Component

Phosphatidylserine

Independent biological entity. Read linked claims for experimental scope and context.

18 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. PTDSS1 variants from Lenz-Majewski syndrome markedly reduced product inhibition by phosphatidylserine and increased phosphatidylserine synthesis in patient fibroblasts.

    Phosphatidylserine → Human phosphatidylserine synthase 1 / PTDSS1 source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_access
    Primary abstract
    experimental_model
    Human genetics and patient fibroblast synthesis assays.
    limitations
    These gain-of-function variants are not serine shortage or proof of an effect from phosphatidylserine supplements.
    nutrient_topic
    L-Serine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Serine
    plain_language
    Failure of a feedback brake can increase lipid production.
    primary_references
    Gain-of-function mutations in the phosphatidylserine synthase 1 (PTDSS1) gene cause Lenz-Majewski syndrome. · 2014 · https://pubmed.ncbi.nlm.nih.gov/24241535/ · DOI 10.1038/ng.2829
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    L-Serine: synthesis, one-carbon metabolism, lipids and cross-nutrient mechanisms (2026-09-19) · lines 262–268

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human genetics and patient fibroblast synthesis assays. · source_derived_draft · unverified_draft

    ## l-serine-pss1-feedback Failure of a feedback brake can increase lipid production. PTDSS1 variants from Lenz-Majewski syndrome markedly reduced product inhibition by phosphatidylserine and increased phosphatidylserine synthesis in patient fibroblasts. Model: Human genetics and patient fibroblast synthesis assays. Limitations: These gain-of-function variants are not serine shortage or proof of an effect from phosphatidylserine supplements. Evidence access: Primary abstract Gain-of-function mutations in the phosphatidylserine synthase 1 (PTDSS1) gene cause Lenz-Majewski syndrome. · 2014 · https://pubmed.ncbi.nlm.nih.gov/24241535/ · DOI 10.1038/ng.2829
    Complete structured claim and evidence

What acts on it

  1. The tested bovine-f2 Gla-domain protein showed calcium-specific contact with negatively charged phospholipid monolayers.

    Bovine prothrombin / F2 → Phosphatidylserine source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/k2-research/9609692.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d29ed548c28e5a8015742351c50aa94c8853d0f1846794964b67a73324c879bd", "start_char": 0, "end_char": 2064, "text_sha256": "d29ed548c28e5a8015742351c50aa94c8853d0f1846794964b67a73324c879bd"}
    experimental_model
    Protein adsorption to model phospholipid monolayers
    exposure
    Phosphatidylserine-containing monolayers
    limitations
    Model membrane binding, not whole-blood thrombosis. Species remain distinct.
    nutrient_topic
    Vitamin K2 research collection; topical membership is not evidence of a direct dietary effect. · Vitamin K2 / menaquinone family
    organism
    Purified human and bovine proteins
    plain_language
    Carboxylation supports a protein surface that interacts with calcium and membranes.
    primary_references
    [k2-p9609692] Adsorption of vitamin K-dependent blood coagulation proteins to spread phospholipid monolayers as determined from combined measurements of the surface pressure and surface protein concentration. (1998). https://pubmed.ncbi.nlm.nih.gov/9609692/ DOI: 10.1021/bi973118+
    tissue_or_cell_type
    Calcium-dependent Gla-domain membrane contact

    Vitamin K2: menaquinone forms, carboxylation, recycling and nutrient interactions (2026-09-17) · lines 942–953

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Protein adsorption to model phospholipid monolayers · source_derived_draft · unverified_draft

    ### k2-membrane-bovine-f2 The tested bovine-f2 Gla-domain protein showed calcium-specific contact with negatively charged phospholipid monolayers. Condition category: normal nutrient_topic: Vitamin K2 research collection; topical membership is not evidence of a direct dietary effect. plain_language: Carboxylation supports a protein surface that interacts with calcium and membranes. organism: Purified human and bovine proteins tissue_or_cell_type: Calcium-dependent Gla-domain membrane contact experimental_model: Protein adsorption to model phospholipid monolayers limitations: Model membrane binding, not whole-blood thrombosis. Species remain distinct. exposure: Phosphatidylserine-containing monolayers evidence_span: {"source_cache": "artifacts/k2-research/9609692.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d29ed548c28e5a8015742351c50aa94c8853d0f1846794964b67a73324c879bd", "start_char": 0, "end_char": 2064, "text_sha256": "d29ed548c28e5a8015742351c50aa94c8853d0f1846794964b67a73324c879bd"} [k2-p9609692] Adsorption of vitamin K-dependent blood coagulation proteins to spread phospholipid monolayers as determined from combined measurements of the surface pressure and surface protein concentration. (1998). https://pubmed.ncbi.nlm.nih.gov/9609692/ DOI: 10.1021/bi973118+
    Complete structured claim and evidence

  2. The tested bovine-proc Gla-domain protein showed calcium-specific contact with negatively charged phospholipid monolayers.

