Component

SLC7A11

Independent entity for contextual scientific-audit claims; no universal nutritional effect implied.

16 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. SLC7A11 silencing lowered GPX4/FTMT expression and total glutathione while worsening ferroptosis-associated measurements in HepG2 cells.

    SLC7A11 → GPX4 source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_access
    Primary full text
    experimental_model
    Human HepG2 loss/gain-of-function experiments.
    limitations
    Not a selective rescue test proving all luteolin effects require SLC7A11.
    nutrient_topic
    Luteolin collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Luteolin / 3′,4′,5,7-tetrahydroxyflavone
    plain_language
    Precursor handling and peroxide defense are linked.
    primary_references
    Luteolin attenuates CCl4-induced hepatic injury by inhibiting ferroptosis via SLC7A11. · 2024 · https://pubmed.ncbi.nlm.nih.gov/38755566/ · DOI 10.1186/s12906-024-04486-2
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Luteolin: metabolism, immune signaling, redox chemistry and cross-nutrient mechanisms (2026-09-19) · lines 524–530

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Human HepG2 loss/gain-of-function experiments. · source_derived_draft · unverified_draft

    ## luteolin-slc7a11-knockdown Precursor handling and peroxide defense are linked. SLC7A11 silencing lowered GPX4/FTMT expression and total glutathione while worsening ferroptosis-associated measurements in HepG2 cells. Model: Human HepG2 loss/gain-of-function experiments. Limitations: Not a selective rescue test proving all luteolin effects require SLC7A11. Evidence access: Primary full text Luteolin attenuates CCl4-induced hepatic injury by inhibiting ferroptosis via SLC7A11. · 2024 · https://pubmed.ncbi.nlm.nih.gov/38755566/ · DOI 10.1186/s12906-024-04486-2
    Complete structured claim and evidence

  2. High SLC7A11-mediated cystine uptake increased reliance on glucose and the pentose phosphate pathway; glucose deprivation depleted NADPH and promoted intracellular disulfide accumulation.

    SLC7A11 → Disulfide stress in SLC7A11-high human cells source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    nutrient_deficiency Imported condition classification; unverified.
    evidence_access
    Primary full text
    experimental_model
    Human cancer-cell transporter manipulation, glucose withdrawal and metabolic assays.
    limitations
    Complete glucose withdrawal in culture is not ordinary fasting or dietary carbohydrate restriction.
    nutrient_topic
    L-Cysteine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Cysteine
    plain_language
    Importing more oxidized nutrient also creates more work for the reducing system.
    primary_references
    Cystine transporter regulation of pentose phosphate pathway dependency and disulfide stress exposes a targetable metabolic vulnerability in cancer. · 2020 · https://pubmed.ncbi.nlm.nih.gov/32231310/ · DOI 10.1038/s41556-020-0496-x
    trigger_kind
    nutrient_deficiency Imported condition classification; unverified.

    L-Cysteine: sulfur allocation, redox supply and cross-nutrient mechanisms (2026-09-19) · lines 236–242

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human cancer-cell transporter manipulation, glucose withdrawal and metabolic assays. · source_derived_draft · unverified_draft

    ## l-cysteine-cystine-nadph-demand Importing more oxidized nutrient also creates more work for the reducing system. High SLC7A11-mediated cystine uptake increased reliance on glucose and the pentose phosphate pathway; glucose deprivation depleted NADPH and promoted intracellular disulfide accumulation. Model: Human cancer-cell transporter manipulation, glucose withdrawal and metabolic assays. Limitations: Complete glucose withdrawal in culture is not ordinary fasting or dietary carbohydrate restriction. Evidence access: Primary full text Cystine transporter regulation of pentose phosphate pathway dependency and disulfide stress exposes a targetable metabolic vulnerability in cancer. · 2020 · https://pubmed.ncbi.nlm.nih.gov/32231310/ · DOI 10.1038/s41556-020-0496-x
    Complete structured claim and evidence

  3. System xc− inhibition lowered CoA and increased upstream pantothenate in the tested pancreatic cancer cells.

    SLC7A11 → Coenzyme A source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_access
    Primary full text
    experimental_model
    Human PDAC cultures with cystine-import inhibition and metabolomics.
    limitations
    Pantothenate accumulation is not proof of B5 toxicity or a clinical biomarker threshold.
    nutrient_topic
    L-Cysteine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Cysteine
    plain_language
    Vitamin B5 could accumulate while its downstream product fell because another substrate was missing.
    primary_references
    Cysteine depletion induces pancreatic tumor ferroptosis in mice. · 2020 · https://pubmed.ncbi.nlm.nih.gov/32241947/ · DOI 10.1126/science.aaw9872
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    L-Cysteine: sulfur allocation, redox supply and cross-nutrient mechanisms (2026-09-19) · lines 196–202

