Component

Lipopolysaccharide

Bacterial endotoxin preparation; species and experimental dose are study-specific.

15 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. LPS reduced the cell-surface fraction of SMVT in NCM460 cells without reducing total SMVT protein or RNA.

    Lipopolysaccharide → Human colonic epithelial cell-surface SMVT abundance source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_span
    {"source_cache": "artifacts/biotin-research/28052864.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "2f27f27a7730837eff6529a7eccf67b3587df28af01ac0507d1b692410483703", "start_char": 0, "end_char": 1549, "text_sha256": "2f27f27a7730837eff6529a7eccf67b3587df28af01ac0507d1b692410483703"}
    experimental_model
    LPS exposure of human NCM460 cells with separate mouse experiments
    exposure
    LPS, CK2 inhibitors and SMVT Thr78Ala mutation
    limitations
    CK2 involvement is supported experimentally but the full causal sequence remains qualified; whole-body human deficiency was not measured.
    nutrient_topic
    Biotin research collection; topical membership is not evidence of a direct dietary effect. · Biotin
    organism
    Homo sapiens
    plain_language
    Total transporter abundance can look normal while functional surface availability falls.
    primary_references
    [b7-p28052864] Lipopolysaccharide inhibits colonic biotin uptake via interference with membrane expression of its transporter: a role for a casein kinase 2-mediated pathway. (2017). https://pubmed.ncbi.nlm.nih.gov/28052864/ DOI: 10.1152/ajpcell.00300.2016
    tissue_or_cell_type
    Colonic epithelial NCM460 cells
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Biotin: carboxylases, recycling, deficiency and nutrient interactions (2026-09-17) · lines 1105–1116

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · LPS exposure of human NCM460 cells with separate mouse experiments · source_derived_draft · unverified_draft

    ### b7-lps-surface LPS reduced the cell-surface fraction of SMVT in NCM460 cells without reducing total SMVT protein or RNA. Condition category: machinery_impairment nutrient_topic: Biotin research collection; topical membership is not evidence of a direct dietary effect. plain_language: Total transporter abundance can look normal while functional surface availability falls. organism: Homo sapiens tissue_or_cell_type: Colonic epithelial NCM460 cells experimental_model: LPS exposure of human NCM460 cells with separate mouse experiments limitations: CK2 involvement is supported experimentally but the full causal sequence remains qualified; whole-body human deficiency was not measured. exposure: LPS, CK2 inhibitors and SMVT Thr78Ala mutation evidence_span: {"source_cache": "artifacts/biotin-research/28052864.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "2f27f27a7730837eff6529a7eccf67b3587df28af01ac0507d1b692410483703", "start_char": 0, "end_char": 1549, "text_sha256": "2f27f27a7730837eff6529a7eccf67b3587df28af01ac0507d1b692410483703"} [b7-p28052864] Lipopolysaccharide inhibits colonic biotin uptake via interference with membrane expression of its transporter: a role for a casein kinase 2-mediated pathway. (2017). https://pubmed.ncbi.nlm.nih.gov/28052864/ DOI: 10.1152/ajpcell.00300.2016
    Complete structured claim and evidence

  2. LPS reduced carrier-mediated biotin uptake in NCM460 cells; CK2 inhibition and a putative CK2-site SMVT mutant supported a CK2-related trafficking mechanism.

    Lipopolysaccharide → Human colonic epithelial biotin uptake source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_span
    {"source_cache": "artifacts/biotin-research/28052864.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "2f27f27a7730837eff6529a7eccf67b3587df28af01ac0507d1b692410483703", "start_char": 0, "end_char": 1549, "text_sha256": "2f27f27a7730837eff6529a7eccf67b3587df28af01ac0507d1b692410483703"}
    experimental_model
    LPS exposure of human NCM460 cells with separate mouse experiments
    exposure
    LPS, CK2 inhibitors and SMVT Thr78Ala mutation
    limitations
    CK2 involvement is supported experimentally but the full causal sequence remains qualified; whole-body human deficiency was not measured.
    nutrient_topic
    Biotin research collection; topical membership is not evidence of a direct dietary effect. · Biotin
    organism
    Homo sapiens
    plain_language
    Inflammatory exposure interfered with biotin entry in this model.
    primary_references
    [b7-p28052864] Lipopolysaccharide inhibits colonic biotin uptake via interference with membrane expression of its transporter: a role for a casein kinase 2-mediated pathway. (2017). https://pubmed.ncbi.nlm.nih.gov/28052864/ DOI: 10.1152/ajpcell.00300.2016
    tissue_or_cell_type
    Colonic epithelial NCM460 cells
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Biotin: carboxylases, recycling, deficiency and nutrient interactions (2026-09-17) · lines 1118–1129

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · LPS exposure of human NCM460 cells with separate mouse experiments · source_derived_draft · unverified_draft