    Bovine protein C / PROC → Phosphatidylserine source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/k2-research/9609692.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d29ed548c28e5a8015742351c50aa94c8853d0f1846794964b67a73324c879bd", "start_char": 0, "end_char": 2064, "text_sha256": "d29ed548c28e5a8015742351c50aa94c8853d0f1846794964b67a73324c879bd"}
    experimental_model
    Protein adsorption to model phospholipid monolayers
    exposure
    Phosphatidylserine-containing monolayers
    limitations
    Model membrane binding, not whole-blood thrombosis. Species remain distinct.
    nutrient_topic
    Vitamin K2 research collection; topical membership is not evidence of a direct dietary effect. · Vitamin K2 / menaquinone family
    organism
    Purified human and bovine proteins
    plain_language
    Carboxylation supports a protein surface that interacts with calcium and membranes.
    primary_references
    [k2-p9609692] Adsorption of vitamin K-dependent blood coagulation proteins to spread phospholipid monolayers as determined from combined measurements of the surface pressure and surface protein concentration. (1998). https://pubmed.ncbi.nlm.nih.gov/9609692/ DOI: 10.1021/bi973118+
    tissue_or_cell_type
    Calcium-dependent Gla-domain membrane contact

    Vitamin K2: menaquinone forms, carboxylation, recycling and nutrient interactions (2026-09-17) · lines 981–992

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Protein adsorption to model phospholipid monolayers · source_derived_draft · unverified_draft

    ### k2-membrane-bovine-proc The tested bovine-proc Gla-domain protein showed calcium-specific contact with negatively charged phospholipid monolayers. Condition category: normal nutrient_topic: Vitamin K2 research collection; topical membership is not evidence of a direct dietary effect. plain_language: Carboxylation supports a protein surface that interacts with calcium and membranes. organism: Purified human and bovine proteins tissue_or_cell_type: Calcium-dependent Gla-domain membrane contact experimental_model: Protein adsorption to model phospholipid monolayers limitations: Model membrane binding, not whole-blood thrombosis. Species remain distinct. exposure: Phosphatidylserine-containing monolayers evidence_span: {"source_cache": "artifacts/k2-research/9609692.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d29ed548c28e5a8015742351c50aa94c8853d0f1846794964b67a73324c879bd", "start_char": 0, "end_char": 2064, "text_sha256": "d29ed548c28e5a8015742351c50aa94c8853d0f1846794964b67a73324c879bd"} [k2-p9609692] Adsorption of vitamin K-dependent blood coagulation proteins to spread phospholipid monolayers as determined from combined measurements of the surface pressure and surface protein concentration. (1998). https://pubmed.ncbi.nlm.nih.gov/9609692/ DOI: 10.1021/bi973118+
    Complete structured claim and evidence

  3. The tested f9 Gla-domain protein showed calcium-specific contact with negatively charged phospholipid monolayers.

    Human coagulation factor IX / F9 → Phosphatidylserine source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/k2-research/9609692.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d29ed548c28e5a8015742351c50aa94c8853d0f1846794964b67a73324c879bd", "start_char": 0, "end_char": 2064, "text_sha256": "d29ed548c28e5a8015742351c50aa94c8853d0f1846794964b67a73324c879bd"}
    experimental_model
    Protein adsorption to model phospholipid monolayers
    exposure
    Phosphatidylserine-containing monolayers
    limitations
    Model membrane binding, not whole-blood thrombosis. Species remain distinct.
    nutrient_topic
    Vitamin K2 research collection; topical membership is not evidence of a direct dietary effect. · Vitamin K2 / menaquinone family
    organism
    Purified human and bovine proteins
    plain_language
    Carboxylation supports a protein surface that interacts with calcium and membranes.
    primary_references
    [k2-p9609692] Adsorption of vitamin K-dependent blood coagulation proteins to spread phospholipid monolayers as determined from combined measurements of the surface pressure and surface protein concentration. (1998). https://pubmed.ncbi.nlm.nih.gov/9609692/ DOI: 10.1021/bi973118+
    tissue_or_cell_type
    Calcium-dependent Gla-domain membrane contact

    Vitamin K2: menaquinone forms, carboxylation, recycling and nutrient interactions (2026-09-17) · lines 955–966

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Protein adsorption to model phospholipid monolayers · source_derived_draft · unverified_draft

    ### k2-membrane-f9 The tested f9 Gla-domain protein showed calcium-specific contact with negatively charged phospholipid monolayers. Condition category: normal nutrient_topic: Vitamin K2 research collection; topical membership is not evidence of a direct dietary effect. plain_language: Carboxylation supports a protein surface that interacts with calcium and membranes. organism: Purified human and bovine proteins tissue_or_cell_type: Calcium-dependent Gla-domain membrane contact experimental_model: Protein adsorption to model phospholipid monolayers limitations: Model membrane binding, not whole-blood thrombosis. Species remain distinct. exposure: Phosphatidylserine-containing monolayers evidence_span: {"source_cache": "artifacts/k2-research/9609692.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d29ed548c28e5a8015742351c50aa94c8853d0f1846794964b67a73324c879bd", "start_char": 0, "end_char": 2064, "text_sha256": "d29ed548c28e5a8015742351c50aa94c8853d0f1846794964b67a73324c879bd"} [k2-p9609692] Adsorption of vitamin K-dependent blood coagulation proteins to spread phospholipid monolayers as determined from combined measurements of the surface pressure and surface protein concentration. (1998). https://pubmed.ncbi.nlm.nih.gov/9609692/ DOI: 10.1021/bi973118+
    Complete structured claim and evidence

