Component

Protein kinase C alpha (PRKCA)

Human PKC alpha used as a recombinant HIS-tagged enzyme in direct tocopherol assays.

6 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. RRR-alpha-tocopherol at 0.1–10 µM inhibited cofactor-dependent recombinant human PKC alpha activity in phosphatidylserine-containing assays.

    RRR-alpha-tocopherol → Protein kinase C alpha (PRKCA) source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    true
    experimental_model
    Recombinant HIS-tagged human PKC alpha biochemical assay
    exposure
    15 ng PKC alpha; 2 mM CaCl2; phosphatidylserine 15–60 µg/mL; 5 min pretreatment, 30 min kinase assay.
    limitations
    Effect depends on reconstituted lipid composition and activation mode; it is not a clinical dosing claim.
    nutrient_topic
    Vitamin E research collection; topical membership is not evidence of a direct dietary effect. · Vitamin E
    organism
    Homo sapiens
    plain_language
    Natural alpha-tocopherol reduced PKC alpha activity in a purified system containing its lipid and calcium cofactors.
    primary_references
    [mccary2012] Vitamin E isoforms directly bind PKCα and differentially regulate activation of PKCα. (2012). https://pubmed.ncbi.nlm.nih.gov/21933153/ DOI: 10.1042/bj20111318
    tissue_or_cell_type
    Cell-free enzyme

    Vitamin E: transport, membrane protection and nutrient interactions (2026-09-17) · lines 933–944

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant HIS-tagged human PKC alpha biochemical assay · source_derived_draft · unverified_draft

    ### e-sig-alpha-pkc-cofactor RRR-alpha-tocopherol at 0.1–10 µM inhibited cofactor-dependent recombinant human PKC alpha activity in phosphatidylserine-containing assays. Condition category: normal nutrient_topic: Vitamin E research collection; topical membership is not evidence of a direct dietary effect. plain_language: Natural alpha-tocopherol reduced PKC alpha activity in a purified system containing its lipid and calcium cofactors. organism: Homo sapiens tissue_or_cell_type: Cell-free enzyme experimental_model: Recombinant HIS-tagged human PKC alpha biochemical assay limitations: Effect depends on reconstituted lipid composition and activation mode; it is not a clinical dosing claim. exposure: 15 ng PKC alpha; 2 mM CaCl2; phosphatidylserine 15–60 µg/mL; 5 min pretreatment, 30 min kinase assay. cross_nutrient: true [mccary2012] Vitamin E isoforms directly bind PKCα and differentially regulate activation of PKCα. (2012). https://pubmed.ncbi.nlm.nih.gov/21933153/ DOI: 10.1042/bj20111318
    Complete structured claim and evidence

  2. RRR-alpha-tocopherol at 0.01 µM inhibited peroxide/iron-induced activation of recombinant PKC alpha; gamma-tocopherol required 0.1 µM for significant inhibition in the same assay.

    RRR-alpha-tocopherol → Protein kinase C alpha (PRKCA) source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    true
    experimental_model
    Recombinant HIS-tagged human PKC alpha biochemical assay with iron and peroxide
    exposure
    15 ng dialyzed PKC alpha; 45 µM FeCl2; 1 or 10 mM H2O2 activation for 2 min, stopped with 9 mM DTT; no PS or calcium cofactors.
    limitations
    Millimolar peroxide in a cell-free reaction is not normal intracellular exposure. This is distinct from cofactor-dependent gamma activation.
    nutrient_topic
    Vitamin E research collection; topical membership is not evidence of a direct dietary effect. · Vitamin E
    organism
    Homo sapiens
    plain_language
    Both natural tocopherols reduced oxidative activation of this kinase, with alpha active at a lower tested concentration.
    primary_references
    [mccary2012] Vitamin E isoforms directly bind PKCα and differentially regulate activation of PKCα. (2012). https://pubmed.ncbi.nlm.nih.gov/21933153/ DOI: 10.1042/bj20111318
    tissue_or_cell_type
    Cell-free enzyme

    Vitamin E: transport, membrane protection and nutrient interactions (2026-09-17) · lines 959–970

