9673279", "start_char": 14986, "end_char": 15205, "text_sha256": "c8a5b844826129e5cff61e4e19c0eb34f04a29a8feb8ced52a567eae1585d935"}

experimental_model

Replicative culture and metabolic/gene-expression measurements

exposure

Sulforaphane treatment during serial culture

limitations

Cell-culture senescence is not human longevity; expression is not necessarily flux.

nutrient_topic

Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study

organism

Human MRC-5 and BJ fibroblasts

plain_language

The response includes this separately identified defense-system protein.

primary_references

[sulforaphane-p30595796] Sulforaphane Delays Fibroblast Senescence by Curbing Cellular Glucose Uptake, Increased Glycolysis, and Oxidative Damage. (2018). https://pubmed.ncbi.nlm.nih.gov/30595796/ DOI: 10.1155/2018/5642148

tissue_or_cell_type

Glucose handling, antioxidant response and senescence

Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 944–955

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Replicative culture and metabolic/gene-expression measurements · source_derived_draft · unverified_draft

### sulforaphane-gsr-induction Sulforaphane increased GSR gene expression in early-passage nonsenescent MRC-5 fibroblasts. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: The response includes this separately identified defense-system protein. organism: Human MRC-5 and BJ fibroblasts tissue_or_cell_type: Glucose handling, antioxidant response and senescence experimental_model: Replicative culture and metabolic/gene-expression measurements limitations: Cell-culture senescence is not human longevity; expression is not necessarily flux. exposure: Sulforaphane treatment during serial culture evidence_span: {"source_cache": "artifacts/sulforaphane-research/30595796.fulltext.txt", "locator": "Primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "13f25a5ca61ca9bdf80d4b24878682c90b414a5718a73b6a5b86ff20a9673279", "start_char": 14986, "end_char": 15205, "text_sha256": "c8a5b844826129e5cff61e4e19c0eb34f04a29a8feb8ced52a567eae1585d935"} [sulforaphane-p30595796] Sulforaphane Delays Fibroblast Senescence by Curbing Cellular Glucose Uptake, Increased Glycolysis, and Oxidative Damage. (2018). https://pubmed.ncbi.nlm.nih.gov/30595796/ DOI: 10.1155/2018/5642148

cross_nutrient

B2-derived cofactor bridges NADPH and the glutathione system.

evidence_location

Results: NADPH binding; Fig 1 consensus cycle; GSH/GSSG complexes

experimental_model

Purified human glutathione reductase crystals with natural substrates, 0.95-1.1-A resolution, chemically reduced controls.

exposure

Purified-enzyme assay

limitations

Mechanism integrates natural-substrate structures with prior kinetic work; transient intermediates were not all directly trapped here.

nutrient_topic

Riboflavin research collection; topical membership is not evidence of a direct dietary effect. · Riboflavin (vitamin B2)

organism

Homo sapiens

plain_language

FAD relays electrons through enzyme cysteines.

primary_references

[berkholz2008] Catalytic cycle of human glutathione reductase near 1 A resolution. (2008). https://pubmed.ncbi.nlm.nih.gov/18638483/ DOI: 10.1016/j.jmb.2008.06.083

tissue_or_cell_type

Purified human GSR

Riboflavin: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 1318–1330

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified human glutathione reductase crystals with natural substrates, 0.95-1.1-A resolution, chemically reduced controls. · source_derived_draft · unverified_draft

### b2-gsr-flavin-disulfide-relay The GSR catalytic cycle transfers reducing equivalents from flavin to the Cys58-Cys63 active-site disulfide before glutathione-disulfide reduction. Condition category: normal nutrient_topic: Riboflavin research collection; topical membership is not evidence of a direct dietary effect. plain_language: FAD relays electrons through enzyme cysteines. organism: Homo sapiens tissue_or_cell_type: Purified human GSR experimental_model: Purified human glutathione reductase crystals with natural substrates, 0.95-1.1-A resolution, chemically reduced controls. limitations: Mechanism integrates natural-substrate structures with prior kinetic work; transient intermediates were not all directly trapped here. exposure: Purified-enzyme assay cross_nutrient: B2-derived cofactor bridges NADPH and the glutathione system. evidence_location: Results: NADPH binding; Fig 1 consensus cycle; GSH/GSSG complexes [berkholz2008] Catalytic cycle of human glutathione reductase near 1 A resolution. (2008). https://pubmed.ncbi.nlm.nih.gov/18638483/ DOI: 10.1016/j.jmb.2008.06.083

evidence_access

Primary abstract

experimental_model

Cultured human endothelial cells.