  4. The tested proc Gla-domain protein showed calcium-specific contact with negatively charged phospholipid monolayers.

    Human protein C / PROC → Phosphatidylserine source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/k2-research/9609692.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d29ed548c28e5a8015742351c50aa94c8853d0f1846794964b67a73324c879bd", "start_char": 0, "end_char": 2064, "text_sha256": "d29ed548c28e5a8015742351c50aa94c8853d0f1846794964b67a73324c879bd"}
    experimental_model
    Protein adsorption to model phospholipid monolayers
    exposure
    Phosphatidylserine-containing monolayers
    limitations
    Model membrane binding, not whole-blood thrombosis. Species remain distinct.
    nutrient_topic
    Vitamin K2 research collection; topical membership is not evidence of a direct dietary effect. · Vitamin K2 / menaquinone family
    organism
    Purified human and bovine proteins
    plain_language
    Carboxylation supports a protein surface that interacts with calcium and membranes.
    primary_references
    [k2-p9609692] Adsorption of vitamin K-dependent blood coagulation proteins to spread phospholipid monolayers as determined from combined measurements of the surface pressure and surface protein concentration. (1998). https://pubmed.ncbi.nlm.nih.gov/9609692/ DOI: 10.1021/bi973118+
    tissue_or_cell_type
    Calcium-dependent Gla-domain membrane contact

    Vitamin K2: menaquinone forms, carboxylation, recycling and nutrient interactions (2026-09-17) · lines 994–1005

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Protein adsorption to model phospholipid monolayers · source_derived_draft · unverified_draft

    ### k2-membrane-proc The tested proc Gla-domain protein showed calcium-specific contact with negatively charged phospholipid monolayers. Condition category: normal nutrient_topic: Vitamin K2 research collection; topical membership is not evidence of a direct dietary effect. plain_language: Carboxylation supports a protein surface that interacts with calcium and membranes. organism: Purified human and bovine proteins tissue_or_cell_type: Calcium-dependent Gla-domain membrane contact experimental_model: Protein adsorption to model phospholipid monolayers limitations: Model membrane binding, not whole-blood thrombosis. Species remain distinct. exposure: Phosphatidylserine-containing monolayers evidence_span: {"source_cache": "artifacts/k2-research/9609692.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d29ed548c28e5a8015742351c50aa94c8853d0f1846794964b67a73324c879bd", "start_char": 0, "end_char": 2064, "text_sha256": "d29ed548c28e5a8015742351c50aa94c8853d0f1846794964b67a73324c879bd"} [k2-p9609692] Adsorption of vitamin K-dependent blood coagulation proteins to spread phospholipid monolayers as determined from combined measurements of the surface pressure and surface protein concentration. (1998). https://pubmed.ncbi.nlm.nih.gov/9609692/ DOI: 10.1021/bi973118+
    Complete structured claim and evidence

  5. The tested pros1 Gla-domain protein showed calcium-specific contact with negatively charged phospholipid monolayers.

    Human protein S / PROS1 → Phosphatidylserine source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/k2-research/9609692.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d29ed548c28e5a8015742351c50aa94c8853d0f1846794964b67a73324c879bd", "start_char": 0, "end_char": 2064, "text_sha256": "d29ed548c28e5a8015742351c50aa94c8853d0f1846794964b67a73324c879bd"}
    experimental_model
    Protein adsorption to model phospholipid monolayers
    exposure
    Phosphatidylserine-containing monolayers
    limitations
    Model membrane binding, not whole-blood thrombosis. Species remain distinct.
    nutrient_topic
    Vitamin K2 research collection; topical membership is not evidence of a direct dietary effect. · Vitamin K2 / menaquinone family
    organism
    Purified human and bovine proteins
    plain_language
    Carboxylation supports a protein surface that interacts with calcium and membranes.
    primary_references
    [k2-p9609692] Adsorption of vitamin K-dependent blood coagulation proteins to spread phospholipid monolayers as determined from combined measurements of the surface pressure and surface protein concentration. (1998). https://pubmed.ncbi.nlm.nih.gov/9609692/ DOI: 10.1021/bi973118+
    tissue_or_cell_type
    Calcium-dependent Gla-domain membrane contact

    Vitamin K2: menaquinone forms, carboxylation, recycling and nutrient interactions (2026-09-17) · lines 968–979

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Protein adsorption to model phospholipid monolayers · source_derived_draft · unverified_draft

