Component

Activation of nuclear factor kappa B

Activation of nuclear factor kappa B. Species, exposure and limitations are retained in each linked claim.

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. Dectin-1 is recruited to phagosomes containing zymosan particles but not to phagosomes containing immunoglobulin G-opsonised particles, dectin-1 expression enhances Toll-like receptor-mediated activation of nuclear factor kappa B by beta-glucan-containing particles, and in macrophages and dendritic cells dectin-1 and Toll-like receptors are synergistic in mediating production of cytokines such as interleukin 12 and tumour necrosis factor alpha, while dectin-1 triggers production of reactive oxygen species, an inflammatory response that is primed by Toll-like receptor activation.

    Dectin-1 / CLEC7A → Activation of nuclear factor kappa B source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/glucan-research/12719479.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "297eb222223ff6861d6890a273716f4cfb3f3c14f887c57c057c2af524f8b425", "start_char": 0, "end_char": 1588, "text_sha256": "297eb222223ff6861d6890a273716f4cfb3f3c14f887c57c057c2af524f8b425"}
    experimental_model
    Dectin-1 and Toll-like receptor co-expression with phagosome recruitment and cytokine measurement
    exposure
    Beta-glucan-containing zymosan particles on cells expressing dectin-1 with and without Toll-like receptor signalling
    limitations
    The particle is zymosan, which carries mannan and other yeast wall components as well as glucan, so a response to zymosan is not by itself a response to purified beta-glucan.
    nutrient_topic
    Beta-glucan research collection; topical membership is not evidence of a direct clinical effect, and each preparation is recorded as its own entity with no family link joining any pair. · Beta-glucan
    organism
    Mouse
    plain_language
    The glucan receptor does not work alone; paired with a bacterial sensor the same particle produces far more than either would.
    primary_references
    [bg-p12719479] Collaborative induction of inflammatory responses by dectin-1 and Toll-like receptor 2. (2003). https://pubmed.ncbi.nlm.nih.gov/12719479/ DOI: 10.1084/jem.20021787
    tissue_or_cell_type
    Macrophage and dendritic cell

    Beta-glucan: a structural family rather than an agent, what decides whether a bound glucan actually signals, the complement route that a cereal and a yeast preparation share, and the unequal human evidence behind each (2026-09-22) · lines 190–201

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Dectin-1 and Toll-like receptor co-expression with phagosome recruitment and cytokine measurement · source_derived_draft · unverified_draft

    ### bg-dectin1-works-with-tlr2 Dectin-1 is recruited to phagosomes containing zymosan particles but not to phagosomes containing immunoglobulin G-opsonised particles, dectin-1 expression enhances Toll-like receptor-mediated activation of nuclear factor kappa B by beta-glucan-containing particles, and in macrophages and dendritic cells dectin-1 and Toll-like receptors are synergistic in mediating production of cytokines such as interleukin 12 and tumour necrosis factor alpha, while dectin-1 triggers production of reactive oxygen species, an inflammatory response that is primed by Toll-like receptor activation. Condition category: normal nutrient_topic: Beta-glucan research collection; topical membership is not evidence of a direct clinical effect, and each preparation is recorded as its own entity with no family link joining any pair. plain_language: The glucan receptor does not work alone; paired with a bacterial sensor the same particle produces far more than either would. organism: Mouse tissue_or_cell_type: Macrophage and dendritic cell experimental_model: Dectin-1 and Toll-like receptor co-expression with phagosome recruitment and cytokine measurement limitations: The particle is zymosan, which carries mannan and other yeast wall components as well as glucan, so a response to zymosan is not by itself a response to purified beta-glucan. exposure: Beta-glucan-containing zymosan particles on cells expressing dectin-1 with and without Toll-like receptor signalling evidence_span: {"source_cache": "artifacts/glucan-research/12719479.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "297eb222223ff6861d6890a273716f4cfb3f3c14f887c57c057c2af524f8b425", "start_char": 0, "end_char": 1588, "text_sha256": "297eb222223ff6861d6890a273716f4cfb3f3c14f887c57c057c2af524f8b425"} [bg-p12719479] Collaborative induction of inflammatory responses by dectin-1 and Toll-like receptor 2. (2003). https://pubmed.ncbi.nlm.nih.gov/12719479/ DOI: 10.1084/jem.20021787
    Complete structured claim and evidence

  2. The anti-inflammatory drugs sodium salicylate and aspirin inhibited activation of nuclear factor kappa B, an inhibition which prevented degradation of the inhibitor I-kappa-B so that nuclear factor kappa B was retained in the cytosol, and both also inhibited nuclear factor kappa B-dependent transcription from the immunoglobulin kappa enhancer and the human immunodeficiency virus long terminal repeat in transfected T cells.