limitations

GSR expression does not establish increased flux or correction of riboflavin deficiency.

nutrient_topic

Ergothioneine collection; molecular form, preparation, species, exposure and manipulation remain explicit. · L-Ergothioneine

plain_language

This connects the response to glutathione recycling.

primary_references

Uptake and protective effects of ergothioneine in human endothelial cells. · 2014 · https://pubmed.ncbi.nlm.nih.gov/25022513/ · DOI 10.1124/jpet.114.214049

Ergothioneine: transport, redox chemistry and cross-nutrient mechanisms (2026-09-19) · lines 296–302

AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Cultured human endothelial cells. · source_derived_draft · unverified_draft

## ergothioneine-endothelial-gsr This connects the response to glutathione recycling. Ergothioneine increased glutathione reductase expression in human brain microvascular endothelial cells. Model: Cultured human endothelial cells. Limitations: GSR expression does not establish increased flux or correction of riboflavin deficiency. Evidence access: Primary abstract Uptake and protective effects of ergothioneine in human endothelial cells. · 2014 · https://pubmed.ncbi.nlm.nih.gov/25022513/ · DOI 10.1124/jpet.114.214049

availability_state

nutrient_deficiency Imported condition classification; unverified.

experimental_model

Erythrocytes from marginally riboflavin-deficient people and controls separated into nine density fractions.

exposure

Red-cell age-fraction enzyme/cofactor assays, glutathione, hemoglobin species and peroxide susceptibility; observational comparison.

limitations

Does not identify a single responsible reductase or prove clinically significant anemia/hemolysis in each person.

nutrient_topic

Riboflavin research collection; topical membership is not evidence of a direct dietary effect. · Riboflavin (vitamin B2)

organism

Homo sapiens

plain_language

The study found a specific hemoglobin oxidation change, not failure of every antioxidant measure.

primary_references

[b2-powers1981] Riboflavin deficiency in man: effects on haemoglobin and reduced glutathione in erythrocytes of different ages (1981). https://pubmed.ncbi.nlm.nih.gov/7284295/ DOI: 10.1079/bjn19810031

tissue_or_cell_type

Human clinical setting

trigger_kind

nutrient_deficiency Imported condition classification; unverified.

Riboflavin: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 1705–1715

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Erythrocytes from marginally riboflavin-deficient people and controls separated into nine density fractions. · source_derived_draft · unverified_draft

### b2-deficiency-methemoglobin Methemoglobin was higher in erythrocytes from the marginally B2-deficient group; the other tested endpoints did not all differ from controls. Condition category: nutrient_deficiency nutrient_topic: Riboflavin research collection; topical membership is not evidence of a direct dietary effect. plain_language: The study found a specific hemoglobin oxidation change, not failure of every antioxidant measure. organism: Homo sapiens tissue_or_cell_type: Human clinical setting experimental_model: Erythrocytes from marginally riboflavin-deficient people and controls separated into nine density fractions. limitations: Does not identify a single responsible reductase or prove clinically significant anemia/hemolysis in each person. exposure: Red-cell age-fraction enzyme/cofactor assays, glutathione, hemoglobin species and peroxide susceptibility; observational comparison. [b2-powers1981] Riboflavin deficiency in man: effects on haemoglobin and reduced glutathione in erythrocytes of different ages (1981). https://pubmed.ncbi.nlm.nih.gov/7284295/ DOI: 10.1079/bjn19810031

availability_state

nutrient_deficiency Imported condition classification; unverified.

cross_nutrient

B2 supports a component of glutathione recycling; this is not proof of universal glutathione exhaustion.