    ### k2-membrane-pros1 The tested pros1 Gla-domain protein showed calcium-specific contact with negatively charged phospholipid monolayers. Condition category: normal nutrient_topic: Vitamin K2 research collection; topical membership is not evidence of a direct dietary effect. plain_language: Carboxylation supports a protein surface that interacts with calcium and membranes. organism: Purified human and bovine proteins tissue_or_cell_type: Calcium-dependent Gla-domain membrane contact experimental_model: Protein adsorption to model phospholipid monolayers limitations: Model membrane binding, not whole-blood thrombosis. Species remain distinct. exposure: Phosphatidylserine-containing monolayers evidence_span: {"source_cache": "artifacts/k2-research/9609692.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d29ed548c28e5a8015742351c50aa94c8853d0f1846794964b67a73324c879bd", "start_char": 0, "end_char": 2064, "text_sha256": "d29ed548c28e5a8015742351c50aa94c8853d0f1846794964b67a73324c879bd"} [k2-p9609692] Adsorption of vitamin K-dependent blood coagulation proteins to spread phospholipid monolayers as determined from combined measurements of the surface pressure and surface protein concentration. (1998). https://pubmed.ncbi.nlm.nih.gov/9609692/ DOI: 10.1021/bi973118+
    Complete structured claim and evidence

  6. Purified human PSS1 reconstituted with phosphatidylcholine showed serine base-exchange activity producing phosphatidylserine.

    Human phosphatidylserine synthase 1 / PTDSS1 → Phosphatidylserine source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text
    experimental_model
    Human PSS1 proteoliposomes with POPC and radioactive serine assays.
    limitations
    The bound endogenous lipid density could not conclusively distinguish PC from PE; no universal exclusion of PE is asserted.
    nutrient_topic
    L-Serine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Serine
    plain_language
    Serine can replace a phospholipid headgroup to make a different membrane lipid.
    primary_references
    Structural basis for catalytic mechanism of human phosphatidylserine synthase 1. · 2025 · https://pubmed.ncbi.nlm.nih.gov/40044636/ · DOI 10.1038/s41421-025-00775-3

    L-Serine: synthesis, one-carbon metabolism, lipids and cross-nutrient mechanisms (2026-09-19) · lines 246–252

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human PSS1 proteoliposomes with POPC and radioactive serine assays. · source_derived_draft · unverified_draft

    ## l-serine-pss1-exchange Serine can replace a phospholipid headgroup to make a different membrane lipid. Purified human PSS1 reconstituted with phosphatidylcholine showed serine base-exchange activity producing phosphatidylserine. Model: Human PSS1 proteoliposomes with POPC and radioactive serine assays. Limitations: The bound endogenous lipid density could not conclusively distinguish PC from PE; no universal exclusion of PE is asserted. Evidence access: Primary full text Structural basis for catalytic mechanism of human phosphatidylserine synthase 1. · 2025 · https://pubmed.ncbi.nlm.nih.gov/40044636/ · DOI 10.1038/s41421-025-00775-3
    Complete structured claim and evidence

  7. Purified human PSS2 converted phosphatidylethanolamine, but not phosphatidylcholine, into phosphatidylserine; added phosphatidylserine inhibited purified PSS2.

    Human phosphatidylserine synthase 2 / PTDSS2 → Phosphatidylserine source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Purified epitope-tagged human PSS1/PSS2 substrate and feedback assays.
    limitations
    In this preparation PSS1 used both PC and PE and was not inhibited by added PS; purified-enzyme feedback cannot be assumed identical across preparations or intact cells.
    nutrient_topic
    L-Serine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Serine
    plain_language
    A second enzyme uses a different membrane-lipid starting material.
    primary_references
    Purification and characterization of human phosphatidylserine synthases 1 and 2. · 2009 · https://pubmed.ncbi.nlm.nih.gov/19014349/ · DOI 10.1042/BJ20081597

    L-Serine: synthesis, one-carbon metabolism, lipids and cross-nutrient mechanisms (2026-09-19) · lines 414–420

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Purified epitope-tagged human PSS1/PSS2 substrate and feedback assays. · source_derived_draft · unverified_draft

    ## l-serine-pss2-exchange A second enzyme uses a different membrane-lipid starting material. Purified human PSS2 converted phosphatidylethanolamine, but not phosphatidylcholine, into phosphatidylserine; added phosphatidylserine inhibited purified PSS2. Model: Purified epitope-tagged human PSS1/PSS2 substrate and feedback assays. Limitations: In this preparation PSS1 used both PC and PE and was not inhibited by added PS; purified-enzyme feedback cannot be assumed identical across preparations or intact cells. Evidence access: Primary abstract Purification and characterization of human phosphatidylserine synthases 1 and 2. · 2009 · https://pubmed.ncbi.nlm.nih.gov/19014349/ · DOI 10.1042/BJ20081597
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. In the bovine prothrombin Gla-domain structure, the lysophosphatidylserine headgroup contacted domain-bound Ca2+ and gamma-carboxyglutamate residues.

