Component

SELENOP

Selenoprotein P; a major circulating selenium-transport protein produced by the liver.

9 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. Acute inflammation and associated hepatic or systemic changes can lower circulating SELENOP.

    Acute inflammation → SELENOP source_derived_draftsource_reported: Human observational context and mechanistic interpretation; source-derived unverified synthesis.
    Experimental context and source evidence
    availability_state
    Acute inflammation or severe illness changes hepatic priorities, protein distribution, losses, or intake.
    experimental_scope
    Inflammatory and acute-illness measurement context, including observational associations with illness severity.
    limitations
    Inflammation and true deficiency can coexist. This is neither proof of adequate nutrition nor proof that supplementation benefits outcomes. Deliberate nutritional immunity remains a hypothesis.
    trigger_kind
    biomarker_context

    Selenium deficiency: a mechanism-first reference · lines 629–635

    Supplied selenium deficiency reference · supports · Supplied reference; verify the primary study and experimental context. · source_derived_draft · unverified_draft

    Inflammation can lower circulating selenium and SELENOP. Cytokine signaling, hepatic reprioritization, albumin changes, redistribution, illness severity, renal losses, and nutritional intake can all contribute. acute inflammation / severe illness ↓ hepatic and systemic protein redistribution ↓ SELENOP and circulating selenium can fall
    Complete structured claim and evidence

  2. Reduced selenium intake or availability can lower circulating SELENOP and tissue selenium delivery.

    Selenium → SELENOP source_derived_draftsource_reported: Animal model and biochemical transport biology; source-derived unverified synthesis.
    Experimental context and source evidence
    availability_state
    Dietary selenium availability declines.
    experimental_scope
    Tissue-selective distribution, largely from experimental models; relative retention differs from absolute protection.
    limitations
    There is no fixed human organ sacrifice sequence. Low circulating SELENOP can also reflect inflammation, and receptor disruption is a distinct machinery state.
    trigger_kind
    nutrient_deficiency

    Selenium deficiency: a mechanism-first reference · lines 783–791

    Supplied selenium deficiency reference · supports · Supplied reference; verify the primary study and experimental context. · source_derived_draft · unverified_draft

    selenium intake / availability ↓ │ ▼ central selenium metabolism and Sec-tRNA supply become constrained │ ├─ tRNA^[Ser]Sec modification can shift (including Um34 / FTSJ1 biology) ├─ SECIS-dependent UGA recoding changes ├─ selected transcripts can undergo stronger repression / NMD └─ circulating SELENOP and tissue delivery can fall
    Complete structured claim and evidence

  3. SELENOP can rise with selenium supply and then approach a study-dependent plateau.

    Selenium → SELENOP source_derived_draftsource_reported: Human intervention for biomarker plateaus; supplied-source interpretation of measurement limits.
    Experimental context and source evidence
    availability_state
    A selenium-responsive circulating biomarker approaches a plateau in a particular study or individual context.
    experimental_scope
    Human intervention dose-response observations and biomarker interpretation.
    limitations
    Study-specific plateaus cannot be mapped to GPX1 NMD, thyroid or immune failure, GPX4 loss, or an absolute antioxidant-to-pro-oxidant switch. Plasma and whole-blood values are not interchangeable.
    trigger_kind
    biomarker_context

    Selenium deficiency: a mechanism-first reference · lines 157–161

    Supplied selenium deficiency reference · supports · Supplied reference; verify the primary study and experimental context. · source_derived_draft · unverified_draft

    SELENOP plateau near ~125 µg/L in the Hurst trial Human randomized dose-response trial Study-specific plateau, not a universal treatment target [2]

    Selenium deficiency: a mechanism-first reference · lines 569–575

    Supplied selenium deficiency reference · supports · Supplied reference; verify the primary study and experimental context. · source_derived_draft · unverified_draft

    SELENOP Rises with selenium supply and can plateau Functional selenium transport / selenoprotein-related status Acute-phase sensitive; assay availability limited
    Complete structured claim and evidence

  4. IL-6 lowers hepatic SELENOP expression and secretion in human hepatocyte cultures.

    IL6 → SELENOP source_derived_draftliterature_reviewed:direct_experimental
    Experimental context and source evidence
    cell_type
    Hepatocytes
    experimental_model
    Human hepatocyte cultures
    limitations
    Adaptive withholding untested; acute illness can coexist with true deficiency.
    organism
    Homo sapiens

    Selenium: literature corrections and mechanism additions · lines 1408–1418

    Metabolic Ledger literature curation, 17 September 2026; primary papers linked individually · supports · Human hepatocyte cultures · secondary_verified · secondary_verified

    ## il6-selenop Inflammation can reduce selenium-carrier production independently of intake. IL-6 lowers hepatic SELENOP expression and secretion in human hepatocyte cultures. Organism: Homo sapiens Cell type: Hepatocytes Experimental model: Human hepatocyte cultures Limitations: Adaptive withholding untested; acute illness can coexist with true deficiency. Primary reference: [Gene-specific regulation of hepatic selenoprotein expression by interleukin-6](https://pubs.rsc.org/en/content/articlelanding/2015/mt/c5mt00211g)
    Complete structured claim and evidence

  5. An ApoER2 variant containing its O-linked glycosylation domain bound SELENOP with high affinity in the tested system.

    LRP8 variant containing the O-linked glycosylation domain → SELENOP source_derived_draftliterature_reviewed:direct_experimental
    Experimental context and source evidence
    cell_type
    Jurkat
    experimental_model
    Receptor-variant assays
    limitations
    Do not generalize to all LRP8 variants.
    organism
    human

    Selenium: literature corrections and mechanism additions · lines 546–556

    Metabolic Ledger literature curation, 17 September 2026; primary papers linked individually · supports · Receptor-variant assays · secondary_verified · secondary_verified

    ## lrp8-variant-binds-selenop A receptor variant improved SELENOP binding. An ApoER2 variant containing its O-linked glycosylation domain bound SELENOP with high affinity in the tested system. Organism: human Cell type: Jurkat Experimental model: Receptor-variant assays Limitations: Do not generalize to all LRP8 variants. Primary reference: [An efficient selenium transport pathway of selenoprotein P utilizing a high-affinity ApoER2 receptor variant and being independent of selenocysteine lyase](https://pubmed.ncbi.nlm.nih.gov/37406814/)
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Vesicle acidification was required for efficient selenium utilization from SELENOP.