    ### b7-lps-uptake LPS reduced carrier-mediated biotin uptake in NCM460 cells; CK2 inhibition and a putative CK2-site SMVT mutant supported a CK2-related trafficking mechanism. Condition category: machinery_impairment nutrient_topic: Biotin research collection; topical membership is not evidence of a direct dietary effect. plain_language: Inflammatory exposure interfered with biotin entry in this model. organism: Homo sapiens tissue_or_cell_type: Colonic epithelial NCM460 cells experimental_model: LPS exposure of human NCM460 cells with separate mouse experiments limitations: CK2 involvement is supported experimentally but the full causal sequence remains qualified; whole-body human deficiency was not measured. exposure: LPS, CK2 inhibitors and SMVT Thr78Ala mutation evidence_span: {"source_cache": "artifacts/biotin-research/28052864.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "2f27f27a7730837eff6529a7eccf67b3587df28af01ac0507d1b692410483703", "start_char": 0, "end_char": 1549, "text_sha256": "2f27f27a7730837eff6529a7eccf67b3587df28af01ac0507d1b692410483703"} [b7-p28052864] Lipopolysaccharide inhibits colonic biotin uptake via interference with membrane expression of its transporter: a role for a casein kinase 2-mediated pathway. (2017). https://pubmed.ncbi.nlm.nih.gov/28052864/ DOI: 10.1152/ajpcell.00300.2016
    Complete structured claim and evidence

  3. LPS lowered circulating retinol without a detected decrease in liver or kidney retinol in vitamin A-sufficient rats.

    Lipopolysaccharide → Plasma retinol concentration source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    biomarker_context Imported condition classification; unverified.
    experimental_model
    LPS versus saline with food withdrawal.
    limitations
    Acute rat model; not every inflammatory illness follows the same kinetics.
    nutrient_topic
    Vitamin A research collection; topical membership is not evidence of a direct dietary effect. · Vitamin A
    organism
    Rattus norvegicus
    plain_language
    A low blood value did not mean the measured tissue stores had been emptied.
    primary_references
    [va-rosales1996] Effects of acute inflammation on plasma retinol, retinol-binding protein, and its mRNA in the liver and kidneys of vitamin A-sufficient rats (1996). https://pubmed.ncbi.nlm.nih.gov/8725149/ DOI: 10.1016/s0022-2275(20)42007-3
    tissue_or_cell_type
    Plasma, liver and kidney
    trigger_kind
    biomarker_context Imported condition classification; unverified.

    Vitamin A: forms, mechanisms, deficiency and excess (2026-09-17) · lines 1674–1683

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · LPS versus saline with food withdrawal. · source_derived_draft · unverified_draft

    ### va-lps-lowers-retinol-with-stores LPS lowered circulating retinol without a detected decrease in liver or kidney retinol in vitamin A-sufficient rats. Condition category: biomarker_context nutrient_topic: Vitamin A research collection; topical membership is not evidence of a direct dietary effect. plain_language: A low blood value did not mean the measured tissue stores had been emptied. organism: Rattus norvegicus tissue_or_cell_type: Plasma, liver and kidney experimental_model: LPS versus saline with food withdrawal. limitations: Acute rat model; not every inflammatory illness follows the same kinetics. [va-rosales1996] Effects of acute inflammation on plasma retinol, retinol-binding protein, and its mRNA in the liver and kidneys of vitamin A-sufficient rats (1996). https://pubmed.ncbi.nlm.nih.gov/8725149/ DOI: 10.1016/s0022-2275(20)42007-3
    Complete structured claim and evidence

  4. Inflammation reduced hepatic RBP mRNA and circulating transport proteins in the same rat study.

    Lipopolysaccharide → RBP4 mRNA source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    biomarker_context Imported condition classification; unverified.
    experimental_model
    Hepatic RNA and RBP/TTR assays.
    limitations
    Reduced secretion is inferred from the combined measurements, not measured as a complete flux chain.
    nutrient_topic
    Vitamin A research collection; topical membership is not evidence of a direct dietary effect. · Vitamin A
    organism
    Rattus norvegicus
    plain_language
    Transport regulation helps explain why blood retinol can fall during illness.
    primary_references
    [va-rosales1996] Effects of acute inflammation on plasma retinol, retinol-binding protein, and its mRNA in the liver and kidneys of vitamin A-sufficient rats (1996). https://pubmed.ncbi.nlm.nih.gov/8725149/ DOI: 10.1016/s0022-2275(20)42007-3
    tissue_or_cell_type
    Liver and plasma
    trigger_kind
    biomarker_context Imported condition classification; unverified.

    Vitamin A: forms, mechanisms, deficiency and excess (2026-09-17) · lines 1685–1694

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Hepatic RNA and RBP/TTR assays. · source_derived_draft · unverified_draft

    ### va-lps-reduces-rbp-transcript Inflammation reduced hepatic RBP mRNA and circulating transport proteins in the same rat study. Condition category: biomarker_context nutrient_topic: Vitamin A research collection; topical membership is not evidence of a direct dietary effect. plain_language: Transport regulation helps explain why blood retinol can fall during illness. organism: Rattus norvegicus tissue_or_cell_type: Liver and plasma experimental_model: Hepatic RNA and RBP/TTR assays. limitations: Reduced secretion is inferred from the combined measurements, not measured as a complete flux chain. [va-rosales1996] Effects of acute inflammation on plasma retinol, retinol-binding protein, and its mRNA in the liver and kidneys of vitamin A-sufficient rats (1996). https://pubmed.ncbi.nlm.nih.gov/8725149/ DOI: 10.1016/s0022-2275(20)42007-3
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. MLG formulations reduced the LPS-induced reporter response.

