Component

Human Caco-2 tight-junction assembly after butyrate

Context-specific entity; species, compartment and exposure are stated on each 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. Butyrate increased AMPK activity and accelerated tight-junction assembly in human Caco-2 monolayers; compound C abolished the improvement in electrical resistance.

    Butyrate → Human Caco-2 tight-junction assembly after butyrate source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Human Caco-2 monolayers; calcium-switch and permeability assays.
    limitations
    Compound C is not uniquely specific for AMPK; this is a culture mechanism, not proven treatment of human intestinal permeability.
    nutrient_topic
    Butyrate collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Butyrate
    plain_language
    An energy-sensing pathway contributed to barrier assembly.
    primary_references
    Butyrate enhances the intestinal barrier by facilitating tight junction assembly via activation of AMP-activated protein kinase in Caco-2 cell monolayers. · 2009 · https://pubmed.ncbi.nlm.nih.gov/19625695/ · DOI 10.3945/jn.109.104638

    Butyrate: microbial production, fuel use, signaling and nutrient interactions (2026-09-19) · lines 262–268

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Human Caco-2 monolayers; calcium-switch and permeability assays. · source_derived_draft · unverified_draft

    ## butyrate-tight-junction-ampk An energy-sensing pathway contributed to barrier assembly. Butyrate increased AMPK activity and accelerated tight-junction assembly in human Caco-2 monolayers; compound C abolished the improvement in electrical resistance. Model: Human Caco-2 monolayers; calcium-switch and permeability assays. Limitations: Compound C is not uniquely specific for AMPK; this is a culture mechanism, not proven treatment of human intestinal permeability. Evidence access: Primary abstract Butyrate enhances the intestinal barrier by facilitating tight junction assembly via activation of AMP-activated protein kinase in Caco-2 cell monolayers. · 2009 · https://pubmed.ncbi.nlm.nih.gov/19625695/ · DOI 10.3945/jn.109.104638
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Sodium butyrate reduced MLC2 Ser19 phosphorylation during Caco-2 tight-junction reassembly.

    Butyrate → MLC2 Ser19 phosphorylation in butyrate-exposed Caco-2 cells source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Human Caco-2 phosphorylation measurements.
    limitations
    MLC2 assay identity is retained without guessing the gene isoform from its shorthand name.
    nutrient_topic
    Butyrate collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Butyrate
    plain_language
    The contractile machinery at the cell boundary changed as junctions reformed.
    primary_references
    Sodium Butyrate Promotes Reassembly of Tight Junctions in Caco-2 Monolayers Involving Inhibition of MLCK/MLC2 Pathway and Phosphorylation of PKCβ2. · 2016 · https://pubmed.ncbi.nlm.nih.gov/27735862/ · DOI 10.3390/ijms17101696

    Butyrate: microbial production, fuel use, signaling and nutrient interactions (2026-09-19) · lines 286–292

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Human Caco-2 phosphorylation measurements. · source_derived_draft · unverified_draft

    ## butyrate-mlc2-junction The contractile machinery at the cell boundary changed as junctions reformed. Sodium butyrate reduced MLC2 Ser19 phosphorylation during Caco-2 tight-junction reassembly. Model: Human Caco-2 phosphorylation measurements. Limitations: MLC2 assay identity is retained without guessing the gene isoform from its shorthand name. Evidence access: Primary abstract Sodium Butyrate Promotes Reassembly of Tight Junctions in Caco-2 Monolayers Involving Inhibition of MLCK/MLC2 Pathway and Phosphorylation of PKCβ2. · 2016 · https://pubmed.ncbi.nlm.nih.gov/27735862/ · DOI 10.3390/ijms17101696
    Complete structured claim and evidence

  2. Sodium butyrate increased PKC-beta2 Ser660 phosphorylation; PKC-beta inhibition blocked the promoted junction reassembly.

    Butyrate → Human protein kinase C beta II / PRKCB beta2 isoform source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Human Caco-2 signaling and inhibitor experiments.
    limitations
    Inhibitor sensitivity does not imply direct binding of butyrate to PKC-beta2.
    nutrient_topic
    Butyrate collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Butyrate
    plain_language
    A downstream kinase contributed to rebuilding the junction.
    primary_references
    Sodium Butyrate Promotes Reassembly of Tight Junctions in Caco-2 Monolayers Involving Inhibition of MLCK/MLC2 Pathway and Phosphorylation of PKCβ2. · 2016 · https://pubmed.ncbi.nlm.nih.gov/27735862/ · DOI 10.3390/ijms17101696

    Butyrate: microbial production, fuel use, signaling and nutrient interactions (2026-09-19) · lines 278–284

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Human Caco-2 signaling and inhibitor experiments. · source_derived_draft · unverified_draft

    ## butyrate-pkcb-junction A downstream kinase contributed to rebuilding the junction. Sodium butyrate increased PKC-beta2 Ser660 phosphorylation; PKC-beta inhibition blocked the promoted junction reassembly. Model: Human Caco-2 signaling and inhibitor experiments. Limitations: Inhibitor sensitivity does not imply direct binding of butyrate to PKC-beta2. Evidence access: Primary abstract Sodium Butyrate Promotes Reassembly of Tight Junctions in Caco-2 Monolayers Involving Inhibition of MLCK/MLC2 Pathway and Phosphorylation of PKCβ2. · 2016 · https://pubmed.ncbi.nlm.nih.gov/27735862/ · DOI 10.3390/ijms17101696
    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