experimental_model

Erythrocytes from marginally riboflavin-deficient people and controls separated into nine density fractions.

exposure

Red-cell age-fraction enzyme/cofactor assays, glutathione, hemoglobin species and peroxide susceptibility; observational comparison.

limitations

Observational age-fraction study; reduced glutathione itself was not among the significant between-group differences.

nutrient_topic

Riboflavin research collection; topical membership is not evidence of a direct dietary effect. · Riboflavin (vitamin B2)

organism

Homo sapiens

plain_language

A B2-dependent recycling enzyme was less active in red cells from the deficient group.

primary_references

[b2-powers1981] Riboflavin deficiency in man: effects on haemoglobin and reduced glutathione in erythrocytes of different ages (1981). https://pubmed.ncbi.nlm.nih.gov/7284295/ DOI: 10.1079/bjn19810031

tissue_or_cell_type

Human clinical setting

trigger_kind

nutrient_deficiency Imported condition classification; unverified.

Riboflavin: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 1692–1703

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Erythrocytes from marginally riboflavin-deficient people and controls separated into nine density fractions. · source_derived_draft · unverified_draft

### b2-deficiency-redcell-gsr Marginally B2-deficient subjects had lower erythrocyte glutathione reductase activity than controls across the study comparison. Condition category: nutrient_deficiency nutrient_topic: Riboflavin research collection; topical membership is not evidence of a direct dietary effect. plain_language: A B2-dependent recycling enzyme was less active in red cells from the deficient group. organism: Homo sapiens tissue_or_cell_type: Human clinical setting experimental_model: Erythrocytes from marginally riboflavin-deficient people and controls separated into nine density fractions. limitations: Observational age-fraction study; reduced glutathione itself was not among the significant between-group differences. exposure: Red-cell age-fraction enzyme/cofactor assays, glutathione, hemoglobin species and peroxide susceptibility; observational comparison. cross_nutrient: B2 supports a component of glutathione recycling; this is not proof of universal glutathione exhaustion. [b2-powers1981] Riboflavin deficiency in man: effects on haemoglobin and reduced glutathione in erythrocytes of different ages (1981). https://pubmed.ncbi.nlm.nih.gov/7284295/ DOI: 10.1079/bjn19810031

availability_state

biomarker_context Imported condition classification; unverified.

cross_nutrient

G6PD genotype and distinct flavin pools alter interpretation of B2/B6-linked assays.

experimental_model

Human erythrocytes from G6PD deficiency, heterozygous beta-thalassemia and controls.

exposure

In-vitro FAD stimulation of glutathione reductase and PNP oxidase activity, with oral-riboflavin response observations.

limitations

Human red-cell observation; the proposed faster FMN-to-FAD flux was an interpretation, not a directly measured universal mechanism.

nutrient_topic

Riboflavin research collection; topical membership is not evidence of a direct dietary effect. · Riboflavin (vitamin B2)

organism

Homo sapiens

plain_language

A red-cell FAD saturation test can look adequate while another B2-dependent enzyme system is poorly supplied.

primary_references

[b2-anderson1987] Glutathione reductase activity and its relationship to pyridoxine phosphate activity in G6PD deficiency (1987). https://pubmed.ncbi.nlm.nih.gov/3582603/ DOI: 10.1111/j.1600-0609.1987.tb01417.x

tissue_or_cell_type

Human clinical setting

trigger_kind

biomarker_context Imported condition classification; unverified.

Riboflavin: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 1666–1677

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human erythrocytes from G6PD deficiency, heterozygous beta-thalassemia and controls. · source_derived_draft · unverified_draft