    MLG-50 fossil-derived fulvic/mineral formulation → LPS-induced NF-kappa-B reporter response in human THP1-Blue cells source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text
    experimental_model
    2026 MLG-50/MLG-A50 study; fossil extracts contain fulvic fractions plus mineral/polyphenol components, stock pH about 1.97/12.1. THP1-Blue cells; 1:8192 dilution, LPS 10 or 50 ng/mL, 24 hours.
    limitations
    Co-components prevent assigning an effect to a single fulvic molecule. In-vitro activity is not established clinical benefit; preparation and dilution remain essential. LPS interaction and receptor interference are proposed from functional assays; direct TLR4 binding is not established.
    nutrient_topic
    Fulvic acid collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Fulvic acid (heterogeneous humic fraction)
    plain_language
    The mixtures changed the response to bacterial endotoxin.
    primary_references
    Integrated safety and microbiota profiling of fulvic acid formulations across in vitro and in vivo models. · 2026 · https://pubmed.ncbi.nlm.nih.gov/41580488/ · DOI 10.1038/s41598-026-37331-2

    Fulvic acid: mixture identity, mineral chemistry, signaling 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 · 2026 MLG-50/MLG-A50 study; fossil extracts contain fulvic fractions plus mineral/polyphenol components, stock pH about 1.97/12.1. THP1-Blue cells; 1:8192 dilution, LPS 10 or 50 ng/mL, 24 hours. · source_derived_draft · unverified_draft

    ## fulvic-acid-lps-signal The mixtures changed the response to bacterial endotoxin. MLG formulations reduced the LPS-induced reporter response. Model: 2026 MLG-50/MLG-A50 study; fossil extracts contain fulvic fractions plus mineral/polyphenol components, stock pH about 1.97/12.1. THP1-Blue cells; 1:8192 dilution, LPS 10 or 50 ng/mL, 24 hours. Limitations: Co-components prevent assigning an effect to a single fulvic molecule. In-vitro activity is not established clinical benefit; preparation and dilution remain essential. LPS interaction and receptor interference are proposed from functional assays; direct TLR4 binding is not established. Evidence access: Primary full text Integrated safety and microbiota profiling of fulvic acid formulations across in vitro and in vivo models. · 2026 · https://pubmed.ncbi.nlm.nih.gov/41580488/ · DOI 10.1038/s41598-026-37331-2
    Complete structured claim and evidence

  2. Nasunin attenuated Akt phosphorylation in stimulated RAW264 cells.

    Nasunin → Mouse Akt protein family (isoform unresolved) source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/nasunin-research/28812425.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "7a697b4eb979f1e6349bc79f4d2ed0d3994de51dfed777a71fb04740819eeabf", "start_char": 0, "end_char": 1094, "text_sha256": "7a697b4eb979f1e6349bc79f4d2ed0d3994de51dfed777a71fb04740819eeabf"}
    experimental_model
    LPS-stimulated macrophage experiments
    exposure
    Dose-dependent nasunin treatment; exact dose/time not reported in indexed abstract
    limitations
    These measurements do not prove direct binding to Akt, p38, NF-kappa-B or NOS2; reduced NOS2 expression is not direct enzyme inhibition. Response is LPS/cell-context dependent.
    nutrient_topic
    Nasunin research collection; topical membership is not evidence of a direct dietary effect. · Nasunin
    organism
    Mouse RAW264 macrophages
    plain_language
    The direction applies to this inflammatory setting.
    primary_references
    [nasunin-p28812425] Nasunin inhibits the lipopolysaccharide-induced pro-inflammatory mediator production in RAW264 mouse macrophages by suppressing ROS-mediated activation of PI3 K/Akt/NF-κB and p38 signaling pathways. (2017). https://pubmed.ncbi.nlm.nih.gov/28812425/ DOI: 10.1080/09168451.2017.1362973
    tissue_or_cell_type
    Inflammatory mediator secretion and signaling

    Nasunin: identity, redox chemistry and nutrient connections (2026-09-17) · lines 276–287

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · LPS-stimulated macrophage experiments · source_derived_draft · unverified_draft

    ### nasunin-akt-macrophage Nasunin attenuated Akt phosphorylation in stimulated RAW264 cells. Condition category: normal nutrient_topic: Nasunin research collection; topical membership is not evidence of a direct dietary effect. plain_language: The direction applies to this inflammatory setting. organism: Mouse RAW264 macrophages tissue_or_cell_type: Inflammatory mediator secretion and signaling experimental_model: LPS-stimulated macrophage experiments limitations: These measurements do not prove direct binding to Akt, p38, NF-kappa-B or NOS2; reduced NOS2 expression is not direct enzyme inhibition. Response is LPS/cell-context dependent. exposure: Dose-dependent nasunin treatment; exact dose/time not reported in indexed abstract evidence_span: {"source_cache": "artifacts/nasunin-research/28812425.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "7a697b4eb979f1e6349bc79f4d2ed0d3994de51dfed777a71fb04740819eeabf", "start_char": 0, "end_char": 1094, "text_sha256": "7a697b4eb979f1e6349bc79f4d2ed0d3994de51dfed777a71fb04740819eeabf"} [nasunin-p28812425] Nasunin inhibits the lipopolysaccharide-induced pro-inflammatory mediator production in RAW264 mouse macrophages by suppressing ROS-mediated activation of PI3 K/Akt/NF-κB and p38 signaling pathways. (2017). https://pubmed.ncbi.nlm.nih.gov/28812425/ DOI: 10.1080/09168451.2017.1362973
    Complete structured claim and evidence

