Component

Human ERK1 / MAPK3

Human ERK1 / MAPK3; model and exposure are recorded in linked claims.

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

Where it participates (unsigned role)

  1. Strontium chloride and the ranelate preparation stimulated ERK phosphorylation in HEK293 cells transfected with human CaSR.

    Strontium ion / Sr2+ → Calcium-sensing receptor / CaSR source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Human receptor transfection and dose-response signaling assays.
    limitations
    Receptor signaling is not itself proof of stronger bone or a nutritional requirement.
    nutrient_topic
    Strontium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Strontium
    plain_language
    Strontium can engage a receptor normally used to sense extracellular calcium.
    primary_references
    The Calcium-sensing Receptor (CaR) is involved in strontium ranelate-induced osteoblast differentiation and mineralization. · 2010 · https://pubmed.ncbi.nlm.nih.gov/20560105/ · DOI 10.1055/s-0030-1255091

    Strontium: calcium interactions, cellular mechanisms and mineralization (2026-09-19) · lines 70–76

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human receptor transfection and dose-response signaling assays. · source_derived_draft · unverified_draft

    ## strontium-human-casr Strontium can engage a receptor normally used to sense extracellular calcium. Strontium chloride and the ranelate preparation stimulated ERK phosphorylation in HEK293 cells transfected with human CaSR. Model: Human receptor transfection and dose-response signaling assays. Limitations: Receptor signaling is not itself proof of stronger bone or a nutritional requirement. Evidence access: Primary abstract The Calcium-sensing Receptor (CaR) is involved in strontium ranelate-induced osteoblast differentiation and mineralization. · 2010 · https://pubmed.ncbi.nlm.nih.gov/20560105/ · DOI 10.1055/s-0030-1255091
    Complete structured claim and evidence

  2. In HUVEC experiments, berberine reduced vanadyl-acetylacetonate-associated apoptosis, junction/cytoskeleton damage and permeability changes, with lower excessive ERK/Akt phosphorylation.

    Berberine → Vanadyl-acetylacetonate injury in human HUVEC cultures source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Human endothelial-cell experiments accompanying diabetic-rat study.
    limitations
    Pathway association does not establish direct inhibition of ERK or Akt by berberine at human exposure.
    nutrient_topic
    Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
    plain_language
    Protection from one compound’s cellular toxicity can accompany lower signaling activity.
    primary_references
    Vanadyl Acetylacetonate and Berberine Synergistically Ameliorate Diabetes-induced Vascular Dysfunction and Reduce Endothelial Toxicity through ERK and Akt Regulation. · 2026 · https://pubmed.ncbi.nlm.nih.gov/40775562/ · DOI 10.1007/s12011-025-04774-z

    Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 350–356

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human endothelial-cell experiments accompanying diabetic-rat study. · source_derived_draft · unverified_draft

    ## vanadium-berberine-endothelium Protection from one compound’s cellular toxicity can accompany lower signaling activity. In HUVEC experiments, berberine reduced vanadyl-acetylacetonate-associated apoptosis, junction/cytoskeleton damage and permeability changes, with lower excessive ERK/Akt phosphorylation. Model: Human endothelial-cell experiments accompanying diabetic-rat study. Limitations: Pathway association does not establish direct inhibition of ERK or Akt by berberine at human exposure. Evidence access: Primary abstract Vanadyl Acetylacetonate and Berberine Synergistically Ameliorate Diabetes-induced Vascular Dysfunction and Reduce Endothelial Toxicity through ERK and Akt Regulation. · 2026 · https://pubmed.ncbi.nlm.nih.gov/40775562/ · DOI 10.1007/s12011-025-04774-z
    Complete structured claim and evidence

  3. ZIP7 phosphorylation was linked to release of stored zinc and downstream AKT and ERK1/2 phosphorylation in the studied human cells.