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human PDAC cultures with cystine-import inhibition and metabolomics. · source_derived_draft · unverified_draft

    ## l-cysteine-pdac-coa-branch Vitamin B5 could accumulate while its downstream product fell because another substrate was missing. System xc− inhibition lowered CoA and increased upstream pantothenate in the tested pancreatic cancer cells. Model: Human PDAC cultures with cystine-import inhibition and metabolomics. Limitations: Pantothenate accumulation is not proof of B5 toxicity or a clinical biomarker threshold. Evidence access: Primary full text Cysteine depletion induces pancreatic tumor ferroptosis in mice. · 2020 · https://pubmed.ncbi.nlm.nih.gov/32241947/ · DOI 10.1126/science.aaw9872
    Complete structured claim and evidence

  4. Human hxCTb required 4F2hc for sodium-independent cystine/glutamate transport in oocytes.

    SLC7A11 → Cystine source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/glutathione-research/11406111.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e7118afd8c6055ed926ee24dbb7a07538f676163d605115ae0d32d49fbef7fdc", "start_char": 0, "end_char": 1364, "text_sha256": "e7118afd8c6055ed926ee24dbb7a07538f676163d605115ae0d32d49fbef7fdc"}
    experimental_model
    Human xCT expression and oxidative-stress response
    exposure
    hxCTb with 4F2hc; diethyl maleate challenge
    limitations
    Sodium independence belongs to this transporter; other cysteine-entry routes differ.
    nutrient_topic
    Glutathione research collection; topical membership is not evidence of a direct dietary effect. · GSH
    organism
    Human transporter; Xenopus expression host
    plain_language
    The precursor-entry route depends on two transporter subunits.
    primary_references
    [glutathione-p11406111] Human cystine/glutamate transporter: cDNA cloning and upregulation by oxidative stress in glioma cells. (2001). https://pubmed.ncbi.nlm.nih.gov/11406111/ DOI: 10.1016/s0005-2736(01)00338-8
    tissue_or_cell_type
    Oocyte membranes and human U87 glioma cells
    transport_effect
    depends The record names the cystine/glutamate exchange pair and the 4F2hc requirement, not which way cystine crossed.
    transport_pool
    the cytosol across the plasma membrane The record names the cystine/glutamate exchange pair and the 4F2hc requirement, not which way cystine crossed.

    Glutathione: metabolism, signaling and nutrient connections (2026-09-17) · lines 736–747

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human xCT expression and oxidative-stress response · source_derived_draft · unverified_draft

    ### glutathione-xct-cystine Human hxCTb required 4F2hc for sodium-independent cystine/glutamate transport in oocytes. Condition category: normal nutrient_topic: Glutathione research collection; topical membership is not evidence of a direct dietary effect. plain_language: The precursor-entry route depends on two transporter subunits. organism: Human transporter; Xenopus expression host tissue_or_cell_type: Oocyte membranes and human U87 glioma cells experimental_model: Human xCT expression and oxidative-stress response limitations: Sodium independence belongs to this transporter; other cysteine-entry routes differ. exposure: hxCTb with 4F2hc; diethyl maleate challenge evidence_span: {"source_cache": "artifacts/glutathione-research/11406111.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e7118afd8c6055ed926ee24dbb7a07538f676163d605115ae0d32d49fbef7fdc", "start_char": 0, "end_char": 1364, "text_sha256": "e7118afd8c6055ed926ee24dbb7a07538f676163d605115ae0d32d49fbef7fdc"} [glutathione-p11406111] Human cystine/glutamate transporter: cDNA cloning and upregulation by oxidative stress in glioma cells. (2001). https://pubmed.ncbi.nlm.nih.gov/11406111/ DOI: 10.1016/s0005-2736(01)00338-8
    Complete structured claim and evidence