  3. Nasunin suppressed stimulus-associated I-kappa-B-alpha degradation.

    Nasunin → Mouse inhibitor of NF-kappa-B alpha / Nfkbia source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/nasunin-research/28812425.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "7a697b4eb979f1e6349bc79f4d2ed0d3994de51dfed777a71fb04740819eeabf", "start_char": 0, "end_char": 1094, "text_sha256": "7a697b4eb979f1e6349bc79f4d2ed0d3994de51dfed777a71fb04740819eeabf"}
    experimental_model
    LPS-stimulated macrophage experiments
    exposure
    Dose-dependent nasunin treatment; exact dose/time not reported in indexed abstract
    limitations
    These measurements do not prove direct binding to Akt, p38, NF-kappa-B or NOS2; reduced NOS2 expression is not direct enzyme inhibition. Response is LPS/cell-context dependent.
    nutrient_topic
    Nasunin research collection; topical membership is not evidence of a direct dietary effect. · Nasunin
    organism
    Mouse RAW264 macrophages
    plain_language
    The inhibitory control protein was better retained.
    primary_references
    [nasunin-p28812425] Nasunin inhibits the lipopolysaccharide-induced pro-inflammatory mediator production in RAW264 mouse macrophages by suppressing ROS-mediated activation of PI3 K/Akt/NF-κB and p38 signaling pathways. (2017). https://pubmed.ncbi.nlm.nih.gov/28812425/ DOI: 10.1080/09168451.2017.1362973
    tissue_or_cell_type
    Inflammatory mediator secretion and signaling

    Nasunin: identity, redox chemistry and nutrient connections (2026-09-17) · lines 250–261

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · LPS-stimulated macrophage experiments · source_derived_draft · unverified_draft

    ### nasunin-ikba-preservation Nasunin suppressed stimulus-associated I-kappa-B-alpha degradation. Condition category: normal nutrient_topic: Nasunin research collection; topical membership is not evidence of a direct dietary effect. plain_language: The inhibitory control protein was better retained. organism: Mouse RAW264 macrophages tissue_or_cell_type: Inflammatory mediator secretion and signaling experimental_model: LPS-stimulated macrophage experiments limitations: These measurements do not prove direct binding to Akt, p38, NF-kappa-B or NOS2; reduced NOS2 expression is not direct enzyme inhibition. Response is LPS/cell-context dependent. exposure: Dose-dependent nasunin treatment; exact dose/time not reported in indexed abstract evidence_span: {"source_cache": "artifacts/nasunin-research/28812425.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "7a697b4eb979f1e6349bc79f4d2ed0d3994de51dfed777a71fb04740819eeabf", "start_char": 0, "end_char": 1094, "text_sha256": "7a697b4eb979f1e6349bc79f4d2ed0d3994de51dfed777a71fb04740819eeabf"} [nasunin-p28812425] Nasunin inhibits the lipopolysaccharide-induced pro-inflammatory mediator production in RAW264 mouse macrophages by suppressing ROS-mediated activation of PI3 K/Akt/NF-κB and p38 signaling pathways. (2017). https://pubmed.ncbi.nlm.nih.gov/28812425/ DOI: 10.1080/09168451.2017.1362973
    Complete structured claim and evidence

  4. Nasunin reduced LPS-induced IL-6 secretion.

    Nasunin → Mouse interleukin-6 / Il6 source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/nasunin-research/28812425.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "7a697b4eb979f1e6349bc79f4d2ed0d3994de51dfed777a71fb04740819eeabf", "start_char": 0, "end_char": 1094, "text_sha256": "7a697b4eb979f1e6349bc79f4d2ed0d3994de51dfed777a71fb04740819eeabf"}
    experimental_model
    LPS-stimulated macrophage experiments
    exposure
    Dose-dependent nasunin treatment; exact dose/time not reported in indexed abstract
    limitations
    These measurements do not prove direct binding to Akt, p38, NF-kappa-B or NOS2; reduced NOS2 expression is not direct enzyme inhibition. Response is LPS/cell-context dependent.
    nutrient_topic
    Nasunin research collection; topical membership is not evidence of a direct dietary effect. · Nasunin
    organism
    Mouse RAW264 macrophages
    plain_language
    A second messenger decreased.
    primary_references
    [nasunin-p28812425] Nasunin inhibits the lipopolysaccharide-induced pro-inflammatory mediator production in RAW264 mouse macrophages by suppressing ROS-mediated activation of PI3 K/Akt/NF-κB and p38 signaling pathways. (2017). https://pubmed.ncbi.nlm.nih.gov/28812425/ DOI: 10.1080/09168451.2017.1362973
    tissue_or_cell_type
    Inflammatory mediator secretion and signaling

    Nasunin: identity, redox chemistry and nutrient connections (2026-09-17) · lines 211–222

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · LPS-stimulated macrophage experiments · source_derived_draft · unverified_draft

