Component

Myosin light-chain phosphorylation in human Caco-2 cells

Myosin light-chain phosphorylation in human Caco-2 cells. Interpret through the linked experimental species, preparation, compartment and exposure; no universal causal effect is implied.

2 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. The active glucoside reduced TNF-triggered downstream myosin-light-chain phosphorylation in the barrier experiment.

    Cyanidin 3-O-beta-D-glucopyranoside → Myosin light-chain phosphorylation in human Caco-2 cells source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Full text retrieved; relevant methods/results/figure text reviewed. No independent raw-data verification.
    experimental_condition
    TNF alone present · Tumor necrosis factor Condition belongs to the full experimental contrast; do not separate a joint intervention.
    experimental_condition
    TNF alone present · Cyanidin 3-O-beta-D-glucopyranoside Condition belongs to the full experimental contrast; do not separate a joint intervention.
    experimental_contrast
    {"intervention": "cyanidin-3-glucoside plus TNF", "comparator": "TNF alone", "endpoint": "The active glucoside reduced TNF-triggered downstream myosin-light-chain phosphorylation in the barrier experiment.", "effect_direction": "decrease", "combination": "joint", "conditions": [{"entity_slug": "cyanidin-3-glucoside", "state": "present"}, {"entity_slug": "tnf", "state": "present"}]} Explicit extracted experimental comparison; source-derived draft.
    experimental_model
    Human Caco-2 monolayers; 0.25-1 uM glucosides; NF-kappa-B and MLC signaling studied.
    interpretation_status
    Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.
    limitations
    Pathway evidence in cultured intestinal epithelium, not systemic NF-kappa-B suppression.
    plain_language
    The active glucoside reduced TNF-triggered downstream myosin-light-chain phosphorylation in the barrier experiment.
    primary_references
    Anthocyanins inhibit tumor necrosis alpha-induced loss of Caco-2 cell barrier integrity. | 2017 | DOI 10.1039/c7fo00625j | PMID 28740990 | https://pubmed.ncbi.nlm.nih.gov/28740990/ | https://doi.org/10.1039/c7fo00625j | https://pubs.rsc.org/en/content/articlehtml/2017/fo/c7fo00625j
    source_locator
    Reviewed reference lines 78-78; exact primary location described in quoted passage where extracted.

    Anthocyanins: detailed mechanisms of action (reviewed 4 October 2026) · lines 78–78

    Original AI-assisted review of primary studies and, where relevant, official regulatory records. Access level is retained per claim. Corrections, null results and unresolved questions remain explicit. Not publisher full text or independent replication. · supports · Human Caco-2 monolayers; 0.25-1 uM glucosides; NF-kappa-B and MLC signaling studied. · source_derived_draft · unverified_draft

    **Barrier protection is compound-selective.** In TNF-challenged human Caco-2 monolayers, cyanidin and delphinidin O-glucosides at 0.25–1 µM limited the fall in electrical resistance and rise in FITC-dextran permeability. Tested malvidin, peonidin and petunidin glucosides did not provide the same protection. NF-κB activation and downstream myosin-light-chain phosphorylation were reduced by the active compounds. This experiment measured functional permeability, not just more ZO-1 or occludin. It does not establish a clinical treatment for intestinal disease or a universal anthocyanin effect. [Cremonini et al., 2017](https://pubs.rsc.org/en/content/articlehtml/2017/fo/c7fo00625j).
    Complete structured claim and evidence

  2. The active glucoside reduced TNF-triggered downstream myosin-light-chain phosphorylation in the barrier experiment.

    Delphinidin 3-O-beta-D-glucopyranoside → Myosin light-chain phosphorylation in human Caco-2 cells source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Full text retrieved; relevant methods/results/figure text reviewed. No independent raw-data verification.
    experimental_condition
    TNF alone present · Delphinidin 3-O-beta-D-glucopyranoside Condition belongs to the full experimental contrast; do not separate a joint intervention.
    experimental_condition
    TNF alone present · Tumor necrosis factor Condition belongs to the full experimental contrast; do not separate a joint intervention.
    experimental_contrast
    {"intervention": "delphinidin-3-glucoside plus TNF", "comparator": "TNF alone", "endpoint": "The active glucoside reduced TNF-triggered downstream myosin-light-chain phosphorylation in the barrier experiment.", "effect_direction": "decrease", "combination": "joint", "conditions": [{"entity_slug": "delphinidin-3-glucoside", "state": "present"}, {"entity_slug": "tnf", "state": "present"}]} Explicit extracted experimental comparison; source-derived draft.
    experimental_model
    Human Caco-2 monolayers; 0.25-1 uM glucosides; NF-kappa-B and MLC signaling studied.
    interpretation_status
    Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.
    limitations
    Pathway evidence in cultured intestinal epithelium, not systemic NF-kappa-B suppression.
    plain_language
    The active glucoside reduced TNF-triggered downstream myosin-light-chain phosphorylation in the barrier experiment.
    primary_references
    Anthocyanins inhibit tumor necrosis alpha-induced loss of Caco-2 cell barrier integrity. | 2017 | DOI 10.1039/c7fo00625j | PMID 28740990 | https://pubmed.ncbi.nlm.nih.gov/28740990/ | https://doi.org/10.1039/c7fo00625j | https://pubs.rsc.org/en/content/articlehtml/2017/fo/c7fo00625j
    source_locator
    Reviewed reference lines 78-78; exact primary location described in quoted passage where extracted.

    Anthocyanins: detailed mechanisms of action (reviewed 4 October 2026) · lines 78–78

    Original AI-assisted review of primary studies and, where relevant, official regulatory records. Access level is retained per claim. Corrections, null results and unresolved questions remain explicit. Not publisher full text or independent replication. · supports · Human Caco-2 monolayers; 0.25-1 uM glucosides; NF-kappa-B and MLC signaling studied. · source_derived_draft · unverified_draft

    **Barrier protection is compound-selective.** In TNF-challenged human Caco-2 monolayers, cyanidin and delphinidin O-glucosides at 0.25–1 µM limited the fall in electrical resistance and rise in FITC-dextran permeability. Tested malvidin, peonidin and petunidin glucosides did not provide the same protection. NF-κB activation and downstream myosin-light-chain phosphorylation were reduced by the active compounds. This experiment measured functional permeability, not just more ZO-1 or occludin. It does not establish a clinical treatment for intestinal disease or a universal anthocyanin effect. [Cremonini et al., 2017](https://pubs.rsc.org/en/content/articlehtml/2017/fo/c7fo00625j).
    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.