    SELENOP-containing vesicle acidification → Selenoprotein biosynthesis source_derived_draftliterature_reviewed:direct_experimental
    Experimental context and source evidence
    cell_type
    Jurkat and RD
    experimental_model
    Acidification inhibition
    limitations
    Chemical recovery steps are incompletely resolved.
    organism
    human

    Selenium: literature corrections and mechanism additions · lines 558–568

    Metabolic Ledger literature curation, 17 September 2026; primary papers linked individually · supports · Acidification inhibition · secondary_verified · secondary_verified

    ## acidified-vesicles-enable-selenop-use Cells processed SELENOP in acidified compartments. Vesicle acidification was required for efficient selenium utilization from SELENOP. Organism: human Cell type: Jurkat and RD Experimental model: Acidification inhibition Limitations: Chemical recovery steps are incompletely resolved. Primary reference: [An efficient selenium transport pathway of selenoprotein P utilizing a high-affinity ApoER2 receptor variant and being independent of selenocysteine lyase](https://pubmed.ncbi.nlm.nih.gov/37406814/)
    Complete structured claim and evidence

  2. Jurkat cells retained efficient SELENOP utilization without SCLY.

    SCLY → Selenoprotein biosynthesis source_derived_draftliterature_reviewed:direct_experimental
    Experimental context and source evidence
    cell_type
    Jurkat
    experimental_model
    SCLY disruption
    limitations
    Alternative recovery chemistry is unresolved.
    organism
    human

    Selenium: literature corrections and mechanism additions · lines 582–592

    Metabolic Ledger literature curation, 17 September 2026; primary papers linked individually · supports · SCLY disruption · secondary_verified · secondary_verified

    ## jurkat-selenop-use-persists-without-scly This cell line used a SCLY-independent recovery route. Jurkat cells retained efficient SELENOP utilization without SCLY. Organism: human Cell type: Jurkat Experimental model: SCLY disruption Limitations: Alternative recovery chemistry is unresolved. Primary reference: [An efficient selenium transport pathway of selenoprotein P utilizing a high-affinity ApoER2 receptor variant and being independent of selenocysteine lyase](https://pubmed.ncbi.nlm.nih.gov/37406814/)
    Complete structured claim and evidence

  3. RD cells used a lysosomal SELENOP recovery route dependent on SCLY.

    SCLY → Selenoprotein biosynthesis source_derived_draftliterature_reviewed:direct_experimental
    Experimental context and source evidence
    cell_type
    RD rhabdomyosarcoma
    experimental_model
    Perturbation assays
    limitations
    Dependency does not locate SCLY catalysis inside lysosomes.
    organism
    human

    Selenium: literature corrections and mechanism additions · lines 570–580

    Metabolic Ledger literature curation, 17 September 2026; primary papers linked individually · supports · Perturbation assays · secondary_verified · secondary_verified

    ## rd-lysosomal-selenop-recovery-requires-scly These rhabdomyosarcoma cells required SCLY for SELENOP selenium recovery. RD cells used a lysosomal SELENOP recovery route dependent on SCLY. Organism: human Cell type: RD rhabdomyosarcoma Experimental model: Perturbation assays Limitations: Dependency does not locate SCLY catalysis inside lysosomes. Primary reference: [An efficient selenium transport pathway of selenoprotein P utilizing a high-affinity ApoER2 receptor variant and being independent of selenocysteine lyase](https://pubmed.ncbi.nlm.nih.gov/37406814/)
    Complete structured claim and evidence

  4. SCLY knockdown reduced incorporation of SELENOP-derived selenium into newly synthesized selenoproteins in HeLa cells.

    SCLY → Selenoprotein biosynthesis source_derived_draftliterature_reviewed:direct_experimental
    Experimental context and source evidence
    cell_type
    HeLa
    experimental_model
    75Se-labeled SELENOP and RNA interference
    limitations
    Cell-specific dependency; not a universal uptake sequence.
    organism
    human

    Selenium: literature corrections and mechanism additions · lines 534–544

    Metabolic Ledger literature curation, 17 September 2026; primary papers linked individually · supports · 75Se-labeled SELENOP and RNA interference · secondary_verified · secondary_verified

    ## scly-supports-selenop-selenium-reuse These cells needed SCLY for efficient selenium reuse. SCLY knockdown reduced incorporation of SELENOP-derived selenium into newly synthesized selenoproteins in HeLa cells. Organism: human Cell type: HeLa Experimental model: 75Se-labeled SELENOP and RNA interference Limitations: Cell-specific dependency; not a universal uptake sequence. Primary reference: [Mammalian Selenocysteine Lyase Is Involved in Selenoprotein Biosynthesis](https://www.jstage.jst.go.jp/article/jnsv/57/4/57_4_298/_article/-char/en)
    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.

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