  5. Diethyl maleate induced xCT expression and increased cystine uptake in U87 cells.

    SLC7A11 → cystine uptake source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/glutathione-research/11406111.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e7118afd8c6055ed926ee24dbb7a07538f676163d605115ae0d32d49fbef7fdc", "start_char": 0, "end_char": 1364, "text_sha256": "e7118afd8c6055ed926ee24dbb7a07538f676163d605115ae0d32d49fbef7fdc"}
    experimental_model
    Human xCT expression and oxidative-stress response
    exposure
    hxCTb with 4F2hc; diethyl maleate challenge
    limitations
    Sodium independence belongs to this transporter; other cysteine-entry routes differ.
    nutrient_topic
    Glutathione research collection; topical membership is not evidence of a direct dietary effect. · GSH
    organism
    Human transporter; Xenopus expression host
    plain_language
    The cells adjusted precursor uptake during the experimental challenge.
    primary_references
    [glutathione-p11406111] Human cystine/glutamate transporter: cDNA cloning and upregulation by oxidative stress in glioma cells. (2001). https://pubmed.ncbi.nlm.nih.gov/11406111/ DOI: 10.1016/s0005-2736(01)00338-8
    tissue_or_cell_type
    Oocyte membranes and human U87 glioma cells

    Glutathione: metabolism, signaling and nutrient connections (2026-09-17) · lines 749–760

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human xCT expression and oxidative-stress response · source_derived_draft · unverified_draft

    ### glutathione-xct-stress Diethyl maleate induced xCT expression and increased cystine uptake in U87 cells. Condition category: normal nutrient_topic: Glutathione research collection; topical membership is not evidence of a direct dietary effect. plain_language: The cells adjusted precursor uptake during the experimental challenge. organism: Human transporter; Xenopus expression host tissue_or_cell_type: Oocyte membranes and human U87 glioma cells experimental_model: Human xCT expression and oxidative-stress response limitations: Sodium independence belongs to this transporter; other cysteine-entry routes differ. exposure: hxCTb with 4F2hc; diethyl maleate challenge evidence_span: {"source_cache": "artifacts/glutathione-research/11406111.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e7118afd8c6055ed926ee24dbb7a07538f676163d605115ae0d32d49fbef7fdc", "start_char": 0, "end_char": 1364, "text_sha256": "e7118afd8c6055ed926ee24dbb7a07538f676163d605115ae0d32d49fbef7fdc"} [glutathione-p11406111] Human cystine/glutamate transporter: cDNA cloning and upregulation by oxidative stress in glioma cells. (2001). https://pubmed.ncbi.nlm.nih.gov/11406111/ DOI: 10.1016/s0005-2736(01)00338-8
    Complete structured claim and evidence

  6. Activated human CD4/CD8 T lymphocytes upregulate xCT and cystine uptake after TCR stimulation.

    SLC7A11 → cystine uptake source_derived_draftliterature_reviewed:direct_experimental
    Experimental context and source evidence
    cell_type
    Activated CD4 and CD8 T cells
    experimental_model
    TCR-stimulated human CD4/CD8 lymphocytes
    limitations
    Not universal basal uptake in resting cells or a selenium supplementation result.
    organism
    Homo sapiens

    Selenium: literature corrections and mechanism additions · lines 1300–1310

    Metabolic Ledger literature curation, 17 September 2026; primary papers linked individually · supports · TCR-stimulated human CD4/CD8 lymphocytes · secondary_verified · secondary_verified

    ## activated-xct Activated T cells can import cystine; resting cells need separate treatment. Activated human CD4/CD8 T lymphocytes upregulate xCT and cystine uptake after TCR stimulation. Organism: Homo sapiens Cell type: Activated CD4 and CD8 T cells Experimental model: TCR-stimulated human CD4/CD8 lymphocytes Limitations: Not universal basal uptake in resting cells or a selenium supplementation result. Primary reference: [Fluorescence-based measurement of cystine uptake through xCT shows requirement for ROS detoxification in activated lymphocytes](https://pmc.ncbi.nlm.nih.gov/articles/PMC5065394/)
    Complete structured claim and evidence

What acts on it

  1. At 5 micromolar, luteolin increased SLC7A11 expression in CCl4-challenged human HepG2 cells.

    Luteolin / 3′,4′,5,7-tetrahydroxyflavone → SLC7A11 source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text
    experimental_model
    HepG2 culture, 3.5 mM CCl4.
    limitations
    Not direct binding, transporter flux, or normal human-liver exposure.
    nutrient_topic
    Luteolin collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Luteolin / 3′,4′,5,7-tetrahydroxyflavone
    plain_language
    Cystine-handling machinery responded in an injury model.
    primary_references
    Luteolin attenuates CCl4-induced hepatic injury by inhibiting ferroptosis via SLC7A11. · 2024 · https://pubmed.ncbi.nlm.nih.gov/38755566/ · DOI 10.1186/s12906-024-04486-2

    Luteolin: metabolism, immune signaling, redox chemistry and cross-nutrient mechanisms (2026-09-19) · lines 516–522