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant HIS-tagged human PKC alpha biochemical assay with iron and peroxide · source_derived_draft · unverified_draft

    ### e-sig-alpha-pkc-oxidative RRR-alpha-tocopherol at 0.01 µM inhibited peroxide/iron-induced activation of recombinant PKC alpha; gamma-tocopherol required 0.1 µM for significant inhibition in the same assay. Condition category: normal nutrient_topic: Vitamin E research collection; topical membership is not evidence of a direct dietary effect. plain_language: Both natural tocopherols reduced oxidative activation of this kinase, with alpha active at a lower tested concentration. organism: Homo sapiens tissue_or_cell_type: Cell-free enzyme experimental_model: Recombinant HIS-tagged human PKC alpha biochemical assay with iron and peroxide limitations: Millimolar peroxide in a cell-free reaction is not normal intracellular exposure. This is distinct from cofactor-dependent gamma activation. exposure: 15 ng dialyzed PKC alpha; 45 µM FeCl2; 1 or 10 mM H2O2 activation for 2 min, stopped with 9 mM DTT; no PS or calcium cofactors. cross_nutrient: true [mccary2012] Vitamin E isoforms directly bind PKCα and differentially regulate activation of PKCα. (2012). https://pubmed.ncbi.nlm.nih.gov/21933153/ DOI: 10.1042/bj20111318
    Complete structured claim and evidence

  3. RRR-gamma-tocopherol at 1 µM increased recombinant human PKC alpha activity with 15–30 µg/mL phosphatidylserine and calcium; it did not increase the low activity in the absence of phosphatidylserine.

    RRR-gamma-tocopherol → Protein kinase C alpha (PRKCA) source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    true
    experimental_model
    Recombinant HIS-tagged human PKC alpha biochemical assay
    exposure
    1 µM gamma-tocopherol; 2 mM CaCl2; 15–30 µg/mL phosphatidylserine; 5 min pretreatment, 30 min kinase assay.
    limitations
    Small biochemical activation is not equivalent to uniformly increased inflammation in people; oxidative activation shows a different response.
    nutrient_topic
    Vitamin E research collection; topical membership is not evidence of a direct dietary effect. · Vitamin E
    organism
    Homo sapiens
    plain_language
    Natural gamma-tocopherol increased this kinase’s activity only when the required lipid cofactor was present.
    primary_references
    [mccary2012] Vitamin E isoforms directly bind PKCα and differentially regulate activation of PKCα. (2012). https://pubmed.ncbi.nlm.nih.gov/21933153/ DOI: 10.1042/bj20111318
    tissue_or_cell_type
    Cell-free enzyme

    Vitamin E: transport, membrane protection and nutrient interactions (2026-09-17) · lines 946–957

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant HIS-tagged human PKC alpha biochemical assay · source_derived_draft · unverified_draft

    ### e-sig-gamma-pkc-cofactor RRR-gamma-tocopherol at 1 µM increased recombinant human PKC alpha activity with 15–30 µg/mL phosphatidylserine and calcium; it did not increase the low activity in the absence of phosphatidylserine. Condition category: normal nutrient_topic: Vitamin E research collection; topical membership is not evidence of a direct dietary effect. plain_language: Natural gamma-tocopherol increased this kinase’s activity only when the required lipid cofactor was present. organism: Homo sapiens tissue_or_cell_type: Cell-free enzyme experimental_model: Recombinant HIS-tagged human PKC alpha biochemical assay limitations: Small biochemical activation is not equivalent to uniformly increased inflammation in people; oxidative activation shows a different response. exposure: 1 µM gamma-tocopherol; 2 mM CaCl2; 15–30 µg/mL phosphatidylserine; 5 min pretreatment, 30 min kinase assay. cross_nutrient: true [mccary2012] Vitamin E isoforms directly bind PKCα and differentially regulate activation of PKCα. (2012). https://pubmed.ncbi.nlm.nih.gov/21933153/ DOI: 10.1042/bj20111318
    Complete structured claim and evidence

  4. NBD-alpha-tocopherol bound recombinant human PKC alpha in solution: fluorescence increased at 1 µM probe, and 5 µM was used in competition assays with 0.1 µM enzyme.