    ### nasunin-il6-release Nasunin reduced LPS-induced IL-6 secretion. Condition category: normal nutrient_topic: Nasunin research collection; topical membership is not evidence of a direct dietary effect. plain_language: A second messenger decreased. organism: Mouse RAW264 macrophages tissue_or_cell_type: Inflammatory mediator secretion and signaling experimental_model: LPS-stimulated macrophage experiments limitations: These measurements do not prove direct binding to Akt, p38, NF-kappa-B or NOS2; reduced NOS2 expression is not direct enzyme inhibition. Response is LPS/cell-context dependent. exposure: Dose-dependent nasunin treatment; exact dose/time not reported in indexed abstract evidence_span: {"source_cache": "artifacts/nasunin-research/28812425.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "7a697b4eb979f1e6349bc79f4d2ed0d3994de51dfed777a71fb04740819eeabf", "start_char": 0, "end_char": 1094, "text_sha256": "7a697b4eb979f1e6349bc79f4d2ed0d3994de51dfed777a71fb04740819eeabf"} [nasunin-p28812425] Nasunin inhibits the lipopolysaccharide-induced pro-inflammatory mediator production in RAW264 mouse macrophages by suppressing ROS-mediated activation of PI3 K/Akt/NF-κB and p38 signaling pathways. (2017). https://pubmed.ncbi.nlm.nih.gov/28812425/ DOI: 10.1080/09168451.2017.1362973
    Complete structured claim and evidence

  5. Nasunin reduced LPS-associated intracellular ROS accumulation.

    Nasunin → ROS accumulation in RAW264 mouse macrophages source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/nasunin-research/28812425.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "7a697b4eb979f1e6349bc79f4d2ed0d3994de51dfed777a71fb04740819eeabf", "start_char": 0, "end_char": 1094, "text_sha256": "7a697b4eb979f1e6349bc79f4d2ed0d3994de51dfed777a71fb04740819eeabf"}
    experimental_model
    LPS-stimulated macrophage experiments
    exposure
    Dose-dependent nasunin treatment; exact dose/time not reported in indexed abstract
    limitations
    These measurements do not prove direct binding to Akt, p38, NF-kappa-B or NOS2; reduced NOS2 expression is not direct enzyme inhibition. Response is LPS/cell-context dependent.
    nutrient_topic
    Nasunin research collection; topical membership is not evidence of a direct dietary effect. · Nasunin
    organism
    Mouse RAW264 macrophages
    plain_language
    The stimulated immune cells showed a smaller oxidant readout.
    primary_references
    [nasunin-p28812425] Nasunin inhibits the lipopolysaccharide-induced pro-inflammatory mediator production in RAW264 mouse macrophages by suppressing ROS-mediated activation of PI3 K/Akt/NF-κB and p38 signaling pathways. (2017). https://pubmed.ncbi.nlm.nih.gov/28812425/ DOI: 10.1080/09168451.2017.1362973
    tissue_or_cell_type
    Inflammatory mediator secretion and signaling

    Nasunin: identity, redox chemistry and nutrient connections (2026-09-17) · lines 185–196

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · LPS-stimulated macrophage experiments · source_derived_draft · unverified_draft

    ### nasunin-macrophage-ros Nasunin reduced LPS-associated intracellular ROS accumulation. Condition category: normal nutrient_topic: Nasunin research collection; topical membership is not evidence of a direct dietary effect. plain_language: The stimulated immune cells showed a smaller oxidant readout. organism: Mouse RAW264 macrophages tissue_or_cell_type: Inflammatory mediator secretion and signaling experimental_model: LPS-stimulated macrophage experiments limitations: These measurements do not prove direct binding to Akt, p38, NF-kappa-B or NOS2; reduced NOS2 expression is not direct enzyme inhibition. Response is LPS/cell-context dependent. exposure: Dose-dependent nasunin treatment; exact dose/time not reported in indexed abstract evidence_span: {"source_cache": "artifacts/nasunin-research/28812425.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "7a697b4eb979f1e6349bc79f4d2ed0d3994de51dfed777a71fb04740819eeabf", "start_char": 0, "end_char": 1094, "text_sha256": "7a697b4eb979f1e6349bc79f4d2ed0d3994de51dfed777a71fb04740819eeabf"} [nasunin-p28812425] Nasunin inhibits the lipopolysaccharide-induced pro-inflammatory mediator production in RAW264 mouse macrophages by suppressing ROS-mediated activation of PI3 K/Akt/NF-κB and p38 signaling pathways. (2017). https://pubmed.ncbi.nlm.nih.gov/28812425/ DOI: 10.1080/09168451.2017.1362973
    Complete structured claim and evidence

  6. Nasunin reduced LPS-induced nitric-oxide production.

    Nasunin → NO source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/nasunin-research/28812425.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "7a697b4eb979f1e6349bc79f4d2ed0d3994de51dfed777a71fb04740819eeabf", "start_char": 0, "end_char": 1094, "text_sha256": "7a697b4eb979f1e6349bc79f4d2ed0d3994de51dfed777a71fb04740819eeabf"}
    experimental_model
    LPS-stimulated macrophage experiments
    exposure
    Dose-dependent nasunin treatment; exact dose/time not reported in indexed abstract
    limitations
    These measurements do not prove direct binding to Akt, p38, NF-kappa-B or NOS2; reduced NOS2 expression is not direct enzyme inhibition. Response is LPS/cell-context dependent.
    nutrient_topic
    Nasunin research collection; topical membership is not evidence of a direct dietary effect. · Nasunin
    organism
    Mouse RAW264 macrophages
    plain_language
    Output from the stimulated pathway decreased.
    primary_references
    [nasunin-p28812425] Nasunin inhibits the lipopolysaccharide-induced pro-inflammatory mediator production in RAW264 mouse macrophages by suppressing ROS-mediated activation of PI3 K/Akt/NF-κB and p38 signaling pathways. (2017). https://pubmed.ncbi.nlm.nih.gov/28812425/ DOI: 10.1080/09168451.2017.1362973
    tissue_or_cell_type
    Inflammatory mediator secretion and signaling