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · HepG2 culture, 3.5 mM CCl4. · source_derived_draft · unverified_draft

    ## luteolin-slc7a11-expression Cystine-handling machinery responded in an injury model. At 5 micromolar, luteolin increased SLC7A11 expression in CCl4-challenged human HepG2 cells. Model: HepG2 culture, 3.5 mM CCl4. Limitations: Not direct binding, transporter flux, or normal human-liver exposure. Evidence access: Primary full text Luteolin attenuates CCl4-induced hepatic injury by inhibiting ferroptosis via SLC7A11. · 2024 · https://pubmed.ncbi.nlm.nih.gov/38755566/ · DOI 10.1186/s12906-024-04486-2
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. ATOX1 knockdown also impaired copper-induced SLC7A11 expression.

    Human copper chaperone ATOX1 → Copper-exposure-induced SLC7A11 expression in human MDA-MB-231 cells source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/copper-research/40944334.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "6df1716e8998546d22a1d96116e1bc35b1f7e24c94868ec5e441ada6a2be3e89", "start_char": 0, "end_char": 1634, "text_sha256": "6df1716e8998546d22a1d96116e1bc35b1f7e24c94868ec5e441ada6a2be3e89"}
    experimental_model
    Copper and iron exposure with transcription-factor knockdown
    exposure
    CuCl2 or FeCl2 exposure; NFE2L2 or ATOX1 knockdown
    limitations
    One cancer-cell model. Expression changes do not prove increased glutathione synthesis, tumor progression, or a clinical nutrient interaction.
    nutrient_topic
    Copper research collection; topical membership is not evidence of a direct dietary effect. · Copper
    organism
    Human MDA-MB-231 breast cancer cells
    plain_language
    A copper-handling protein participated in this gene-expression response.
    primary_references
    [copper-p40944334] Copper induces cystine/glutamate antiporter SLC7A11 through the activation of Nrf2 and Atox1 pathways. (2025). https://pubmed.ncbi.nlm.nih.gov/40944334/ DOI: 10.1080/10715762.2025.2560847
    tissue_or_cell_type
    Cellular amino-acid transport machinery

    Copper: transport, cuproenzymes, deficiency, excess and nutrient interactions (2026-09-17) · lines 1313–1324

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Copper and iron exposure with transcription-factor knockdown · source_derived_draft · unverified_draft

    ### copper-atox1-slc7a11 ATOX1 knockdown also impaired copper-induced SLC7A11 expression. Condition category: normal nutrient_topic: Copper research collection; topical membership is not evidence of a direct dietary effect. plain_language: A copper-handling protein participated in this gene-expression response. organism: Human MDA-MB-231 breast cancer cells tissue_or_cell_type: Cellular amino-acid transport machinery experimental_model: Copper and iron exposure with transcription-factor knockdown limitations: One cancer-cell model. Expression changes do not prove increased glutathione synthesis, tumor progression, or a clinical nutrient interaction. exposure: CuCl2 or FeCl2 exposure; NFE2L2 or ATOX1 knockdown evidence_span: {"source_cache": "artifacts/copper-research/40944334.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "6df1716e8998546d22a1d96116e1bc35b1f7e24c94868ec5e441ada6a2be3e89", "start_char": 0, "end_char": 1634, "text_sha256": "6df1716e8998546d22a1d96116e1bc35b1f7e24c94868ec5e441ada6a2be3e89"} [copper-p40944334] Copper induces cystine/glutamate antiporter SLC7A11 through the activation of Nrf2 and Atox1 pathways. (2025). https://pubmed.ncbi.nlm.nih.gov/40944334/ DOI: 10.1080/10715762.2025.2560847
    Complete structured claim and evidence

  2. CuCl2 treatment induced SLC7A11 expression in human MDA-MB-231 cells.

    Copper(II) ion → Copper-exposure-induced SLC7A11 expression in human MDA-MB-231 cells source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/copper-research/40944334.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "6df1716e8998546d22a1d96116e1bc35b1f7e24c94868ec5e441ada6a2be3e89", "start_char": 0, "end_char": 1634, "text_sha256": "6df1716e8998546d22a1d96116e1bc35b1f7e24c94868ec5e441ada6a2be3e89"}
    experimental_model
    Copper and iron exposure with transcription-factor knockdown
    exposure
    CuCl2 or FeCl2 exposure; NFE2L2 or ATOX1 knockdown
    limitations
    One cancer-cell model. Expression changes do not prove increased glutathione synthesis, tumor progression, or a clinical nutrient interaction.
    nutrient_topic
    Copper research collection; topical membership is not evidence of a direct dietary effect. · Copper
    organism
    Human MDA-MB-231 breast cancer cells
    plain_language
    Copper exposure changed part of the cystine-entry system in these cells.
    primary_references
    [copper-p40944334] Copper induces cystine/glutamate antiporter SLC7A11 through the activation of Nrf2 and Atox1 pathways. (2025). https://pubmed.ncbi.nlm.nih.gov/40944334/ DOI: 10.1080/10715762.2025.2560847
    tissue_or_cell_type
    Cellular amino-acid transport machinery