    Salicylate / salicylic acid → Activation of nuclear factor kappa B source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/aspirin-research/8052854.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d1d488e1bc53706da4f733f3fecc2bb981c09c0aa2dccae2bac9fac1bb04cec1", "start_char": 0, "end_char": 737, "text_sha256": "d1d488e1bc53706da4f733f3fecc2bb981c09c0aa2dccae2bac9fac1bb04cec1"}
    experimental_model
    Electrophoretic mobility shift and reporter transcription assays in transfected T cells
    exposure
    Sodium salicylate and aspirin applied to nuclear factor kappa B activation
    limitations
    A cell-based mechanism recorded at the concentrations used in the assay, which are far above those reached by antiplatelet dosing. It does not distinguish the two compounds from one another.
    nutrient_topic
    Aspirin research collection; topical membership is not evidence of a direct clinical effect, and aspirin is recorded separately from salicylate, the metabolite it becomes. · Aspirin / acetylsalicylic acid
    organism
    Human cells
    plain_language
    Both compounds keep an inflammatory master switch locked out of the nucleus.
    primary_references
    [asa-p8052854] Inhibition of NF-kappa B by sodium salicylate and aspirin. (1994). https://pubmed.ncbi.nlm.nih.gov/8052854/ DOI: 10.1126/science.8052854
    tissue_or_cell_type
    T lymphocytes

    Aspirin: the serine it acetylates, the enzyme that acetylation creates, the dose that separates platelet from vessel wall, and the metabolite that is a different drug (2026-09-22) · lines 468–479

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Electrophoretic mobility shift and reporter transcription assays in transfected T cells · source_derived_draft · unverified_draft

    ### asa-salicylate-blocks-nfkb The anti-inflammatory drugs sodium salicylate and aspirin inhibited activation of nuclear factor kappa B, an inhibition which prevented degradation of the inhibitor I-kappa-B so that nuclear factor kappa B was retained in the cytosol, and both also inhibited nuclear factor kappa B-dependent transcription from the immunoglobulin kappa enhancer and the human immunodeficiency virus long terminal repeat in transfected T cells. Condition category: normal nutrient_topic: Aspirin research collection; topical membership is not evidence of a direct clinical effect, and aspirin is recorded separately from salicylate, the metabolite it becomes. plain_language: Both compounds keep an inflammatory master switch locked out of the nucleus. organism: Human cells tissue_or_cell_type: T lymphocytes experimental_model: Electrophoretic mobility shift and reporter transcription assays in transfected T cells limitations: A cell-based mechanism recorded at the concentrations used in the assay, which are far above those reached by antiplatelet dosing. It does not distinguish the two compounds from one another. exposure: Sodium salicylate and aspirin applied to nuclear factor kappa B activation evidence_span: {"source_cache": "artifacts/aspirin-research/8052854.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d1d488e1bc53706da4f733f3fecc2bb981c09c0aa2dccae2bac9fac1bb04cec1", "start_char": 0, "end_char": 737, "text_sha256": "d1d488e1bc53706da4f733f3fecc2bb981c09c0aa2dccae2bac9fac1bb04cec1"} [asa-p8052854] Inhibition of NF-kappa B by sodium salicylate and aspirin. (1994). https://pubmed.ncbi.nlm.nih.gov/8052854/ DOI: 10.1126/science.8052854
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Oat-beta-glucan enhances anti-PD-1 efficacy in murine models by selectively expanding Faecalibacterium prausnitzii, combining anti-PD-1 with either oat-beta-glucan or F. prausnitzii boosts intratumoral dendritic cell and CD8+ T cell infiltration and cytotoxic activation compared with anti-PD-1 monotherapy, metabolomics identifies F. prausnitzii-derived butyrate and indole-3-propionic acid as key mediators with butyrate activating dendritic cells via the HDAC8, H3K27ac and NF-kappa-B p65 pathway, in a colorectal cancer cohort undergoing anti-PD-1 treatment higher baseline F. prausnitzii abundance and elevated plasma butyrate and indole-3-propionic acid correlate with improved responses, and a human intervention study confirms oat-beta-glucan safety, its ability to increase butyrate and indole-3-propionic acid, and its capacity to modulate F. prausnitzii.

