Component

Glutathione-synthesis gene expression

Transcription of genes supporting glutathione production.

3 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 acts on it

  1. DIM increased gamma-glutamylcysteine synthetase mRNA and protein in the mouse fibroblast study.

    3,3'-Diindolylmethane / DIM → Glutathione-synthesis gene expression source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/dim-research/21615272.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "1ae26f09db419c2cd095519c3326616a14343b52e23a71e7994a4aed764ab1b8", "start_char": 0, "end_char": 737, "text_sha256": "1ae26f09db419c2cd095519c3326616a14343b52e23a71e7994a4aed764ab1b8"}
    experimental_model
    Reporter and gene/protein expression experiments
    exposure
    DIM compared with I3C and sulforaphane
    limitations
    Mouse cells; transcriptional induction does not establish clinical antioxidant benefit or nutrient repletion.
    nutrient_topic
    Diindolylmethane (DIM) research collection; topical membership is not evidence of a direct dietary effect. · 3,3'-Diindolylmethane / DIM
    organism
    Mouse NIH3T3 fibroblasts
    plain_language
    This downstream enzyme is recorded separately from the Nrf2 regulator.
    primary_references
    [dim-p21615272] 3,3'-Diindolylmethane but not indole-3-carbinol activates Nrf2 and induces Nrf2 target gene expression in cultured murine fibroblasts. (2011). https://pubmed.ncbi.nlm.nih.gov/21615272/ DOI: 10.3109/10715762.2011.571683
    tissue_or_cell_type
    Nrf2-regulated defense genes

    Diindolylmethane (DIM): formation, receptor signaling, metabolism and drug interactions (2026-09-17) · lines 1273–1284

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

    ### dim-nrf2-glutathione-synthesis-gene-expression DIM increased gamma-glutamylcysteine synthetase mRNA and protein in the mouse fibroblast study. Condition category: normal nutrient_topic: Diindolylmethane (DIM) research collection; topical membership is not evidence of a direct dietary effect. plain_language: This downstream enzyme is recorded separately from the Nrf2 regulator. organism: Mouse NIH3T3 fibroblasts tissue_or_cell_type: Nrf2-regulated defense genes experimental_model: Reporter and gene/protein expression experiments limitations: Mouse cells; transcriptional induction does not establish clinical antioxidant benefit or nutrient repletion. exposure: DIM compared with I3C and sulforaphane evidence_span: {"source_cache": "artifacts/dim-research/21615272.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "1ae26f09db419c2cd095519c3326616a14343b52e23a71e7994a4aed764ab1b8", "start_char": 0, "end_char": 737, "text_sha256": "1ae26f09db419c2cd095519c3326616a14343b52e23a71e7994a4aed764ab1b8"} [dim-p21615272] 3,3'-Diindolylmethane but not indole-3-carbinol activates Nrf2 and induces Nrf2 target gene expression in cultured murine fibroblasts. (2011). https://pubmed.ncbi.nlm.nih.gov/21615272/ DOI: 10.3109/10715762.2011.571683
    Complete structured claim and evidence

  2. Human SELENOH overexpression increased glutathione-synthesis gene expression in murine HT22 cells.

    SELENOH → Glutathione-synthesis gene expression source_derived_draftliterature_reviewed:direct_experimental
    Experimental context and source evidence
    cell_type
    HT22 hippocampal cells
    experimental_model
    Overexpression
    limitations
    Does not prove an equivalent response to dietary selenium.
    organism
    human protein in mouse cells

    Selenium: literature corrections and mechanism additions · lines 870–880

    Metabolic Ledger literature curation, 17 September 2026; primary papers linked individually · supports · Overexpression · secondary_verified · secondary_verified

    ## selenoh-increases-glutathione-gene-expression Extra SELENOH increased expression of glutathione-building genes in these cells. Human SELENOH overexpression increased glutathione-synthesis gene expression in murine HT22 cells. Organism: human protein in mouse cells Cell type: HT22 hippocampal cells Experimental model: Overexpression Limitations: Does not prove an equivalent response to dietary selenium. Primary reference: [Selenoprotein H is a redox-sensing high mobility group family DNA-binding protein that up-regulates genes involved in glutathione synthesis and phase II detoxification](https://pubmed.ncbi.nlm.nih.gov/17526492/)
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. The human GCL holoenzyme was more active and less sensitive to glutathione inhibition than its catalytic subunit alone.

    Human glutamate-cysteine ligase modifier subunit / GCLM → Human glutamate-cysteine ligase catalytic activity source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/sulforaphane-research/9637733.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "4e7a66b2c4a636f70f2a5954ff304e54d4ef0f00055e53bc32ba8ceb9772fbe2", "start_char": 0, "end_char": 1258, "text_sha256": "4e7a66b2c4a636f70f2a5954ff304e54d4ef0f00055e53bc32ba8ceb9772fbe2"}
    experimental_model
    Purified recombinant subunit/holoenzyme kinetics
    exposure
    Substrate comparisons and glutathione inhibition
    limitations
    Baseline enzymology, not a sulforaphane or nutrient-repletion trial.
    nutrient_topic
    Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
    organism
    Human GCLC and GCLM expressed in insect cells
    plain_language
    The modifier subunit changes how the glutathione-building enzyme works.
    primary_references
    [sulforaphane-p9637733] Expression and characterization of human glutamate-cysteine ligase. (1998). https://pubmed.ncbi.nlm.nih.gov/9637733/ DOI: 10.1006/abbi.1998.0676
    tissue_or_cell_type
    Glutathione synthesis first-step enzyme

    Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 814–825

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified recombinant subunit/holoenzyme kinetics · source_derived_draft · unverified_draft

    ### sulforaphane-gclm-activity The human GCL holoenzyme was more active and less sensitive to glutathione inhibition than its catalytic subunit alone. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: The modifier subunit changes how the glutathione-building enzyme works. organism: Human GCLC and GCLM expressed in insect cells tissue_or_cell_type: Glutathione synthesis first-step enzyme experimental_model: Purified recombinant subunit/holoenzyme kinetics limitations: Baseline enzymology, not a sulforaphane or nutrient-repletion trial. exposure: Substrate comparisons and glutathione inhibition evidence_span: {"source_cache": "artifacts/sulforaphane-research/9637733.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "4e7a66b2c4a636f70f2a5954ff304e54d4ef0f00055e53bc32ba8ceb9772fbe2", "start_char": 0, "end_char": 1258, "text_sha256": "4e7a66b2c4a636f70f2a5954ff304e54d4ef0f00055e53bc32ba8ceb9772fbe2"} [sulforaphane-p9637733] Expression and characterization of human glutamate-cysteine ligase. (1998). https://pubmed.ncbi.nlm.nih.gov/9637733/ DOI: 10.1006/abbi.1998.0676
    Complete structured claim and evidence

In the sources

Preserved passages that mention this component, quoted exactly. Open one to read it in context.

    This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.

    Evidence, AI assistance and curation standards