    Copper: transport, cuproenzymes, deficiency, excess and nutrient interactions (2026-09-17) · lines 1274–1285

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Copper and iron exposure with transcription-factor knockdown · source_derived_draft · unverified_draft

    ### copper-cu-slc7a11 CuCl2 treatment induced SLC7A11 expression in human MDA-MB-231 cells. Condition category: normal nutrient_topic: Copper research collection; topical membership is not evidence of a direct dietary effect. plain_language: Copper exposure changed part of the cystine-entry system in these cells. organism: Human MDA-MB-231 breast cancer cells tissue_or_cell_type: Cellular amino-acid transport machinery experimental_model: Copper and iron exposure with transcription-factor knockdown limitations: One cancer-cell model. Expression changes do not prove increased glutathione synthesis, tumor progression, or a clinical nutrient interaction. exposure: CuCl2 or FeCl2 exposure; NFE2L2 or ATOX1 knockdown evidence_span: {"source_cache": "artifacts/copper-research/40944334.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "6df1716e8998546d22a1d96116e1bc35b1f7e24c94868ec5e441ada6a2be3e89", "start_char": 0, "end_char": 1634, "text_sha256": "6df1716e8998546d22a1d96116e1bc35b1f7e24c94868ec5e441ada6a2be3e89"} [copper-p40944334] Copper induces cystine/glutamate antiporter SLC7A11 through the activation of Nrf2 and Atox1 pathways. (2025). https://pubmed.ncbi.nlm.nih.gov/40944334/ DOI: 10.1080/10715762.2025.2560847
    Complete structured claim and evidence

  3. NRF2 knockdown suppressed copper-induced SLC7A11 expression.

    Human Nrf2 / NFE2L2 → Copper-exposure-induced SLC7A11 expression in human MDA-MB-231 cells source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/copper-research/40944334.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "6df1716e8998546d22a1d96116e1bc35b1f7e24c94868ec5e441ada6a2be3e89", "start_char": 0, "end_char": 1634, "text_sha256": "6df1716e8998546d22a1d96116e1bc35b1f7e24c94868ec5e441ada6a2be3e89"}
    experimental_model
    Copper and iron exposure with transcription-factor knockdown
    exposure
    CuCl2 or FeCl2 exposure; NFE2L2 or ATOX1 knockdown
    limitations
    One cancer-cell model. Expression changes do not prove increased glutathione synthesis, tumor progression, or a clinical nutrient interaction.
    nutrient_topic
    Copper research collection; topical membership is not evidence of a direct dietary effect. · Copper
    organism
    Human MDA-MB-231 breast cancer cells
    plain_language
    The stress-response regulator was part of the transporter-expression response.
    primary_references
    [copper-p40944334] Copper induces cystine/glutamate antiporter SLC7A11 through the activation of Nrf2 and Atox1 pathways. (2025). https://pubmed.ncbi.nlm.nih.gov/40944334/ DOI: 10.1080/10715762.2025.2560847
    tissue_or_cell_type
    Cellular amino-acid transport machinery

    Copper: transport, cuproenzymes, deficiency, excess and nutrient interactions (2026-09-17) · lines 1300–1311

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Copper and iron exposure with transcription-factor knockdown · source_derived_draft · unverified_draft

    ### copper-nrf2-slc7a11 NRF2 knockdown suppressed copper-induced SLC7A11 expression. Condition category: normal nutrient_topic: Copper research collection; topical membership is not evidence of a direct dietary effect. plain_language: The stress-response regulator was part of the transporter-expression response. organism: Human MDA-MB-231 breast cancer cells tissue_or_cell_type: Cellular amino-acid transport machinery experimental_model: Copper and iron exposure with transcription-factor knockdown limitations: One cancer-cell model. Expression changes do not prove increased glutathione synthesis, tumor progression, or a clinical nutrient interaction. exposure: CuCl2 or FeCl2 exposure; NFE2L2 or ATOX1 knockdown evidence_span: {"source_cache": "artifacts/copper-research/40944334.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "6df1716e8998546d22a1d96116e1bc35b1f7e24c94868ec5e441ada6a2be3e89", "start_char": 0, "end_char": 1634, "text_sha256": "6df1716e8998546d22a1d96116e1bc35b1f7e24c94868ec5e441ada6a2be3e89"} [copper-p40944334] Copper induces cystine/glutamate antiporter SLC7A11 through the activation of Nrf2 and Atox1 pathways. (2025). https://pubmed.ncbi.nlm.nih.gov/40944334/ DOI: 10.1080/10715762.2025.2560847
    Complete structured claim and evidence