### b2-g6pd-fad-assay-limit In G6PD-deficient erythrocytes, glutathione reductase was usually already FAD-saturated despite evidence of low FMN-dependent oxidase activity. Condition category: biomarker_context nutrient_topic: Riboflavin research collection; topical membership is not evidence of a direct dietary effect. plain_language: A red-cell FAD saturation test can look adequate while another B2-dependent enzyme system is poorly supplied. organism: Homo sapiens tissue_or_cell_type: Human clinical setting experimental_model: Human erythrocytes from G6PD deficiency, heterozygous beta-thalassemia and controls. limitations: Human red-cell observation; the proposed faster FMN-to-FAD flux was an interpretation, not a directly measured universal mechanism. exposure: In-vitro FAD stimulation of glutathione reductase and PNP oxidase activity, with oral-riboflavin response observations. cross_nutrient: G6PD genotype and distinct flavin pools alter interpretation of B2/B6-linked assays. [b2-anderson1987] Glutathione reductase activity and its relationship to pyridoxine phosphate activity in G6PD deficiency (1987). https://pubmed.ncbi.nlm.nih.gov/3582603/ DOI: 10.1111/j.1600-0609.1987.tb01417.x

cross_nutrient

Nicotinamide-containing NADPH and B2-derived FAD perform distinct functions.

evidence_location

Results: NADPH binding; Fig 1 consensus cycle; GSH/GSSG complexes

experimental_model

Purified human glutathione reductase crystals with natural substrates, 0.95-1.1-A resolution, chemically reduced controls.

exposure

Purified-enzyme assay

limitations

Structural support for the established catalytic cycle; radiation reduction must be distinguished from natural catalysis.

nutrient_topic

Riboflavin research collection; topical membership is not evidence of a direct dietary effect. · Riboflavin (vitamin B2)

organism

Homo sapiens

plain_language

NADPH supplies electrons to the B2-derived cofactor.

primary_references

[berkholz2008] Catalytic cycle of human glutathione reductase near 1 A resolution. (2008). https://pubmed.ncbi.nlm.nih.gov/18638483/ DOI: 10.1016/j.jmb.2008.06.083

tissue_or_cell_type

Purified human erythrocyte-type GSR crystals

Riboflavin: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 1304–1316

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified human glutathione reductase crystals with natural substrates, 0.95-1.1-A resolution, chemically reduced controls. · source_derived_draft · unverified_draft

### b2-gsr-nadph-to-fad Human GSR substrate structures place NADPH for hydride transfer to bound FAD, the first redox step in glutathione recycling. Condition category: normal nutrient_topic: Riboflavin research collection; topical membership is not evidence of a direct dietary effect. plain_language: NADPH supplies electrons to the B2-derived cofactor. organism: Homo sapiens tissue_or_cell_type: Purified human erythrocyte-type GSR crystals experimental_model: Purified human glutathione reductase crystals with natural substrates, 0.95-1.1-A resolution, chemically reduced controls. limitations: Structural support for the established catalytic cycle; radiation reduction must be distinguished from natural catalysis. exposure: Purified-enzyme assay cross_nutrient: Nicotinamide-containing NADPH and B2-derived FAD perform distinct functions. evidence_location: Results: NADPH binding; Fig 1 consensus cycle; GSH/GSSG complexes [berkholz2008] Catalytic cycle of human glutathione reductase near 1 A resolution. (2008). https://pubmed.ncbi.nlm.nih.gov/18638483/ DOI: 10.1016/j.jmb.2008.06.083

availability_state

nutrient_deficiency Imported condition classification; unverified.

experimental_model

Double-blind controlled trial in 60 lactating women from two Gambian villages and their infants.

exposure

Maternal 2 mg/day riboflavin or placebo for 12 weeks; background intake about 0.5 mg/day; supplementation-withdrawal observations.

limitations

Supports maternal-infant supply responsiveness; not proof of a developmental benefit or an independently measured transport mechanism.

nutrient_topic

Riboflavin research collection; topical membership is not evidence of a direct dietary effect. · Riboflavin (vitamin B2)

organism

Homo sapiens

plain_language

The infant marker improved while maternal B2 was supplied and worsened again after it stopped.

primary_references

[b2-bates1982] Riboflavin requirements of lactating Gambian women: a controlled supplementation trial (1982). https://pubmed.ncbi.nlm.nih.gov/7072623/ DOI: 10.1093/ajcn/35.4.701

tissue_or_cell_type

Infant erythrocytes in maternal lactation trial

trigger_kind

nutrient_deficiency Imported condition classification; unverified.