    Oat mixed-linkage beta-(1->3)/(1->4)-glucan → Efficacy of anti-PD-1 checkpoint blockade source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/glucan-research/42214334.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "1e145fb1c4163d9e0cd10a4055b68fa47de521dcf19d25253d42fc9c971d56ba", "start_char": 0, "end_char": 1310, "text_sha256": "1e145fb1c4163d9e0cd10a4055b68fa47de521dcf19d25253d42fc9c971d56ba"}
    experimental_model
    Murine tumour models with selective bacterial expansion and metabolomics, plus a human cohort and a human intervention study
    exposure
    Oat beta-glucan with anti-PD-1 checkpoint blockade in mice, and oat beta-glucan supplementation in people
    limitations
    The causal efficacy claim is demonstrated in mice. The human components are a correlation in a colorectal cancer cohort and an intervention study reporting safety and metabolite change, so no anticancer benefit in people is established here.
    nutrient_topic
    Beta-glucan research collection; topical membership is not evidence of a direct clinical effect, and each preparation is recorded as its own entity with no family link joining any pair. · Beta-glucan
    organism
    Mouse
    plain_language
    The cereal glucan never touches the tumour; it feeds a gut bacterium whose products wake the cells that do.
    primary_references
    [bg-p42214334] Oat-β-glucan potentiates anti-PD-1 efficacy through Faecalibacterium prausnitzii-derived butyrate and indole-3-propionic acid. (2026). https://pubmed.ncbi.nlm.nih.gov/42214334/ DOI: 10.1016/j.chom.2026.05.002
    tissue_or_cell_type
    Gut microbiota and tumour microenvironment

    Beta-glucan: a structural family rather than an agent, what decides whether a bound glucan actually signals, the complement route that a cereal and a yeast preparation share, and the unequal human evidence behind each (2026-09-22) · lines 658–669

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Murine tumour models with selective bacterial expansion and metabolomics, plus a human cohort and a human intervention study · source_derived_draft · unverified_draft

    ### bg-a-cereal-glucan-reaches-immunity Oat-beta-glucan enhances anti-PD-1 efficacy in murine models by selectively expanding Faecalibacterium prausnitzii, combining anti-PD-1 with either oat-beta-glucan or F. prausnitzii boosts intratumoral dendritic cell and CD8+ T cell infiltration and cytotoxic activation compared with anti-PD-1 monotherapy, metabolomics identifies F. prausnitzii-derived butyrate and indole-3-propionic acid as key mediators with butyrate activating dendritic cells via the HDAC8, H3K27ac and NF-kappa-B p65 pathway, in a colorectal cancer cohort undergoing anti-PD-1 treatment higher baseline F. prausnitzii abundance and elevated plasma butyrate and indole-3-propionic acid correlate with improved responses, and a human intervention study confirms oat-beta-glucan safety, its ability to increase butyrate and indole-3-propionic acid, and its capacity to modulate F. prausnitzii. Condition category: normal nutrient_topic: Beta-glucan research collection; topical membership is not evidence of a direct clinical effect, and each preparation is recorded as its own entity with no family link joining any pair. plain_language: The cereal glucan never touches the tumour; it feeds a gut bacterium whose products wake the cells that do. organism: Mouse tissue_or_cell_type: Gut microbiota and tumour microenvironment experimental_model: Murine tumour models with selective bacterial expansion and metabolomics, plus a human cohort and a human intervention study limitations: The causal efficacy claim is demonstrated in mice. The human components are a correlation in a colorectal cancer cohort and an intervention study reporting safety and metabolite change, so no anticancer benefit in people is established here. exposure: Oat beta-glucan with anti-PD-1 checkpoint blockade in mice, and oat beta-glucan supplementation in people evidence_span: {"source_cache": "artifacts/glucan-research/42214334.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "1e145fb1c4163d9e0cd10a4055b68fa47de521dcf19d25253d42fc9c971d56ba", "start_char": 0, "end_char": 1310, "text_sha256": "1e145fb1c4163d9e0cd10a4055b68fa47de521dcf19d25253d42fc9c971d56ba"} [bg-p42214334] Oat-β-glucan potentiates anti-PD-1 efficacy through Faecalibacterium prausnitzii-derived butyrate and indole-3-propionic acid. (2026). https://pubmed.ncbi.nlm.nih.gov/42214334/ DOI: 10.1016/j.chom.2026.05.002
    Complete structured claim and evidence

In the sources

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