    Calcium ion → Gamma-carboxylated prothrombin Gla domain source_derived_draftungraded
    Experimental context and source evidence
    compartment_description
    Extracellular protein-membrane interface
    experimental_model
    X-ray crystallography and NMR with lysophosphatidylserine
    limitations
    The carboxylated Gla domain is a vitamin-K-dependent protein state; calcium binding does not perform gamma-carboxylation.
    nutrient_topic
    Calcium research collection; topical membership is not evidence of a direct dietary effect. · Calcium
    organism
    Bos taurus
    plain_language
    Protein-bound calcium helps a clotting protein recognize a membrane lipid headgroup.
    primary_references
    [huang2003] Structural basis of membrane binding by Gla domains of vitamin K-dependent proteins (2003). https://www.nature.com/articles/nsb971 DOI: 10.1038/nsb971
    tissue_or_cell_type
    Purified prothrombin fragment; blood-protein context

    Calcium: mechanism-first literature curation (2026-09-17) · lines 1104–1114

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · X-ray crystallography and NMR with lysophosphatidylserine · source_derived_draft · unverified_draft

    ### calcium-gla-phosphatidylserine-binding In the bovine prothrombin Gla-domain structure, the lysophosphatidylserine headgroup contacted domain-bound Ca2+ and gamma-carboxyglutamate residues. Condition category: normal nutrient_topic: Calcium research collection; topical membership is not evidence of a direct dietary effect. plain_language: Protein-bound calcium helps a clotting protein recognize a membrane lipid headgroup. organism: Bos taurus tissue_or_cell_type: Purified prothrombin fragment; blood-protein context experimental_model: X-ray crystallography and NMR with lysophosphatidylserine limitations: The carboxylated Gla domain is a vitamin-K-dependent protein state; calcium binding does not perform gamma-carboxylation. compartment_description: Extracellular protein-membrane interface [huang2003] Structural basis of membrane binding by Gla domains of vitamin K-dependent proteins (2003). https://www.nature.com/articles/nsb971 DOI: 10.1038/nsb971
    Complete structured claim and evidence

  2. Factor Xa activated bovine prothrombin efficiently when factor Va, Ca2+ and phosphatidylserine-containing phospholipids assembled the complete prothrombinase system.

    Prothrombin / coagulation factor II / F2 → Thrombin (proteolytically activated F2) source_derived_draftungraded
    Experimental context and source evidence
    compartment_description
    Phospholipid surface
    experimental_model
    Kinetic reconstitution with defined phospholipids
    limitations
    Low residual Xa activity exists without the complete complex; this establishes biochemical assistance, not that extra dietary calcium accelerates clotting.
    nutrient_topic
    Calcium research collection; topical membership is not evidence of a direct dietary effect. · Calcium
    organism
    Bos taurus
    plain_language
    Calcium helps the membrane-associated clotting machinery generate thrombin.
    primary_references
    [rosing1980] The role of phospholipids and factor Va in the prothrombinase complex (1980). https://pubmed.ncbi.nlm.nih.gov/7350159/ DOI: 10.1016/S0021-9258(19)86294-4
    tissue_or_cell_type
    Purified blood proteins

    Calcium: mechanism-first literature curation (2026-09-17) · lines 1116–1126

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Kinetic reconstitution with defined phospholipids · source_derived_draft · unverified_draft

    ### calcium-phospholipid-prothrombinase Factor Xa activated bovine prothrombin efficiently when factor Va, Ca2+ and phosphatidylserine-containing phospholipids assembled the complete prothrombinase system. Condition category: normal nutrient_topic: Calcium research collection; topical membership is not evidence of a direct dietary effect. plain_language: Calcium helps the membrane-associated clotting machinery generate thrombin. organism: Bos taurus tissue_or_cell_type: Purified blood proteins experimental_model: Kinetic reconstitution with defined phospholipids limitations: Low residual Xa activity exists without the complete complex; this establishes biochemical assistance, not that extra dietary calcium accelerates clotting. compartment_description: Phospholipid surface [rosing1980] The role of phospholipids and factor Va in the prothrombinase complex (1980). https://pubmed.ncbi.nlm.nih.gov/7350159/ DOI: 10.1016/S0021-9258(19)86294-4
    Complete structured claim and evidence

  3. Functional AXL activation by GAS6 in the reporter system depended on vitamin K-mediated carboxylation and phosphatidylserine engagement.

