Component

Human inducible nitric oxide synthase / iNOS / NOS2

Human inducible nitric oxide synthase / iNOS / NOS2. Species, exposure and limitations are retained in each linked claim.

2 recorded relationships. Experimental role, claim status and evidence remain attached to each record.

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. Indicaxanthin reduced induced nitric oxide synthase expression in IL-1beta-exposed Caco-2 cells.

    Experimental context and source evidence
    dose
    Indicaxanthin 5-25 micromolar with IL-1beta 25 ng/mL
    duration
    24 h for mediator release and permeability; earlier signaling assays
    evidence_access
    Primary PubMed abstract; detailed exposure for PMID 23931157 additionally checked in publisher results. No uninspected full text is claimed.
    evidence_scope
    literature_reviewed; source-derived curation, not universally established human effects
    experimental_model
    Differentiated human Caco-2 intestinal epithelial monolayers
    limitations
    No clinical IBD treatment effect or molecular binding site was established. Total thiols must not be relabeled as a specific glutathione measurement.
    nutrient_topic
    Betalains collection; each molecular form, species, exposure and preparation remains explicit. · Betalains
    organism
    Differentiated human Caco-2 intestinal epithelial monolayers
    plain_language
    Indicaxanthin reduced induced nitric oxide synthase expression in IL-1beta-exposed Caco-2 cells.
    primary_references
    Indicaxanthin inhibits NADPH oxidase (NOX)-1 activation and NF-κB-dependent release of inflammatory mediators and prevents the increase of epithelial permeability in IL-1β-exposed Caco-2 cells. (2014). https://pubmed.ncbi.nlm.nih.gov/23931157/ DOI: 10.1017/S0007114513002663
    route
    In vitro co-incubation
    tissue
    Intestinal epithelial model

    Betalains: mechanisms, molecular forms and cross-actor connections (2026-09-20) · lines 287–295

    Original AI-assisted curation of twelve primary research papers; study-specific PubMed/DOI links and limitations retained. Not publisher full text. · supports · Differentiated human Caco-2 intestinal epithelial monolayers · source_derived_draft · unverified_draft

    ## betalains-caco2-nos2 Indicaxanthin reduced induced nitric oxide synthase expression in IL-1beta-exposed Caco-2 cells. Model/species: Differentiated human Caco-2 intestinal epithelial monolayers Tissue: Intestinal epithelial model Exposure: Indicaxanthin 5-25 micromolar with IL-1beta 25 ng/mL Route: In vitro co-incubation Duration: 24 h for mediator release and permeability; earlier signaling assays Limits: No clinical IBD treatment effect or molecular binding site was established. Total thiols must not be relabeled as a specific glutathione measurement. Primary reference: Indicaxanthin inhibits NADPH oxidase (NOX)-1 activation and NF-κB-dependent release of inflammatory mediators and prevents the increase of epithelial permeability in IL-1β-exposed Caco-2 cells. (2014). https://pubmed.ncbi.nlm.nih.gov/23931157/ DOI: 10.1017/S0007114513002663
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. The NOS2 zinc-tetrathiolate center supported intersubunit contacts and integrity of the BH4-binding site.

    Zinc(II) ion → Human iNOS dimer stability source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/citrulline-research/10409685.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "c320fb6f3fd659a2e7df4a8ddd3467a902a07b84380075d429040eaf244ccf6b", "start_char": 0, "end_char": 942, "text_sha256": "c320fb6f3fd659a2e7df4a8ddd3467a902a07b84380075d429040eaf244ccf6b"}
    experimental_model
    Crystal structures of zinc-free and zinc-bound heme domains
    exposure
    Zinc-free versus zinc-tetrathiolate-containing structures
    limitations
    Direct structure is NOS2; similarity to NOS3 does not justify silently treating the proteins as identical.
    nutrient_topic
    Citrulline research collection; topical membership is not evidence of a direct dietary effect. · L-Citrulline
    organism
    Human NOS2
    plain_language
    The structural metal and the pterin-binding region are connected.
    primary_references
    [citrulline-p10409685] Crystal structures of zinc-free and -bound heme domain of human inducible nitric-oxide synthase. Implications for dimer stability and comparison with endothelial nitric-oxide synthase. (1999). https://pubmed.ncbi.nlm.nih.gov/10409685/ DOI: 10.1074/jbc.274.30.21276
    tissue_or_cell_type
    NOS dimer interface and pterin-binding region

    Citrulline: arginine recycling, nitrogen disposal and nutrient connections (2026-09-17) · lines 606–617

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Crystal structures of zinc-free and zinc-bound heme domains · source_derived_draft · unverified_draft

    ### citrulline-inos-zinc-interface The NOS2 zinc-tetrathiolate center supported intersubunit contacts and integrity of the BH4-binding site. Condition category: normal nutrient_topic: Citrulline research collection; topical membership is not evidence of a direct dietary effect. plain_language: The structural metal and the pterin-binding region are connected. organism: Human NOS2 tissue_or_cell_type: NOS dimer interface and pterin-binding region experimental_model: Crystal structures of zinc-free and zinc-bound heme domains limitations: Direct structure is NOS2; similarity to NOS3 does not justify silently treating the proteins as identical. exposure: Zinc-free versus zinc-tetrathiolate-containing structures evidence_span: {"source_cache": "artifacts/citrulline-research/10409685.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "c320fb6f3fd659a2e7df4a8ddd3467a902a07b84380075d429040eaf244ccf6b", "start_char": 0, "end_char": 942, "text_sha256": "c320fb6f3fd659a2e7df4a8ddd3467a902a07b84380075d429040eaf244ccf6b"} [citrulline-p10409685] Crystal structures of zinc-free and -bound heme domain of human inducible nitric-oxide synthase. Implications for dimer stability and comparison with endothelial nitric-oxide synthase. (1999). https://pubmed.ncbi.nlm.nih.gov/10409685/ DOI: 10.1074/jbc.274.30.21276
    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