    NBD-alpha-tocopherol → Protein kinase C alpha (PRKCA) source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    false
    experimental_model
    Fluorescence ligand binding in solution
    exposure
    0.1 µM PKC alpha; 1–5 µM NBD-alpha-tocopherol; 30 min at room temperature; 1% ethanol buffer.
    limitations
    The fluorophore reports a hydrophobic environment. Competition controls support specific binding, but the labeled probe is distinct from native tocopherol.
    nutrient_topic
    Vitamin E research collection; topical membership is not evidence of a direct dietary effect. · Vitamin E
    organism
    Homo sapiens
    plain_language
    A fluorescently tagged vitamin E probe associated directly with purified PKC alpha.
    primary_references
    [mccary2012] Vitamin E isoforms directly bind PKCα and differentially regulate activation of PKCα. (2012). https://pubmed.ncbi.nlm.nih.gov/21933153/ DOI: 10.1042/bj20111318
    tissue_or_cell_type
    Cell-free enzyme

    Vitamin E: transport, membrane protection and nutrient interactions (2026-09-17) · lines 972–983

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Fluorescence ligand binding in solution · source_derived_draft · unverified_draft

    ### e-sig-nbd-pkc-binding NBD-alpha-tocopherol bound recombinant human PKC alpha in solution: fluorescence increased at 1 µM probe, and 5 µM was used in competition assays with 0.1 µM enzyme. Condition category: normal nutrient_topic: Vitamin E research collection; topical membership is not evidence of a direct dietary effect. plain_language: A fluorescently tagged vitamin E probe associated directly with purified PKC alpha. organism: Homo sapiens tissue_or_cell_type: Cell-free enzyme experimental_model: Fluorescence ligand binding in solution limitations: The fluorophore reports a hydrophobic environment. Competition controls support specific binding, but the labeled probe is distinct from native tocopherol. exposure: 0.1 µM PKC alpha; 1–5 µM NBD-alpha-tocopherol; 30 min at room temperature; 1% ethanol buffer. cross_nutrient: false [mccary2012] Vitamin E isoforms directly bind PKCα and differentially regulate activation of PKCα. (2012). https://pubmed.ncbi.nlm.nih.gov/21933153/ DOI: 10.1042/bj20111318
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Berberine decreased forskolin-stimulated chloride secretion in T84 monolayers through a predominantly PKC-alpha-dependent pathway.

    Berberine → Colonic epithelial chloride secretion source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/berberine-research/21747769.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "b8864a2844ea828aeabcfc05219050ac1cb6efe7f24c663dc3302887f7f59ad4", "start_char": 0, "end_char": 1734, "text_sha256": "b8864a2844ea828aeabcfc05219050ac1cb6efe7f24c663dc3302887f7f59ad4"}
    experimental_model
    Ussing-chamber short-circuit current, patch clamp and kinase perturbation
    exposure
    Forskolin-stimulated secretion and berberine; IC50 about 80 micromolar
    limitations
    Intestinal cell mechanism, not proof of systemic potassium depletion. The observed channel complex differs from cardiac KCNQ1/KCNE1.
    nutrient_topic
    Berberine research collection; topical membership is not evidence of a direct dietary effect. · Berberine
    organism
    Human T84 colonic cells
    plain_language
    The potassium-channel response is connected to movement of a different ion: chloride.
    primary_references
    [berberine-p21747769] Berberine Reduces cAMP-Induced Chloride Secretion in T84 Human Colonic Carcinoma Cells through Inhibition of Basolateral KCNQ1 Channels. (2011). https://pubmed.ncbi.nlm.nih.gov/21747769/ DOI: 10.3389/fphys.2011.00033
    tissue_or_cell_type
    Basolateral potassium recycling and chloride secretion

    Berberine: metabolism, nutrient connections and drug interactions (2026-09-17) · lines 571–582