    Nasunin: identity, redox chemistry and nutrient connections (2026-09-17) · lines 237–248

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · LPS-stimulated macrophage experiments · source_derived_draft · unverified_draft

    ### nasunin-no-output Nasunin reduced LPS-induced nitric-oxide production. Condition category: normal nutrient_topic: Nasunin research collection; topical membership is not evidence of a direct dietary effect. plain_language: Output from the stimulated pathway decreased. organism: Mouse RAW264 macrophages tissue_or_cell_type: Inflammatory mediator secretion and signaling experimental_model: LPS-stimulated macrophage experiments limitations: These measurements do not prove direct binding to Akt, p38, NF-kappa-B or NOS2; reduced NOS2 expression is not direct enzyme inhibition. Response is LPS/cell-context dependent. exposure: Dose-dependent nasunin treatment; exact dose/time not reported in indexed abstract evidence_span: {"source_cache": "artifacts/nasunin-research/28812425.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "7a697b4eb979f1e6349bc79f4d2ed0d3994de51dfed777a71fb04740819eeabf", "start_char": 0, "end_char": 1094, "text_sha256": "7a697b4eb979f1e6349bc79f4d2ed0d3994de51dfed777a71fb04740819eeabf"} [nasunin-p28812425] Nasunin inhibits the lipopolysaccharide-induced pro-inflammatory mediator production in RAW264 mouse macrophages by suppressing ROS-mediated activation of PI3 K/Akt/NF-κB and p38 signaling pathways. (2017). https://pubmed.ncbi.nlm.nih.gov/28812425/ DOI: 10.1080/09168451.2017.1362973
    Complete structured claim and evidence

  7. Nasunin reduced induced NOS2 expression.

    Nasunin → Mouse inducible nitric oxide synthase / Nos2 source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/nasunin-research/28812425.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "7a697b4eb979f1e6349bc79f4d2ed0d3994de51dfed777a71fb04740819eeabf", "start_char": 0, "end_char": 1094, "text_sha256": "7a697b4eb979f1e6349bc79f4d2ed0d3994de51dfed777a71fb04740819eeabf"}
    experimental_model
    LPS-stimulated macrophage experiments
    exposure
    Dose-dependent nasunin treatment; exact dose/time not reported in indexed abstract
    limitations
    These measurements do not prove direct binding to Akt, p38, NF-kappa-B or NOS2; reduced NOS2 expression is not direct enzyme inhibition. Response is LPS/cell-context dependent.
    nutrient_topic
    Nasunin research collection; topical membership is not evidence of a direct dietary effect. · Nasunin
    organism
    Mouse RAW264 macrophages
    plain_language
    Less of the inducible nitric-oxide enzyme was measured.
    primary_references
    [nasunin-p28812425] Nasunin inhibits the lipopolysaccharide-induced pro-inflammatory mediator production in RAW264 mouse macrophages by suppressing ROS-mediated activation of PI3 K/Akt/NF-κB and p38 signaling pathways. (2017). https://pubmed.ncbi.nlm.nih.gov/28812425/ DOI: 10.1080/09168451.2017.1362973
    tissue_or_cell_type
    Inflammatory mediator secretion and signaling

    Nasunin: identity, redox chemistry and nutrient connections (2026-09-17) · lines 224–235

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · LPS-stimulated macrophage experiments · source_derived_draft · unverified_draft

    ### nasunin-nos2-expression Nasunin reduced induced NOS2 expression. Condition category: normal nutrient_topic: Nasunin research collection; topical membership is not evidence of a direct dietary effect. plain_language: Less of the inducible nitric-oxide enzyme was measured. organism: Mouse RAW264 macrophages tissue_or_cell_type: Inflammatory mediator secretion and signaling experimental_model: LPS-stimulated macrophage experiments limitations: These measurements do not prove direct binding to Akt, p38, NF-kappa-B or NOS2; reduced NOS2 expression is not direct enzyme inhibition. Response is LPS/cell-context dependent. exposure: Dose-dependent nasunin treatment; exact dose/time not reported in indexed abstract evidence_span: {"source_cache": "artifacts/nasunin-research/28812425.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "7a697b4eb979f1e6349bc79f4d2ed0d3994de51dfed777a71fb04740819eeabf", "start_char": 0, "end_char": 1094, "text_sha256": "7a697b4eb979f1e6349bc79f4d2ed0d3994de51dfed777a71fb04740819eeabf"} [nasunin-p28812425] Nasunin inhibits the lipopolysaccharide-induced pro-inflammatory mediator production in RAW264 mouse macrophages by suppressing ROS-mediated activation of PI3 K/Akt/NF-κB and p38 signaling pathways. (2017). https://pubmed.ncbi.nlm.nih.gov/28812425/ DOI: 10.1080/09168451.2017.1362973
    Complete structured claim and evidence