  4. Preventing cystine uptake or removing cystine relieved the disulfide stress associated with glucose deprivation in SLC7A11-high cells.

    Cystine removal during glucose starvation → Disulfide stress in SLC7A11-high human cells source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    nutrient_deficiency Imported condition classification; unverified.
    evidence_access
    Primary full text
    experimental_model
    Human cancer-cell glucose/cystine manipulation.
    limitations
    This is distinct from cystine-withdrawal ferroptosis under other conditions; no universal benefit of removing cystine is implied.
    nutrient_topic
    L-Cysteine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Cysteine
    plain_language
    Reducing the incoming load helped when the cell could not process it.
    primary_references
    Cystine transporter regulation of pentose phosphate pathway dependency and disulfide stress exposes a targetable metabolic vulnerability in cancer. · 2020 · https://pubmed.ncbi.nlm.nih.gov/32231310/ · DOI 10.1038/s41556-020-0496-x
    trigger_kind
    nutrient_deficiency Imported condition classification; unverified.

    L-Cysteine: sulfur allocation, redox supply and cross-nutrient mechanisms (2026-09-19) · lines 244–250

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human cancer-cell glucose/cystine manipulation. · source_derived_draft · unverified_draft

    ## l-cysteine-cystine-reduction-rescue Reducing the incoming load helped when the cell could not process it. Preventing cystine uptake or removing cystine relieved the disulfide stress associated with glucose deprivation in SLC7A11-high cells. Model: Human cancer-cell glucose/cystine manipulation. Limitations: This is distinct from cystine-withdrawal ferroptosis under other conditions; no universal benefit of removing cystine is implied. Evidence access: Primary full text Cystine transporter regulation of pentose phosphate pathway dependency and disulfide stress exposes a targetable metabolic vulnerability in cancer. · 2020 · https://pubmed.ncbi.nlm.nih.gov/32231310/ · DOI 10.1038/s41556-020-0496-x
    Complete structured claim and evidence

  5. Glucose starvation of SLC7A11-high human cancer cells induced abnormal disulfide bonding in actin-cytoskeleton proteins, F-actin collapse and disulfidptosis, distinct from apoptosis and ferroptosis.

    Disulfide stress in SLC7A11-high human cells → Actin-cytoskeleton disulfide bonding and collapse in human cells source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    nutrient_deficiency Imported condition classification; unverified.
    evidence_access
    Primary abstract and primary publisher figure descriptions
    experimental_model
    Human cancer cultures, chemical proteomics and cell-biological assays.
    limitations
    Experimental deprivation; do not infer this occurs whenever blood glucose falls modestly.
    nutrient_topic
    L-Cysteine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Cysteine
    plain_language
    The damage involved cross-linked structural proteins rather than the same lipid-peroxide pathway.
    primary_references
    Actin cytoskeleton vulnerability to disulfide stress mediates disulfidptosis. · 2023 · https://pubmed.ncbi.nlm.nih.gov/36747082/ · DOI 10.1038/s41556-023-01091-2
    trigger_kind
    nutrient_deficiency Imported condition classification; unverified.

    L-Cysteine: sulfur allocation, redox supply and cross-nutrient mechanisms (2026-09-19) · lines 252–258

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human cancer cultures, chemical proteomics and cell-biological assays. · source_derived_draft · unverified_draft

    ## l-cysteine-disulfidptosis-actin The damage involved cross-linked structural proteins rather than the same lipid-peroxide pathway. Glucose starvation of SLC7A11-high human cancer cells induced abnormal disulfide bonding in actin-cytoskeleton proteins, F-actin collapse and disulfidptosis, distinct from apoptosis and ferroptosis. Model: Human cancer cultures, chemical proteomics and cell-biological assays. Limitations: Experimental deprivation; do not infer this occurs whenever blood glucose falls modestly. Evidence access: Primary abstract and primary publisher figure descriptions Actin cytoskeleton vulnerability to disulfide stress mediates disulfidptosis. · 2023 · https://pubmed.ncbi.nlm.nih.gov/36747082/ · DOI 10.1038/s41556-023-01091-2
    Complete structured claim and evidence