    Human zinc transporter ZIP7 / SLC39A7 → Endoplasmic-reticulum zinc release source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    Human protein kinase CK2 complex (upstream_kinase); AKT serine/threonine kinase family (downstream_kinase_family); Human ERK2 / MAPK1 (downstream_kinase); Human ERK1 / MAPK3 (downstream_kinase); Cytosolic labile zinc availability (increased_pool)
    evidence_span
    {"source_cache": "artifacts/zinc-signaling-sources/22317921-abstract.txt", "locator": "Primary indexed abstract", "file_sha256": "a8e31db38c22019d7ebef8ff165e2b3dc0b3a338e18514f0bf0c48cc5215944d"}
    experimental_model
    Human breast-cell model with ZIP7/CK2 perturbations
    exposure
    Signaling stimuli and ZIP7/CK2 phosphorylation comparisons.
    limitations
    Cellular signaling study; it does not establish dietary zinc supplementation as an anticancer intervention. Intracellular release is different from net dietary uptake.
    nutrient_topic
    Zinc research collection; topical membership is not evidence of a direct dietary effect. · Zinc
    organism
    Homo sapiens
    plain_language
    Zinc redistribution connected a storage compartment to kinase signaling.
    primary_references
    [zn-sig-22317921] Protein kinase CK2 triggers cytosolic zinc signaling pathways by phosphorylation of zinc channel ZIP7. (2012). https://pubmed.ncbi.nlm.nih.gov/22317921/ DOI: 10.1126/scisignal.2002585
    tissue_or_cell_type
    Endoplasmic reticulum and cytoplasm

    Zinc: transport, enzyme loading, deficiency and nutrient interactions (2026-09-17) · lines 999–1011

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human breast-cell model with ZIP7/CK2 perturbations · source_derived_draft · unverified_draft

    ### zn-sig-zip7-release ZIP7 phosphorylation was linked to release of stored zinc and downstream AKT and ERK1/2 phosphorylation in the studied human cells. Condition category: normal nutrient_topic: Zinc research collection; topical membership is not evidence of a direct dietary effect. plain_language: Zinc redistribution connected a storage compartment to kinase signaling. organism: Homo sapiens tissue_or_cell_type: Endoplasmic reticulum and cytoplasm experimental_model: Human breast-cell model with ZIP7/CK2 perturbations limitations: Cellular signaling study; it does not establish dietary zinc supplementation as an anticancer intervention. Intracellular release is different from net dietary uptake. exposure: Signaling stimuli and ZIP7/CK2 phosphorylation comparisons. cross_nutrient: Human protein kinase CK2 complex (upstream_kinase); AKT serine/threonine kinase family (downstream_kinase_family); Human ERK2 / MAPK1 (downstream_kinase); Human ERK1 / MAPK3 (downstream_kinase); Cytosolic labile zinc availability (increased_pool) evidence_span: {"source_cache": "artifacts/zinc-signaling-sources/22317921-abstract.txt", "locator": "Primary indexed abstract", "file_sha256": "a8e31db38c22019d7ebef8ff165e2b3dc0b3a338e18514f0bf0c48cc5215944d"} [zn-sig-22317921] Protein kinase CK2 triggers cytosolic zinc signaling pathways by phosphorylation of zinc channel ZIP7. (2012). https://pubmed.ncbi.nlm.nih.gov/22317921/ DOI: 10.1126/scisignal.2002585
    Complete structured claim and evidence

  4. Adding t10,c12 CLA increased PPAR-gamma and ERK1/2 phosphorylation before PPAR-gamma protein declined.

    trans-10,cis-12 conjugated linoleic acid → Human PPAR gamma / PPARG source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Human adipocyte time-course experiments.
    limitations
    ERK causation of the PPAR-gamma phosphorylation was proposed rather than isolated here.
    nutrient_topic
    CLA collection; isomer, preparation, species, exposure and manipulation remain explicit. · Conjugated linoleic acid / CLA isomer family
    plain_language
    Signaling changed before the regulator became less abundant.
    primary_references
    Trans-10, cis-12 conjugated linoleic acid antagonizes ligand-dependent PPARgamma activity in primary cultures of human adipocytes. · 2008 · https://pubmed.ncbi.nlm.nih.gov/18287349/ · DOI 10.1093/jn/138.3.455

    Conjugated linoleic acid: isomers, signaling, nutrient interactions and discovery (2026-09-19) · lines 110–116

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Human adipocyte time-course experiments. · source_derived_draft · unverified_draft

    ## cla-pparg-phosphorylation Signaling changed before the regulator became less abundant. Adding t10,c12 CLA increased PPAR-gamma and ERK1/2 phosphorylation before PPAR-gamma protein declined. Model: Human adipocyte time-course experiments. Limitations: ERK causation of the PPAR-gamma phosphorylation was proposed rather than isolated here. Evidence access: Primary abstract Trans-10, cis-12 conjugated linoleic acid antagonizes ligand-dependent PPARgamma activity in primary cultures of human adipocytes. · 2008 · https://pubmed.ncbi.nlm.nih.gov/18287349/ · DOI 10.1093/jn/138.3.455
    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