  8. Nasunin attenuated p38 phosphorylation in stimulated RAW264 cells.

    Nasunin → Mouse p38 MAP kinase family, isoform unresolved source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/nasunin-research/28812425.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "7a697b4eb979f1e6349bc79f4d2ed0d3994de51dfed777a71fb04740819eeabf", "start_char": 0, "end_char": 1094, "text_sha256": "7a697b4eb979f1e6349bc79f4d2ed0d3994de51dfed777a71fb04740819eeabf"}
    experimental_model
    LPS-stimulated macrophage experiments
    exposure
    Dose-dependent nasunin treatment; exact dose/time not reported in indexed abstract
    limitations
    These measurements do not prove direct binding to Akt, p38, NF-kappa-B or NOS2; reduced NOS2 expression is not direct enzyme inhibition. Response is LPS/cell-context dependent.
    nutrient_topic
    Nasunin research collection; topical membership is not evidence of a direct dietary effect. · Nasunin
    organism
    Mouse RAW264 macrophages
    plain_language
    A separate kinase response also decreased.
    primary_references
    [nasunin-p28812425] Nasunin inhibits the lipopolysaccharide-induced pro-inflammatory mediator production in RAW264 mouse macrophages by suppressing ROS-mediated activation of PI3 K/Akt/NF-κB and p38 signaling pathways. (2017). https://pubmed.ncbi.nlm.nih.gov/28812425/ DOI: 10.1080/09168451.2017.1362973
    tissue_or_cell_type
    Inflammatory mediator secretion and signaling

    Nasunin: identity, redox chemistry and nutrient connections (2026-09-17) · lines 289–300

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · LPS-stimulated macrophage experiments · source_derived_draft · unverified_draft

    ### nasunin-p38-macrophage Nasunin attenuated p38 phosphorylation in stimulated RAW264 cells. Condition category: normal nutrient_topic: Nasunin research collection; topical membership is not evidence of a direct dietary effect. plain_language: A separate kinase response also decreased. organism: Mouse RAW264 macrophages tissue_or_cell_type: Inflammatory mediator secretion and signaling experimental_model: LPS-stimulated macrophage experiments limitations: These measurements do not prove direct binding to Akt, p38, NF-kappa-B or NOS2; reduced NOS2 expression is not direct enzyme inhibition. Response is LPS/cell-context dependent. exposure: Dose-dependent nasunin treatment; exact dose/time not reported in indexed abstract evidence_span: {"source_cache": "artifacts/nasunin-research/28812425.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "7a697b4eb979f1e6349bc79f4d2ed0d3994de51dfed777a71fb04740819eeabf", "start_char": 0, "end_char": 1094, "text_sha256": "7a697b4eb979f1e6349bc79f4d2ed0d3994de51dfed777a71fb04740819eeabf"} [nasunin-p28812425] Nasunin inhibits the lipopolysaccharide-induced pro-inflammatory mediator production in RAW264 mouse macrophages by suppressing ROS-mediated activation of PI3 K/Akt/NF-κB and p38 signaling pathways. (2017). https://pubmed.ncbi.nlm.nih.gov/28812425/ DOI: 10.1080/09168451.2017.1362973
    Complete structured claim and evidence

  9. Nasunin reduced p65 nuclear translocation.

    Nasunin → Mouse NF-kappa-B p65 / Rela source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/nasunin-research/28812425.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "7a697b4eb979f1e6349bc79f4d2ed0d3994de51dfed777a71fb04740819eeabf", "start_char": 0, "end_char": 1094, "text_sha256": "7a697b4eb979f1e6349bc79f4d2ed0d3994de51dfed777a71fb04740819eeabf"}
    experimental_model
    LPS-stimulated macrophage experiments
    exposure
    Dose-dependent nasunin treatment; exact dose/time not reported in indexed abstract
    limitations
    These measurements do not prove direct binding to Akt, p38, NF-kappa-B or NOS2; reduced NOS2 expression is not direct enzyme inhibition. Response is LPS/cell-context dependent.
    nutrient_topic
    Nasunin research collection; topical membership is not evidence of a direct dietary effect. · Nasunin
    organism
    Mouse RAW264 macrophages
    plain_language
    Less of this regulator moved into the nucleus.
    primary_references
    [nasunin-p28812425] Nasunin inhibits the lipopolysaccharide-induced pro-inflammatory mediator production in RAW264 mouse macrophages by suppressing ROS-mediated activation of PI3 K/Akt/NF-κB and p38 signaling pathways. (2017). https://pubmed.ncbi.nlm.nih.gov/28812425/ DOI: 10.1080/09168451.2017.1362973
    tissue_or_cell_type
    Inflammatory mediator secretion and signaling

    Nasunin: identity, redox chemistry and nutrient connections (2026-09-17) · lines 263–274

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · LPS-stimulated macrophage experiments · source_derived_draft · unverified_draft

    ### nasunin-p65-localization Nasunin reduced p65 nuclear translocation. Condition category: normal nutrient_topic: Nasunin research collection; topical membership is not evidence of a direct dietary effect. plain_language: Less of this regulator moved into the nucleus. organism: Mouse RAW264 macrophages tissue_or_cell_type: Inflammatory mediator secretion and signaling experimental_model: LPS-stimulated macrophage experiments limitations: These measurements do not prove direct binding to Akt, p38, NF-kappa-B or NOS2; reduced NOS2 expression is not direct enzyme inhibition. Response is LPS/cell-context dependent. exposure: Dose-dependent nasunin treatment; exact dose/time not reported in indexed abstract evidence_span: {"source_cache": "artifacts/nasunin-research/28812425.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "7a697b4eb979f1e6349bc79f4d2ed0d3994de51dfed777a71fb04740819eeabf", "start_char": 0, "end_char": 1094, "text_sha256": "7a697b4eb979f1e6349bc79f4d2ed0d3994de51dfed777a71fb04740819eeabf"} [nasunin-p28812425] Nasunin inhibits the lipopolysaccharide-induced pro-inflammatory mediator production in RAW264 mouse macrophages by suppressing ROS-mediated activation of PI3 K/Akt/NF-κB and p38 signaling pathways. (2017). https://pubmed.ncbi.nlm.nih.gov/28812425/ DOI: 10.1080/09168451.2017.1362973
    Complete structured claim and evidence