  6. Adding CoA prevented ferroptosis induced by imidazole ketone erastin in the reported PDAC cell experiments.

    Coenzyme A → Ferroptosis in human pancreatic cancer models source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_access
    Primary full text
    experimental_model
    Human PDAC culture and exogenous CoA treatment.
    limitations
    Cell-culture rescue does not establish oral CoA absorption, intact cellular uptake in vivo or clinical efficacy.
    nutrient_topic
    L-Cysteine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Cysteine
    plain_language
    Restoring a downstream metabolite bypassed part of an upstream block in culture.
    primary_references
    Cysteine depletion induces pancreatic tumor ferroptosis in mice. · 2020 · https://pubmed.ncbi.nlm.nih.gov/32241947/ · DOI 10.1126/science.aaw9872
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    L-Cysteine: sulfur allocation, redox supply and cross-nutrient mechanisms (2026-09-19) · lines 220–226

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human PDAC culture and exogenous CoA treatment. · source_derived_draft · unverified_draft

    ## l-cysteine-pdac-coa-rescue Restoring a downstream metabolite bypassed part of an upstream block in culture. Adding CoA prevented ferroptosis induced by imidazole ketone erastin in the reported PDAC cell experiments. Model: Human PDAC culture and exogenous CoA treatment. Limitations: Cell-culture rescue does not establish oral CoA absorption, intact cellular uptake in vivo or clinical efficacy. Evidence access: Primary full text Cysteine depletion induces pancreatic tumor ferroptosis in mice. · 2020 · https://pubmed.ncbi.nlm.nih.gov/32241947/ · DOI 10.1126/science.aaw9872
    Complete structured claim and evidence

  7. Cystine starvation induced lipid oxidation and ferroptosis in four of five tested human PDAC cell lines.

    Cystine → Ferroptosis in human pancreatic cancer models source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    nutrient_deficiency Imported condition classification; unverified.
    evidence_access
    Primary full text
    experimental_model
    Human pancreatic cancer cultures; nutrient withdrawal, oxidation and viability assays.
    limitations
    Culture starvation is not dietary treatment; one of the tested lines differed.
    nutrient_topic
    L-Cysteine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Cysteine
    plain_language
    Dependence on external sulfur varied between cancer-cell models.
    primary_references
    Cysteine depletion induces pancreatic tumor ferroptosis in mice. · 2020 · https://pubmed.ncbi.nlm.nih.gov/32241947/ · DOI 10.1126/science.aaw9872
    trigger_kind
    nutrient_deficiency Imported condition classification; unverified.

    L-Cysteine: sulfur allocation, redox supply and cross-nutrient mechanisms (2026-09-19) · lines 180–186

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human pancreatic cancer cultures; nutrient withdrawal, oxidation and viability assays. · source_derived_draft · unverified_draft

    ## l-cysteine-pdac-cystine-withdrawal Dependence on external sulfur varied between cancer-cell models. Cystine starvation induced lipid oxidation and ferroptosis in four of five tested human PDAC cell lines. Model: Human pancreatic cancer cultures; nutrient withdrawal, oxidation and viability assays. Limitations: Culture starvation is not dietary treatment; one of the tested lines differed. Evidence access: Primary full text Cysteine depletion induces pancreatic tumor ferroptosis in mice. · 2020 · https://pubmed.ncbi.nlm.nih.gov/32241947/ · DOI 10.1126/science.aaw9872
    Complete structured claim and evidence

  8. Solasonine suppressed STAT3-driven SLC7A11 wild-type promoter reporter activity; binding-motif mutations abolished the reported responses.

    Solasonine → SLC7A11 promoter luciferase activity in human cells source_derived_draftungraded
    Experimental context and source evidence
    experimental_model
    Human NOZ and GBC-SD gallbladder cancer cells
    exposure
    Methods 2.2 describes 48-hour cellular drug treatments with refresh at 24 hours; exact concentration must be checked per figure and is not inferred from another assay.
    limitations
    Human cancer-cell experiments; no clinical or dietary inference. Solasonine exposure is not equivalent to APT2 depletion, ML349, or sulforaphane. Mutant rescue does not by itself establish selectivity or normal baseline mutant function. Figure 5C calls this APT2 activity, but Methods 2.17 describes an anti-LYPLA2 ELISA with mass-concentration standards and an HRP/TMB readout from cell supernatants. No direct APT2 substrate-turnover assay is described there. The result is retained as an author-labelled activity proxy, not established catalytic inhibition. This methodological qualification does not invalidate the separately reported binding or cellular observations.
    organism
    Human
    primary_locator
    Figure 3I; Results 3.3; ChIP evidence in Figure 3E-H.
    primary_references
    https://doi.org/10.1002/ptr.70245

