Component

Erastin

Erastin. Species, exposure and limitations are retained in each linked claim.

4 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. Erastin inhibited cystine uptake through system xc-minus, weakening antioxidant defenses before iron-dependent oxidative death.

    Erastin → cystine uptake source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/iron-research/22632970.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "c0137d17ae5942c8904ece05ab6513f4fad588149ed0d7167e49f01a63b36cb0", "start_char": 0, "end_char": 1089, "text_sha256": "c0137d17ae5942c8904ece05ab6513f4fad588149ed0d7167e49f01a63b36cb0"}
    experimental_model
    Chemical and genetic characterization of nonapoptotic cell death
    exposure
    Erastin and ferrostatin-1 experiments
    limitations
    Experimental ferroptosis; dietary iron is not equated with a cancer-cell-death drug exposure.
    nutrient_topic
    Iron research collection; topical membership is not evidence of a direct dietary effect. · Iron
    organism
    Cancer-cell systems and rat brain slices
    plain_language
    The death pathway connected iron with the supply of material needed for glutathione.
    primary_references
    [iron-p22632970] Ferroptosis: an iron-dependent form of nonapoptotic cell death. (2012). https://pubmed.ncbi.nlm.nih.gov/22632970/ DOI: 10.1016/j.cell.2012.03.042
    tissue_or_cell_type
    Cellular iron, cystine transport and oxidative injury

    Iron: absorption, trafficking, iron-dependent enzymes and nutrient interactions (2026-09-17) · lines 1239–1250

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Chemical and genetic characterization of nonapoptotic cell death · source_derived_draft · unverified_draft

    ### iron-cystine-ferroptosis Erastin inhibited cystine uptake through system xc-minus, weakening antioxidant defenses before iron-dependent oxidative death. Condition category: normal nutrient_topic: Iron research collection; topical membership is not evidence of a direct dietary effect. plain_language: The death pathway connected iron with the supply of material needed for glutathione. organism: Cancer-cell systems and rat brain slices tissue_or_cell_type: Cellular iron, cystine transport and oxidative injury experimental_model: Chemical and genetic characterization of nonapoptotic cell death limitations: Experimental ferroptosis; dietary iron is not equated with a cancer-cell-death drug exposure. exposure: Erastin and ferrostatin-1 experiments evidence_span: {"source_cache": "artifacts/iron-research/22632970.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "c0137d17ae5942c8904ece05ab6513f4fad588149ed0d7167e49f01a63b36cb0", "start_char": 0, "end_char": 1089, "text_sha256": "c0137d17ae5942c8904ece05ab6513f4fad588149ed0d7167e49f01a63b36cb0"} [iron-p22632970] Ferroptosis: an iron-dependent form of nonapoptotic cell death. (2012). https://pubmed.ncbi.nlm.nih.gov/22632970/ DOI: 10.1016/j.cell.2012.03.042
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. One micromolar spermidine enhanced erastin-associated lipid peroxidation and cell death in PC3 and DU145 cells.

    Spermidine → Human PC3/DU145 spermidine–erastin ferroptosis response source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text
    experimental_model
    Human prostate cancer cells; 1.25–5 micromolar erastin, 24-hour viability assays.
    limitations
    Not evidence of cancer prevention or a safe self-treatment combination.
    nutrient_topic
    Spermidine collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Spermidine
    plain_language
    A cancer-cell context can turn the response toward iron-dependent injury.
    primary_references
    Spermidine inactivates proteasome activity and enhances ferroptosis in prostate cancer. · 2025 · https://pubmed.ncbi.nlm.nih.gov/40486852/ · DOI 10.1016/j.apsb.2025.02.023

    Spermidine: biosynthesis, hypusination, transport and cross-nutrient mechanisms (2026-09-19) · lines 502–508

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human prostate cancer cells; 1.25–5 micromolar erastin, 24-hour viability assays. · source_derived_draft · unverified_draft

    ## spermidine-erastin-sensitization A cancer-cell context can turn the response toward iron-dependent injury. One micromolar spermidine enhanced erastin-associated lipid peroxidation and cell death in PC3 and DU145 cells. Model: Human prostate cancer cells; 1.25–5 micromolar erastin, 24-hour viability assays. Limitations: Not evidence of cancer prevention or a safe self-treatment combination. Evidence access: Primary full text Spermidine inactivates proteasome activity and enhances ferroptosis in prostate cancer. · 2025 · https://pubmed.ncbi.nlm.nih.gov/40486852/ · DOI 10.1016/j.apsb.2025.02.023
    Complete structured claim and evidence

  2. The study linked elevated NRF2 to HMOX1 upregulation and increased labile ferrous iron during combination treatment.

    Human Nrf2 / NFE2L2 → Human heme oxygenase 1 / HMOX1 source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text
    experimental_model
    Human prostate cancer combination-treatment model.
    limitations
    NRF2/HMOX1 direction depends on cell state and iron handling; no universal ferroptosis prediction.
    nutrient_topic
    Spermidine collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Spermidine
    plain_language
    Heme breakdown links this response to iron availability.
    primary_references
    Spermidine inactivates proteasome activity and enhances ferroptosis in prostate cancer. · 2025 · https://pubmed.ncbi.nlm.nih.gov/40486852/ · DOI 10.1016/j.apsb.2025.02.023

    Spermidine: biosynthesis, hypusination, transport and cross-nutrient mechanisms (2026-09-19) · lines 526–532

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human prostate cancer combination-treatment model. · source_derived_draft · unverified_draft

    ## spermidine-hmox1-iron Heme breakdown links this response to iron availability. The study linked elevated NRF2 to HMOX1 upregulation and increased labile ferrous iron during combination treatment. Model: Human prostate cancer combination-treatment model. Limitations: NRF2/HMOX1 direction depends on cell state and iron handling; no universal ferroptosis prediction. Evidence access: Primary full text Spermidine inactivates proteasome activity and enhances ferroptosis in prostate cancer. · 2025 · https://pubmed.ncbi.nlm.nih.gov/40486852/ · DOI 10.1016/j.apsb.2025.02.023
    Complete structured claim and evidence

  3. Spermidine/erastin treatment reduced proteasome activity and NRF2 degradation in the reported prostate-cell experiments.

    Spermidine → Human prostate-cell proteasome activity source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text
    experimental_model
    Human-cell proteasome activity and protein-stability assays.
    limitations
    Not proof that spermidine directly binds a specific proteasome subunit.
    nutrient_topic
    Spermidine collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Spermidine
    plain_language
    Protein accumulation can involve slower removal as well as faster production.
    primary_references
    Spermidine inactivates proteasome activity and enhances ferroptosis in prostate cancer. · 2025 · https://pubmed.ncbi.nlm.nih.gov/40486852/ · DOI 10.1016/j.apsb.2025.02.023

    Spermidine: biosynthesis, hypusination, transport and cross-nutrient mechanisms (2026-09-19) · lines 518–524

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human-cell proteasome activity and protein-stability assays. · source_derived_draft · unverified_draft

    ## spermidine-proteasome Protein accumulation can involve slower removal as well as faster production. Spermidine/erastin treatment reduced proteasome activity and NRF2 degradation in the reported prostate-cell experiments. Model: Human-cell proteasome activity and protein-stability assays. Limitations: Not proof that spermidine directly binds a specific proteasome subunit. Evidence access: Primary full text Spermidine inactivates proteasome activity and enhances ferroptosis in prostate cancer. · 2025 · https://pubmed.ncbi.nlm.nih.gov/40486852/ · DOI 10.1016/j.apsb.2025.02.023
    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