Component

Cellular copper uptake

Cellular copper uptake

4 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. Ccs deletion did not measurably disrupt overall copper uptake, distribution or incorporation into the other cuproenzymes examined.

    Mouse copper chaperone for SOD1 / Ccs → Cellular copper uptake source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_span
    {"source_cache": "artifacts/copper-research/10694572.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "a8c8eb387b7e9d62e19f8de4ab12db826bbda965d5e673391bff49cb7ffe99ad", "start_char": 0, "end_char": 1205, "text_sha256": "a8c8eb387b7e9d62e19f8de4ab12db826bbda965d5e673391bff49cb7ffe99ad"}
    experimental_model
    Ccs knockout mice and radiocopper labeling
    exposure
    Ccs deletion
    limitations
    Normal protein abundance can coexist with low activity; the phenotype does not establish a general dietary copper deficiency.
    nutrient_topic
    Copper research collection; topical membership is not evidence of a direct dietary effect. · Copper
    organism
    Mouse
    plain_language
    A broken delivery route can affect one enzyme while other copper routes keep working.
    primary_references
    [copper-p10694572] Copper chaperone for superoxide dismutase is essential to activate mammalian Cu/Zn superoxide dismutase. (2000). https://pubmed.ncbi.nlm.nih.gov/10694572/ DOI: 10.1073/pnas.040461197
    tissue_or_cell_type
    Multiple tissues and SOD1 protein
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Copper: transport, cuproenzymes, deficiency, excess and nutrient interactions (2026-09-17) · lines 754–765

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Ccs knockout mice and radiocopper labeling · source_derived_draft · unverified_draft

    ### copper-ccs-selective-copper-route Ccs deletion did not measurably disrupt overall copper uptake, distribution or incorporation into the other cuproenzymes examined. Condition category: machinery_impairment nutrient_topic: Copper research collection; topical membership is not evidence of a direct dietary effect. plain_language: A broken delivery route can affect one enzyme while other copper routes keep working. organism: Mouse tissue_or_cell_type: Multiple tissues and SOD1 protein experimental_model: Ccs knockout mice and radiocopper labeling limitations: Normal protein abundance can coexist with low activity; the phenotype does not establish a general dietary copper deficiency. exposure: Ccs deletion evidence_span: {"source_cache": "artifacts/copper-research/10694572.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "a8c8eb387b7e9d62e19f8de4ab12db826bbda965d5e673391bff49cb7ffe99ad", "start_char": 0, "end_char": 1205, "text_sha256": "a8c8eb387b7e9d62e19f8de4ab12db826bbda965d5e673391bff49cb7ffe99ad"} [copper-p10694572] Copper chaperone for superoxide dismutase is essential to activate mammalian Cu/Zn superoxide dismutase. (2000). https://pubmed.ncbi.nlm.nih.gov/10694572/ DOI: 10.1073/pnas.040461197
    Complete structured claim and evidence

  2. CTR1-mediated radiocopper transport was energy independent and increased at acidic extracellular pH and high extracellular potassium in the assay.

    Human high-affinity copper transporter CTR1 / SLC31A1 → Cellular copper uptake source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/copper-research/11734551.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e7b07ef7169b07bef414cdfb8996cffda2636f9a1bcd93b556d22bdce980a03c", "start_char": 0, "end_char": 1144, "text_sha256": "e7b07ef7169b07bef414cdfb8996cffda2636f9a1bcd93b556d22bdce980a03c"}
    experimental_model
    Human CTR1 expression and radiocopper transport assays
    exposure
    CTR1 expression; pH and potassium changes in culture
    limitations
    Transport kinetics in cells; elevated assay potassium is not evidence that potassium supplements improve human copper status.
    nutrient_topic
    Copper research collection; topical membership is not evidence of a direct dietary effect. · Copper
    organism
    Human protein in human HEK293 cells
    plain_language
    The chemical surroundings changed transport speed; this is not a dietary potassium recommendation.
    primary_references
    [copper-p11734551] Biochemical characterization of the human copper transporter Ctr1. (2002). https://pubmed.ncbi.nlm.nih.gov/11734551/ DOI: 10.1074/jbc.m104728200
    tissue_or_cell_type
    Plasma membrane
    transport_effect
    raises The object already names cellular copper uptake.
    transport_pool
    the cytosol The object already names cellular copper uptake.

    Copper: transport, cuproenzymes, deficiency, excess and nutrient interactions (2026-09-17) · lines 260–271

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human CTR1 expression and radiocopper transport assays · source_derived_draft · unverified_draft

    ### copper-ctr1-energy-ph CTR1-mediated radiocopper transport was energy independent and increased at acidic extracellular pH and high extracellular potassium in the assay. Condition category: normal nutrient_topic: Copper research collection; topical membership is not evidence of a direct dietary effect. plain_language: The chemical surroundings changed transport speed; this is not a dietary potassium recommendation. organism: Human protein in human HEK293 cells tissue_or_cell_type: Plasma membrane experimental_model: Human CTR1 expression and radiocopper transport assays limitations: Transport kinetics in cells; elevated assay potassium is not evidence that potassium supplements improve human copper status. exposure: CTR1 expression; pH and potassium changes in culture evidence_span: {"source_cache": "artifacts/copper-research/11734551.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e7b07ef7169b07bef414cdfb8996cffda2636f9a1bcd93b556d22bdce980a03c", "start_char": 0, "end_char": 1144, "text_sha256": "e7b07ef7169b07bef414cdfb8996cffda2636f9a1bcd93b556d22bdce980a03c"} [copper-p11734551] Biochemical characterization of the human copper transporter Ctr1. (2002). https://pubmed.ncbi.nlm.nih.gov/11734551/ DOI: 10.1074/jbc.m104728200
    Complete structured claim and evidence