    APT2, STAT3 and GPX4: opposing branches and assay qualification · lines 132–138

    Primary observations: 10.1038/s41467-025-56344-5 and 10.1002/ptr.70245; selected full-text review 2026-09-20. · supports · Human NOZ and GBC-SD gallbladder cancer cells · source_derived_draft · unverified_draft

    Solasonine suppressed STAT3-driven SLC7A11 wild-type promoter reporter activity; binding-motif mutations abolished the reported responses. primary_references: https://doi.org/10.1002/ptr.70245 primary_locator: Figure 3I; Results 3.3; ChIP evidence in Figure 3E-H. organism: Human experimental_model: Human NOZ and GBC-SD gallbladder cancer cells exposure: Methods 2.2 describes 48-hour cellular drug treatments with refresh at 24 hours; exact concentration must be checked per figure and is not inferred from another assay. limitations: Human cancer-cell experiments; no clinical or dietary inference. Solasonine exposure is not equivalent to APT2 depletion, ML349, or sulforaphane. Mutant rescue does not by itself establish selectivity or normal baseline mutant function. Figure 5C calls this APT2 activity, but Methods 2.17 describes an anti-LYPLA2 ELISA with mass-concentration standards and an HRP/TMB readout from cell supernatants. No direct APT2 substrate-turnover assay is described there. The result is retained as an author-labelled activity proxy, not established catalytic inhibition. This methodological qualification does not invalidate the separately reported binding or cellular observations.
    Complete structured claim and evidence

  9. STAT3 siRNA reduced SLC7A11 mRNA in the reported gallbladder cancer-cell experiments.

    STAT3 siRNA knockdown in human gallbladder cancer cells → SLC7A11 mRNA abundance in human cells source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    experimental_model
    Human NOZ and GBC-SD gallbladder cancer cells
    exposure
    siSTAT3 versus control; reciprocal STAT3 overexpression increased mRNA/protein in the same reported figure group. Transfection duration not independently resolved here.
    limitations
    Human cancer-cell experiments; no clinical or dietary inference. Solasonine exposure is not equivalent to APT2 depletion, ML349, or sulforaphane. Mutant rescue does not by itself establish selectivity or normal baseline mutant function. Figure 5C calls this APT2 activity, but Methods 2.17 describes an anti-LYPLA2 ELISA with mass-concentration standards and an HRP/TMB readout from cell supernatants. No direct APT2 substrate-turnover assay is described there. The result is retained as an author-labelled activity proxy, not established catalytic inhibition. This methodological qualification does not invalidate the separately reported binding or cellular observations.
    organism
    Human
    primary_locator
    Figure 3A-D and Supplementary Figure S3A-B; Results 3.3.
    primary_references
    https://doi.org/10.1002/ptr.70245
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    APT2, STAT3 and GPX4: opposing branches and assay qualification · lines 150–156

    Primary observations: 10.1038/s41467-025-56344-5 and 10.1002/ptr.70245; selected full-text review 2026-09-20. · supports · Human NOZ and GBC-SD gallbladder cancer cells · source_derived_draft · unverified_draft

    STAT3 siRNA reduced SLC7A11 mRNA in the reported gallbladder cancer-cell experiments. primary_references: https://doi.org/10.1002/ptr.70245 primary_locator: Figure 3A-D and Supplementary Figure S3A-B; Results 3.3. organism: Human experimental_model: Human NOZ and GBC-SD gallbladder cancer cells exposure: siSTAT3 versus control; reciprocal STAT3 overexpression increased mRNA/protein in the same reported figure group. Transfection duration not independently resolved here. limitations: Human cancer-cell experiments; no clinical or dietary inference. Solasonine exposure is not equivalent to APT2 depletion, ML349, or sulforaphane. Mutant rescue does not by itself establish selectivity or normal baseline mutant function. Figure 5C calls this APT2 activity, but Methods 2.17 describes an anti-LYPLA2 ELISA with mass-concentration standards and an HRP/TMB readout from cell supernatants. No direct APT2 substrate-turnover assay is described there. The result is retained as an author-labelled activity proxy, not established catalytic inhibition. This methodological qualification does not invalidate the separately reported binding or cellular observations.
    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