  10. Nasunin reduced LPS-induced TNF-alpha secretion.

    Nasunin → Mouse tumor necrosis factor / Tnf source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/nasunin-research/28812425.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "7a697b4eb979f1e6349bc79f4d2ed0d3994de51dfed777a71fb04740819eeabf", "start_char": 0, "end_char": 1094, "text_sha256": "7a697b4eb979f1e6349bc79f4d2ed0d3994de51dfed777a71fb04740819eeabf"}
    experimental_model
    LPS-stimulated macrophage experiments
    exposure
    Dose-dependent nasunin treatment; exact dose/time not reported in indexed abstract
    limitations
    These measurements do not prove direct binding to Akt, p38, NF-kappa-B or NOS2; reduced NOS2 expression is not direct enzyme inhibition. Response is LPS/cell-context dependent.
    nutrient_topic
    Nasunin research collection; topical membership is not evidence of a direct dietary effect. · Nasunin
    organism
    Mouse RAW264 macrophages
    plain_language
    One inflammatory messenger decreased.
    primary_references
    [nasunin-p28812425] Nasunin inhibits the lipopolysaccharide-induced pro-inflammatory mediator production in RAW264 mouse macrophages by suppressing ROS-mediated activation of PI3 K/Akt/NF-κB and p38 signaling pathways. (2017). https://pubmed.ncbi.nlm.nih.gov/28812425/ DOI: 10.1080/09168451.2017.1362973
    tissue_or_cell_type
    Inflammatory mediator secretion and signaling

    Nasunin: identity, redox chemistry and nutrient connections (2026-09-17) · lines 198–209

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · LPS-stimulated macrophage experiments · source_derived_draft · unverified_draft

    ### nasunin-tnf-release Nasunin reduced LPS-induced TNF-alpha secretion. Condition category: normal nutrient_topic: Nasunin research collection; topical membership is not evidence of a direct dietary effect. plain_language: One inflammatory messenger decreased. organism: Mouse RAW264 macrophages tissue_or_cell_type: Inflammatory mediator secretion and signaling experimental_model: LPS-stimulated macrophage experiments limitations: These measurements do not prove direct binding to Akt, p38, NF-kappa-B or NOS2; reduced NOS2 expression is not direct enzyme inhibition. Response is LPS/cell-context dependent. exposure: Dose-dependent nasunin treatment; exact dose/time not reported in indexed abstract evidence_span: {"source_cache": "artifacts/nasunin-research/28812425.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "7a697b4eb979f1e6349bc79f4d2ed0d3994de51dfed777a71fb04740819eeabf", "start_char": 0, "end_char": 1094, "text_sha256": "7a697b4eb979f1e6349bc79f4d2ed0d3994de51dfed777a71fb04740819eeabf"} [nasunin-p28812425] Nasunin inhibits the lipopolysaccharide-induced pro-inflammatory mediator production in RAW264 mouse macrophages by suppressing ROS-mediated activation of PI3 K/Akt/NF-κB and p38 signaling pathways. (2017). https://pubmed.ncbi.nlm.nih.gov/28812425/ DOI: 10.1080/09168451.2017.1362973
    Complete structured claim and evidence

  11. Tollip silencing impaired EGCG inhibition of TLR4 signaling.

    Toll-interacting protein family / Tollip → TLR4 downstream inflammatory signaling source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    experimental_model
    Macrophage LPS-response experiments, EGCG 1 micromolar; organism not assigned from abstract.
    limitations
    Family nodes preserve the unresolved species. This is not evidence of treating systemic human inflammation.
    nutrient_topic
    EGCG collection; comparator and shared-pathway records retain their actual intervention. · Epigallocatechin-3-gallate (EGCG)
    plain_language
    The anti-inflammatory response depended on Tollip.
    primary_references
    TLR4 signaling inhibitory pathway induced by green tea polyphenol epigallocatechin-3-gallate through 67-kDa laminin receptor. · 2010 · https://pubmed.ncbi.nlm.nih.gov/20511545/ · DOI 10.4049/jimmunol.0903742
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18) · lines 116–122

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Macrophage LPS-response experiments, EGCG 1 micromolar; organism not assigned from abstract. · source_derived_draft · unverified_draft

    ## egcg-tollip-gate The anti-inflammatory response depended on Tollip. Tollip silencing impaired EGCG inhibition of TLR4 signaling. Model: Macrophage LPS-response experiments, EGCG 1 micromolar; organism not assigned from abstract. Limitations: Family nodes preserve the unresolved species. This is not evidence of treating systemic human inflammation. Evidence access: primary abstract. TLR4 signaling inhibitory pathway induced by green tea polyphenol epigallocatechin-3-gallate through 67-kDa laminin receptor. · 2010 · https://pubmed.ncbi.nlm.nih.gov/20511545/ · DOI 10.4049/jimmunol.0903742
    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