    Gamma-carboxylated human GAS6 → Human AXL receptor tyrosine kinase source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/k2-research/29176978.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "14dfae68318cd2654ee423539418eb489da66e26117e35473e99986b29b8efd7", "start_char": 0, "end_char": 1704, "text_sha256": "14dfae68318cd2654ee423539418eb489da66e26117e35473e99986b29b8efd7"}
    experimental_model
    TAM reporter cells and GAS6 domain/point mutagenesis
    exposure
    Warfarin, Gla/EGF mutations and PS-positive cells or vesicles
    limitations
    Receptor binding and receptor activation are different endpoints; no clinical K2 immune benefit was tested.
    nutrient_topic
    Vitamin K2 research collection; topical membership is not evidence of a direct dietary effect. · Vitamin K2 / menaquinone family
    organism
    Recombinant human GAS6 and TAM reporter systems
    plain_language
    A modified signaling protein needs the right membrane surface to activate its receptor.
    primary_references
    [k2-p29176978] Requirement of Gamma-Carboxyglutamic Acid Modification and Phosphatidylserine Binding for the Activation of Tyro3, Axl, and Mertk Receptors by Growth Arrest-Specific 6. (2017). https://pubmed.ncbi.nlm.nih.gov/29176978/ DOI: 10.3389/fimmu.2017.01521
    tissue_or_cell_type
    Phosphatidylserine-bearing surfaces and receptors

    Vitamin K2: menaquinone forms, carboxylation, recycling and nutrient interactions (2026-09-17) · lines 591–602

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · TAM reporter cells and GAS6 domain/point mutagenesis · source_derived_draft · unverified_draft

    ### k2-gas6-axl Functional AXL activation by GAS6 in the reporter system depended on vitamin K-mediated carboxylation and phosphatidylserine engagement. Condition category: normal nutrient_topic: Vitamin K2 research collection; topical membership is not evidence of a direct dietary effect. plain_language: A modified signaling protein needs the right membrane surface to activate its receptor. organism: Recombinant human GAS6 and TAM reporter systems tissue_or_cell_type: Phosphatidylserine-bearing surfaces and receptors experimental_model: TAM reporter cells and GAS6 domain/point mutagenesis limitations: Receptor binding and receptor activation are different endpoints; no clinical K2 immune benefit was tested. exposure: Warfarin, Gla/EGF mutations and PS-positive cells or vesicles evidence_span: {"source_cache": "artifacts/k2-research/29176978.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "14dfae68318cd2654ee423539418eb489da66e26117e35473e99986b29b8efd7", "start_char": 0, "end_char": 1704, "text_sha256": "14dfae68318cd2654ee423539418eb489da66e26117e35473e99986b29b8efd7"} [k2-p29176978] Requirement of Gamma-Carboxyglutamic Acid Modification and Phosphatidylserine Binding for the Activation of Tyro3, Axl, and Mertk Receptors by Growth Arrest-Specific 6. (2017). https://pubmed.ncbi.nlm.nih.gov/29176978/ DOI: 10.3389/fimmu.2017.01521
    Complete structured claim and evidence

  4. Functional MERTK activation by GAS6 in the reporter system depended on vitamin K-mediated carboxylation and phosphatidylserine engagement.

    Gamma-carboxylated human GAS6 → Human MERTK receptor tyrosine kinase source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/k2-research/29176978.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "14dfae68318cd2654ee423539418eb489da66e26117e35473e99986b29b8efd7", "start_char": 0, "end_char": 1704, "text_sha256": "14dfae68318cd2654ee423539418eb489da66e26117e35473e99986b29b8efd7"}
    experimental_model
    TAM reporter cells and GAS6 domain/point mutagenesis
    exposure
    Warfarin, Gla/EGF mutations and PS-positive cells or vesicles
    limitations
    Receptor binding and receptor activation are different endpoints; no clinical K2 immune benefit was tested.
    nutrient_topic
    Vitamin K2 research collection; topical membership is not evidence of a direct dietary effect. · Vitamin K2 / menaquinone family
    organism
    Recombinant human GAS6 and TAM reporter systems
    plain_language
    A modified signaling protein needs the right membrane surface to activate its receptor.
    primary_references
    [k2-p29176978] Requirement of Gamma-Carboxyglutamic Acid Modification and Phosphatidylserine Binding for the Activation of Tyro3, Axl, and Mertk Receptors by Growth Arrest-Specific 6. (2017). https://pubmed.ncbi.nlm.nih.gov/29176978/ DOI: 10.3389/fimmu.2017.01521
    tissue_or_cell_type
    Phosphatidylserine-bearing surfaces and receptors

    Vitamin K2: menaquinone forms, carboxylation, recycling and nutrient interactions (2026-09-17) · lines 604–615

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · TAM reporter cells and GAS6 domain/point mutagenesis · source_derived_draft · unverified_draft