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Ussing-chamber short-circuit current, patch clamp and kinase perturbation · source_derived_draft · unverified_draft

    ### berberine-chloride-secretion Berberine decreased forskolin-stimulated chloride secretion in T84 monolayers through a predominantly PKC-alpha-dependent pathway. Condition category: normal nutrient_topic: Berberine research collection; topical membership is not evidence of a direct dietary effect. plain_language: The potassium-channel response is connected to movement of a different ion: chloride. organism: Human T84 colonic cells tissue_or_cell_type: Basolateral potassium recycling and chloride secretion experimental_model: Ussing-chamber short-circuit current, patch clamp and kinase perturbation limitations: Intestinal cell mechanism, not proof of systemic potassium depletion. The observed channel complex differs from cardiac KCNQ1/KCNE1. exposure: Forskolin-stimulated secretion and berberine; IC50 about 80 micromolar evidence_span: {"source_cache": "artifacts/berberine-research/21747769.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "b8864a2844ea828aeabcfc05219050ac1cb6efe7f24c663dc3302887f7f59ad4", "start_char": 0, "end_char": 1734, "text_sha256": "b8864a2844ea828aeabcfc05219050ac1cb6efe7f24c663dc3302887f7f59ad4"} [berberine-p21747769] Berberine Reduces cAMP-Induced Chloride Secretion in T84 Human Colonic Carcinoma Cells through Inhibition of Basolateral KCNQ1 Channels. (2011). https://pubmed.ncbi.nlm.nih.gov/21747769/ DOI: 10.3389/fphys.2011.00033
    Complete structured claim and evidence

  2. Retinol competed with 5 µM NBD-alpha-tocopherol for binding to 0.1 µM recombinant PKC alpha, whereas phosphatidylserine and cholesterol did not compete in the same study.

    All-trans-retinol → NBD-alpha-tocopherol binding to PKC alpha source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    true
    experimental_model
    Fluorescence competition assay, Figure 6G
    exposure
    5 µM NBD-alpha-tocopherol; 0.1 µM PKC alpha; retinol concentration series; 30 min at room temperature, 1% ethanol.
    limitations
    Exact retinol axis values were not extracted; this is direct in-vitro competition, not demonstrated competition between dietary vitamins in human tissues.
    nutrient_topic
    Vitamin E research collection; topical membership is not evidence of a direct dietary effect. · Vitamin E
    organism
    Homo sapiens
    plain_language
    Vitamin A alcohol competed with the labeled vitamin E probe for association with this purified kinase.
    primary_references
    [mccary2012] Vitamin E isoforms directly bind PKCα and differentially regulate activation of PKCα. (2012). https://pubmed.ncbi.nlm.nih.gov/21933153/ DOI: 10.1042/bj20111318
    tissue_or_cell_type
    Cell-free enzyme

    Vitamin E: transport, membrane protection and nutrient interactions (2026-09-17) · lines 985–996

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Fluorescence competition assay, Figure 6G · source_derived_draft · unverified_draft

    ### e-sig-retinol-pkc-competition Retinol competed with 5 µM NBD-alpha-tocopherol for binding to 0.1 µM recombinant PKC alpha, whereas phosphatidylserine and cholesterol did not compete in the same study. Condition category: normal nutrient_topic: Vitamin E research collection; topical membership is not evidence of a direct dietary effect. plain_language: Vitamin A alcohol competed with the labeled vitamin E probe for association with this purified kinase. organism: Homo sapiens tissue_or_cell_type: Cell-free enzyme experimental_model: Fluorescence competition assay, Figure 6G limitations: Exact retinol axis values were not extracted; this is direct in-vitro competition, not demonstrated competition between dietary vitamins in human tissues. exposure: 5 µM NBD-alpha-tocopherol; 0.1 µM PKC alpha; retinol concentration series; 30 min at room temperature, 1% ethanol. cross_nutrient: true [mccary2012] Vitamin E isoforms directly bind PKCα and differentially regulate activation of PKCα. (2012). https://pubmed.ncbi.nlm.nih.gov/21933153/ DOI: 10.1042/bj20111318
    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