  3. Human CTR1 supported high-affinity, saturable, metal-selective copper uptake at the plasma membrane.

    Human high-affinity copper transporter CTR1 / SLC31A1 → Cellular copper uptake source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/copper-research/11734551.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e7b07ef7169b07bef414cdfb8996cffda2636f9a1bcd93b556d22bdce980a03c", "start_char": 0, "end_char": 1144, "text_sha256": "e7b07ef7169b07bef414cdfb8996cffda2636f9a1bcd93b556d22bdce980a03c"}
    experimental_model
    Human CTR1 expression and radiocopper transport assays
    exposure
    CTR1 expression; pH and potassium changes in culture
    limitations
    Transport kinetics in cells; elevated assay potassium is not evidence that potassium supplements improve human copper status.
    nutrient_topic
    Copper research collection; topical membership is not evidence of a direct dietary effect. · Copper
    organism
    Human protein in human HEK293 cells
    plain_language
    CTR1 is a controlled entry route for copper into cells.
    primary_references
    [copper-p11734551] Biochemical characterization of the human copper transporter Ctr1. (2002). https://pubmed.ncbi.nlm.nih.gov/11734551/ DOI: 10.1074/jbc.m104728200
    tissue_or_cell_type
    Plasma membrane

    Copper: transport, cuproenzymes, deficiency, excess and nutrient interactions (2026-09-17) · lines 247–258

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human CTR1 expression and radiocopper transport assays · source_derived_draft · unverified_draft

    ### copper-ctr1-uptake Human CTR1 supported high-affinity, saturable, metal-selective copper uptake at the plasma membrane. Condition category: normal nutrient_topic: Copper research collection; topical membership is not evidence of a direct dietary effect. plain_language: CTR1 is a controlled entry route for copper into cells. organism: Human protein in human HEK293 cells tissue_or_cell_type: Plasma membrane experimental_model: Human CTR1 expression and radiocopper transport assays limitations: Transport kinetics in cells; elevated assay potassium is not evidence that potassium supplements improve human copper status. exposure: CTR1 expression; pH and potassium changes in culture evidence_span: {"source_cache": "artifacts/copper-research/11734551.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e7b07ef7169b07bef414cdfb8996cffda2636f9a1bcd93b556d22bdce980a03c", "start_char": 0, "end_char": 1144, "text_sha256": "e7b07ef7169b07bef414cdfb8996cffda2636f9a1bcd93b556d22bdce980a03c"} [copper-p11734551] Biochemical characterization of the human copper transporter Ctr1. (2002). https://pubmed.ncbi.nlm.nih.gov/11734551/ DOI: 10.1074/jbc.m104728200
    Complete structured claim and evidence

  4. Mouse ZIP14 did not increase uptake of radiolabeled copper supplied as Cu(I) or Cu(II) in the tested oocyte conditions.

    Mouse ZIP14 (Slc39a14) → Cellular copper uptake source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    true
    experimental_model
    Radiolabeled Cu(I) and Cu(II) uptake in Xenopus oocytes
    exposure
    Cu(I) and Cu(II) tested separately against controls.
    limitations
    A bounded negative result does not mean zinc and copper have no interaction through other proteins or intestinal mechanisms.
    nutrient_topic
    Zinc research collection; topical membership is not evidence of a direct dietary effect. · Zinc
    organism
    Mouse protein in Xenopus laevis oocytes
    plain_language
    This ZIP14 experiment found no copper transport despite detecting other metal substrates.
    primary_references
    [zinc-trans-21653899] Zip14 is a complex broad-scope metal-ion transporter whose functional properties support roles in the cellular uptake of zinc and nontransferrin-bound iron. (2011). https://pubmed.ncbi.nlm.nih.gov/21653899/ DOI: 10.1152/ajpcell.00479.2010
    tissue_or_cell_type
    Oocyte plasma membrane

    Zinc: transport, enzyme loading, deficiency and nutrient interactions (2026-09-17) · lines 518–529

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Radiolabeled Cu(I) and Cu(II) uptake in Xenopus oocytes · source_derived_draft · unverified_draft

    ### zinc-trans-zip14-copper-negative Mouse ZIP14 did not increase uptake of radiolabeled copper supplied as Cu(I) or Cu(II) in the tested oocyte conditions. Condition category: normal nutrient_topic: Zinc research collection; topical membership is not evidence of a direct dietary effect. plain_language: This ZIP14 experiment found no copper transport despite detecting other metal substrates. organism: Mouse protein in Xenopus laevis oocytes tissue_or_cell_type: Oocyte plasma membrane experimental_model: Radiolabeled Cu(I) and Cu(II) uptake in Xenopus oocytes limitations: A bounded negative result does not mean zinc and copper have no interaction through other proteins or intestinal mechanisms. exposure: Cu(I) and Cu(II) tested separately against controls. cross_nutrient: true [zinc-trans-21653899] Zip14 is a complex broad-scope metal-ion transporter whose functional properties support roles in the cellular uptake of zinc and nontransferrin-bound iron. (2011). https://pubmed.ncbi.nlm.nih.gov/21653899/ DOI: 10.1152/ajpcell.00479.2010
    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