    ### k2-gas6-mertk Functional MERTK activation by GAS6 in the reporter system depended on vitamin K-mediated carboxylation and phosphatidylserine engagement. Condition category: normal nutrient_topic: Vitamin K2 research collection; topical membership is not evidence of a direct dietary effect. plain_language: A modified signaling protein needs the right membrane surface to activate its receptor. organism: Recombinant human GAS6 and TAM reporter systems tissue_or_cell_type: Phosphatidylserine-bearing surfaces and receptors experimental_model: TAM reporter cells and GAS6 domain/point mutagenesis limitations: Receptor binding and receptor activation are different endpoints; no clinical K2 immune benefit was tested. exposure: Warfarin, Gla/EGF mutations and PS-positive cells or vesicles evidence_span: {"source_cache": "artifacts/k2-research/29176978.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "14dfae68318cd2654ee423539418eb489da66e26117e35473e99986b29b8efd7", "start_char": 0, "end_char": 1704, "text_sha256": "14dfae68318cd2654ee423539418eb489da66e26117e35473e99986b29b8efd7"} [k2-p29176978] Requirement of Gamma-Carboxyglutamic Acid Modification and Phosphatidylserine Binding for the Activation of Tyro3, Axl, and Mertk Receptors by Growth Arrest-Specific 6. (2017). https://pubmed.ncbi.nlm.nih.gov/29176978/ DOI: 10.3389/fimmu.2017.01521
    Complete structured claim and evidence

  5. Functional TYRO3 activation by GAS6 in the reporter system depended on vitamin K-mediated carboxylation and phosphatidylserine engagement.

    Gamma-carboxylated human GAS6 → Human TYRO3 receptor tyrosine kinase source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/k2-research/29176978.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "14dfae68318cd2654ee423539418eb489da66e26117e35473e99986b29b8efd7", "start_char": 0, "end_char": 1704, "text_sha256": "14dfae68318cd2654ee423539418eb489da66e26117e35473e99986b29b8efd7"}
    experimental_model
    TAM reporter cells and GAS6 domain/point mutagenesis
    exposure
    Warfarin, Gla/EGF mutations and PS-positive cells or vesicles
    limitations
    Receptor binding and receptor activation are different endpoints; no clinical K2 immune benefit was tested.
    nutrient_topic
    Vitamin K2 research collection; topical membership is not evidence of a direct dietary effect. · Vitamin K2 / menaquinone family
    organism
    Recombinant human GAS6 and TAM reporter systems
    plain_language
    A modified signaling protein needs the right membrane surface to activate its receptor.
    primary_references
    [k2-p29176978] Requirement of Gamma-Carboxyglutamic Acid Modification and Phosphatidylserine Binding for the Activation of Tyro3, Axl, and Mertk Receptors by Growth Arrest-Specific 6. (2017). https://pubmed.ncbi.nlm.nih.gov/29176978/ DOI: 10.3389/fimmu.2017.01521
    tissue_or_cell_type
    Phosphatidylserine-bearing surfaces and receptors

    Vitamin K2: menaquinone forms, carboxylation, recycling and nutrient interactions (2026-09-17) · lines 578–589

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · TAM reporter cells and GAS6 domain/point mutagenesis · source_derived_draft · unverified_draft

    ### k2-gas6-tyro3 Functional TYRO3 activation by GAS6 in the reporter system depended on vitamin K-mediated carboxylation and phosphatidylserine engagement. Condition category: normal nutrient_topic: Vitamin K2 research collection; topical membership is not evidence of a direct dietary effect. plain_language: A modified signaling protein needs the right membrane surface to activate its receptor. organism: Recombinant human GAS6 and TAM reporter systems tissue_or_cell_type: Phosphatidylserine-bearing surfaces and receptors experimental_model: TAM reporter cells and GAS6 domain/point mutagenesis limitations: Receptor binding and receptor activation are different endpoints; no clinical K2 immune benefit was tested. exposure: Warfarin, Gla/EGF mutations and PS-positive cells or vesicles evidence_span: {"source_cache": "artifacts/k2-research/29176978.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "14dfae68318cd2654ee423539418eb489da66e26117e35473e99986b29b8efd7", "start_char": 0, "end_char": 1704, "text_sha256": "14dfae68318cd2654ee423539418eb489da66e26117e35473e99986b29b8efd7"} [k2-p29176978] Requirement of Gamma-Carboxyglutamic Acid Modification and Phosphatidylserine Binding for the Activation of Tyro3, Axl, and Mertk Receptors by Growth Arrest-Specific 6. (2017). https://pubmed.ncbi.nlm.nih.gov/29176978/ DOI: 10.3389/fimmu.2017.01521
    Complete structured claim and evidence

  6. Human PISD converts phosphatidylserine to phosphatidylethanolamine in the inner mitochondrial membrane; patient fibroblasts with PISD variants showed reduced conversion.

    Human phosphatidylserine decarboxylase / PISD → Phosphatidylethanolamine source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Human family genetics and fibroblast lipid-conversion measurements.
    limitations
    This pathway uses membrane-bound phosphatidylserine, not free serine as the direct PISD substrate.
    nutrient_topic
    L-Serine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Serine
    plain_language
    A serine-derived lipid feeds another lipid needed inside mitochondria.
    primary_references
    PISD is a mitochondrial disease gene causing skeletal dysplasia, cataracts, and white matter changes. · 2019 · https://pubmed.ncbi.nlm.nih.gov/30858161/ · DOI 10.26508/lsa.201900353

    L-Serine: synthesis, one-carbon metabolism, lipids and cross-nutrient mechanisms (2026-09-19) · lines 422–428

