Component

PTPRC

Independent entity for contextual scientific-audit claims; no universal nutritional effect implied.

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 it acts on

  1. CD45 removal of activation-loop LCK Y394 phosphorylation reduces activating phosphorylation.

    PTPRC → LCK activation competence source_derived_draftliterature_reviewed:direct_experimental
    Experimental context and source evidence
    cell_type
    Purified kinase/phosphatase
    experimental_model
    Biochemical LCK/CD45 phosphorylation assays
    limitations
    Site effect does not determine total cellular output or dietary selenium response.
    organism
    Mammalian biochemical systems

    Selenium: literature corrections and mechanism additions · lines 1288–1298

    Metabolic Ledger literature curation, 17 September 2026; primary papers linked individually · supports · Biochemical LCK/CD45 phosphorylation assays · secondary_verified · secondary_verified

    ## cd45-y394 Removing the Y394 phosphate reduces an activating LCK signal. CD45 removal of activation-loop LCK Y394 phosphorylation reduces activating phosphorylation. Organism: Mammalian biochemical systems Cell type: Purified kinase/phosphatase Experimental model: Biochemical LCK/CD45 phosphorylation assays Limitations: Site effect does not determine total cellular output or dietary selenium response. Primary reference: [The noncatalytic domains of Lck regulate its dephosphorylation by CD45](https://pubmed.ncbi.nlm.nih.gov/12922168/)
    Complete structured claim and evidence

  2. CD45 removal of inhibitory LCK Y505 phosphorylation can favor an open activation-competent state.

    PTPRC → LCK activation competence source_derived_draftliterature_reviewed:direct_experimental
    Experimental context and source evidence
    cell_type
    T-cell and biochemical assays
    experimental_model
    Biochemical LCK/CD45 phosphorylation assays; CD45-deficient cells and LCK binding/phosphorylation experiments
    limitations
    Net effect depends on concentration/localization and both sites; no selenium-dependent site effect established.
    organism
    Mammalian biochemical and T-cell systems

    Selenium: literature corrections and mechanism additions · lines 1275–1286

    Metabolic Ledger literature curation, 17 September 2026; primary papers linked individually · supports · Biochemical LCK/CD45 phosphorylation assays; CD45-deficient cells and LCK binding/phosphorylation experiments · secondary_verified · secondary_verified

    ## cd45-y505 Removing the Y505 phosphate can release LCK inhibition. CD45 removal of inhibitory LCK Y505 phosphorylation can favor an open activation-competent state. Organism: Mammalian biochemical and T-cell systems Cell type: T-cell and biochemical assays Experimental model: Biochemical LCK/CD45 phosphorylation assays; CD45-deficient cells and LCK binding/phosphorylation experiments Limitations: Net effect depends on concentration/localization and both sites; no selenium-dependent site effect established. Primary reference: [The noncatalytic domains of Lck regulate its dephosphorylation by CD45](https://pubmed.ncbi.nlm.nih.gov/12922168/) Primary reference: [CD45 specifically modulates binding of Lck to a phosphopeptide encompassing the negative regulatory tyrosine of Lck.](https://pubmed.ncbi.nlm.nih.gov/8428589/)
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Despite its ability to bind both soluble and particulate beta-glucan polymers, Dectin-1 signalling is only activated by particulate beta-glucans, which cluster the receptor in synapse-like structures from which the regulatory tyrosine phosphatases CD45 and CD148 are excluded, providing a model mechanism by which innate immune receptors can distinguish direct microbial contact from detection of microbes at a distance and initiate direct cellular antimicrobial responses only when they are required.

    The phagocytic synapse, a receptor-rich contact that excludes CD45 and CD148 → Dectin-1 / CLEC7A source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/glucan-research/21525931.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "5bb7dfc847efb60e644eeaf672d3277d18bca9c4fc75051c8d568d8e5dc450e0", "start_char": 0, "end_char": 1406, "text_sha256": "5bb7dfc847efb60e644eeaf672d3277d18bca9c4fc75051c8d568d8e5dc450e0"}
    experimental_model
    Comparison of soluble and particulate beta-glucan polymers on Dectin-1 signalling, with imaging of receptor and phosphatase distribution
    exposure
    Soluble against particulate beta-glucan polymers on Dectin-1-expressing phagocytes
    limitations
    The abstract reports the soluble-versus-particulate comparison and the phosphatase exclusion. It does not state what happens when a soluble glucan is immobilised, so no claim here rests on that.
    nutrient_topic
    Beta-glucan research collection; topical membership is not evidence of a direct clinical effect, and each preparation is recorded as its own entity with no family link joining any pair. · Beta-glucan
    organism
    Mouse
    plain_language
    Binding was not enough: the receptor only fired when particles packed it into a patch that shut out the enzymes which switch it off.
    primary_references
    [bg-p21525931] Activation of the innate immune receptor Dectin-1 upon formation of a 'phagocytic synapse'. (2011). https://pubmed.ncbi.nlm.nih.gov/21525931/ DOI: 10.1038/nature10071
    tissue_or_cell_type
    Myeloid phagocytes

    Beta-glucan: a structural family rather than an agent, what decides whether a bound glucan actually signals, the complement route that a cereal and a yeast preparation share, and the unequal human evidence behind each (2026-09-22) · lines 138–149

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Comparison of soluble and particulate beta-glucan polymers on Dectin-1 signalling, with imaging of receptor and phosphatase distribution · source_derived_draft · unverified_draft

    ### bg-only-particles-signal Despite its ability to bind both soluble and particulate beta-glucan polymers, Dectin-1 signalling is only activated by particulate beta-glucans, which cluster the receptor in synapse-like structures from which the regulatory tyrosine phosphatases CD45 and CD148 are excluded, providing a model mechanism by which innate immune receptors can distinguish direct microbial contact from detection of microbes at a distance and initiate direct cellular antimicrobial responses only when they are required. Condition category: normal nutrient_topic: Beta-glucan research collection; topical membership is not evidence of a direct clinical effect, and each preparation is recorded as its own entity with no family link joining any pair. plain_language: Binding was not enough: the receptor only fired when particles packed it into a patch that shut out the enzymes which switch it off. organism: Mouse tissue_or_cell_type: Myeloid phagocytes experimental_model: Comparison of soluble and particulate beta-glucan polymers on Dectin-1 signalling, with imaging of receptor and phosphatase distribution limitations: The abstract reports the soluble-versus-particulate comparison and the phosphatase exclusion. It does not state what happens when a soluble glucan is immobilised, so no claim here rests on that. exposure: Soluble against particulate beta-glucan polymers on Dectin-1-expressing phagocytes evidence_span: {"source_cache": "artifacts/glucan-research/21525931.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "5bb7dfc847efb60e644eeaf672d3277d18bca9c4fc75051c8d568d8e5dc450e0", "start_char": 0, "end_char": 1406, "text_sha256": "5bb7dfc847efb60e644eeaf672d3277d18bca9c4fc75051c8d568d8e5dc450e0"} [bg-p21525931] Activation of the innate immune receptor Dectin-1 upon formation of a 'phagocytic synapse'. (2011). https://pubmed.ncbi.nlm.nih.gov/21525931/ DOI: 10.1038/nature10071
    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