Riboflavin: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 1777–1787

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Double-blind controlled trial in 60 lactating women from two Gambian villages and their infants. · source_derived_draft · unverified_draft

### b2-milk-infant-marker-response Infants of supplemented mothers had lower activation coefficients; maternal and infant values rose toward placebo levels after supplement withdrawal. Condition category: nutrient_deficiency nutrient_topic: Riboflavin research collection; topical membership is not evidence of a direct dietary effect. plain_language: The infant marker improved while maternal B2 was supplied and worsened again after it stopped. organism: Homo sapiens tissue_or_cell_type: Infant erythrocytes in maternal lactation trial experimental_model: Double-blind controlled trial in 60 lactating women from two Gambian villages and their infants. limitations: Supports maternal-infant supply responsiveness; not proof of a developmental benefit or an independently measured transport mechanism. exposure: Maternal 2 mg/day riboflavin or placebo for 12 weeks; background intake about 0.5 mg/day; supplementation-withdrawal observations. [b2-bates1982] Riboflavin requirements of lactating Gambian women: a controlled supplementation trial (1982). https://pubmed.ncbi.nlm.nih.gov/7072623/ DOI: 10.1093/ajcn/35.4.701

evidence_span

{"source_cache": "artifacts/nasunin-research/25442541.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "14f1cfb323570e36200958bb6acb4c083621b7b02ebda1e793d133b3ea95b1c7", "start_char": 0, "end_char": 1299, "text_sha256": "14f1cfb323570e36200958bb6acb4c083621b7b02ebda1e793d133b3ea95b1c7"}

experimental_model

Comparative anthocyanin exposure in cultured colon cancer lines

exposure

Nasunin and differently glycosylated delphinidin derivatives; quantitative regimens not specified in indexed abstract

limitations

Primary experiments are described despite an additional Review index tag. Protein association does not establish GSR-mediated causality; these are cancer cells, not normal colon tissue or patients.

nutrient_topic

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

organism

Human HT-29 and HCT-116 cells

plain_language

This identifies a shared enzyme connection without proving it caused the response.

primary_references

[nasunin-p25442541] Effect of glycosylation patterns of Chinese eggplant anthocyanins and other derivatives on antioxidant effectiveness in human colon cell lines. (2015). https://pubmed.ncbi.nlm.nih.gov/25442541/ DOI: 10.1016/j.foodchem.2014.08.100

tissue_or_cell_type

ROS, glutathione reductase protein and DNA damage

Nasunin: identity, redox chemistry and nutrient connections (2026-09-17) · lines 692–703

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Comparative anthocyanin exposure in cultured colon cancer lines · source_derived_draft · unverified_draft

### nasunin-colon-gsr-association The derivative-dependent ROS results tracked GSR protein levels in HT-29 cells. Condition category: normal nutrient_topic: Nasunin research collection; topical membership is not evidence of a direct dietary effect. plain_language: This identifies a shared enzyme connection without proving it caused the response. organism: Human HT-29 and HCT-116 cells tissue_or_cell_type: ROS, glutathione reductase protein and DNA damage experimental_model: Comparative anthocyanin exposure in cultured colon cancer lines limitations: Primary experiments are described despite an additional Review index tag. Protein association does not establish GSR-mediated causality; these are cancer cells, not normal colon tissue or patients. exposure: Nasunin and differently glycosylated delphinidin derivatives; quantitative regimens not specified in indexed abstract evidence_span: {"source_cache": "artifacts/nasunin-research/25442541.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "14f1cfb323570e36200958bb6acb4c083621b7b02ebda1e793d133b3ea95b1c7", "start_char": 0, "end_char": 1299, "text_sha256": "14f1cfb323570e36200958bb6acb4c083621b7b02ebda1e793d133b3ea95b1c7"} [nasunin-p25442541] Effect of glycosylation patterns of Chinese eggplant anthocyanins and other derivatives on antioxidant effectiveness in human colon cell lines. (2015). https://pubmed.ncbi.nlm.nih.gov/25442541/ DOI: 10.1016/j.foodchem.2014.08.100