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human family genetics and fibroblast lipid-conversion measurements. · source_derived_draft · unverified_draft

    ## l-serine-pisd-decarboxylation A serine-derived lipid feeds another lipid needed inside mitochondria. Human PISD converts phosphatidylserine to phosphatidylethanolamine in the inner mitochondrial membrane; patient fibroblasts with PISD variants showed reduced conversion. Model: Human family genetics and fibroblast lipid-conversion measurements. Limitations: This pathway uses membrane-bound phosphatidylserine, not free serine as the direct PISD substrate. Evidence access: Primary abstract PISD is a mitochondrial disease gene causing skeletal dysplasia, cataracts, and white matter changes. · 2019 · https://pubmed.ncbi.nlm.nih.gov/30858161/ · DOI 10.26508/lsa.201900353
    Complete structured claim and evidence

  7. PISD patient fibroblasts had fragmented mitochondria, enlarged lysosomes and reduced maximal oxygen consumption; one variant impaired the enzyme autocatalytic processing required for activity.

    Human phosphatidylserine decarboxylase / PISD → Mitochondrial function in PISD patient fibroblasts source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_access
    Primary abstract
    experimental_model
    Two affected sisters, patient fibroblasts and functional variant characterization.
    limitations
    The other allele produced an alternative splice product; different molecular defects remain distinct.
    nutrient_topic
    L-Serine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Serine
    plain_language
    A downstream processing defect can persist despite precursor availability.
    primary_references
    PISD is a mitochondrial disease gene causing skeletal dysplasia, cataracts, and white matter changes. · 2019 · https://pubmed.ncbi.nlm.nih.gov/30858161/ · DOI 10.26508/lsa.201900353
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    L-Serine: synthesis, one-carbon metabolism, lipids and cross-nutrient mechanisms (2026-09-19) · lines 430–436

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Two affected sisters, patient fibroblasts and functional variant characterization. · source_derived_draft · unverified_draft

    ## l-serine-pisd-failure A downstream processing defect can persist despite precursor availability. PISD patient fibroblasts had fragmented mitochondria, enlarged lysosomes and reduced maximal oxygen consumption; one variant impaired the enzyme autocatalytic processing required for activity. Model: Two affected sisters, patient fibroblasts and functional variant characterization. Limitations: The other allele produced an alternative splice product; different molecular defects remain distinct. Evidence access: Primary abstract PISD is a mitochondrial disease gene causing skeletal dysplasia, cataracts, and white matter changes. · 2019 · https://pubmed.ncbi.nlm.nih.gov/30858161/ · DOI 10.26508/lsa.201900353
    Complete structured claim and evidence

  8. 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

  9. Adding 1 mol% alpha-tocopherol enhanced isolated PKC alpha C2-domain association with phosphatidylserine-containing lipid surfaces by surface plasmon resonance. Tocopherol without phosphatidylserine did not support binding.

    RRR-alpha-tocopherol → PKC alpha C2-domain association with phosphatidylserine membranes source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    false
    experimental_model
    Surface plasmon resonance with recombinant C2 domain and lipid vesicles
    exposure
    Base lipid composition 70:20:10 mol%; alpha-tocopherol at 1 mol% replacing POPC; no-PS control had 10 mol% tocopherol.
    limitations
    A membrane association endpoint is distinct from kinase activation. No direct C2-domain binding to free tocopherol is claimed.
    nutrient_topic
    Vitamin E research collection; topical membership is not evidence of a direct dietary effect. · Vitamin E
    organism
    Recombinant construct; species not independently stated
    plain_language
    Alpha-tocopherol changed how the kinase’s membrane-binding domain associated with a membrane containing phosphatidylserine.
    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
    Artificial POPC/POPE/POPS membrane

    Vitamin E: transport, membrane protection and nutrient interactions (2026-09-17) · lines 998–1009

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Surface plasmon resonance with recombinant C2 domain and lipid vesicles · source_derived_draft · unverified_draft

    ### e-sig-alpha-pkc-ps-association Adding 1 mol% alpha-tocopherol enhanced isolated PKC alpha C2-domain association with phosphatidylserine-containing lipid surfaces by surface plasmon resonance. Tocopherol without phosphatidylserine did not support binding. Condition category: normal nutrient_topic: Vitamin E research collection; topical membership is not evidence of a direct dietary effect. plain_language: Alpha-tocopherol changed how the kinase’s membrane-binding domain associated with a membrane containing phosphatidylserine. organism: Recombinant construct; species not independently stated tissue_or_cell_type: Artificial POPC/POPE/POPS membrane experimental_model: Surface plasmon resonance with recombinant C2 domain and lipid vesicles limitations: A membrane association endpoint is distinct from kinase activation. No direct C2-domain binding to free tocopherol is claimed. exposure: Base lipid composition 70:20:10 mol%; alpha-tocopherol at 1 mol% replacing POPC; no-PS control had 10 mol% tocopherol. 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

  10. 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

In the sources

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    This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.

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