Component

Human AMPK catalytic subunit alpha 1 / PRKAA1

Human AMPK catalytic subunit alpha 1 / PRKAA1. Species, exposure and limitations are retained in each linked claim.

2 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. Berberine reduced association between UHRF1 and AMPK alpha 1.

    Berberine → UHRF1 association with AMPK alpha 1 source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/berberine-research/37144221.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e146553474cca4ec8441b54580959225dcf3dfee60a50ea519ccac5e2cb6488d", "start_char": 0, "end_char": 1212, "text_sha256": "e146553474cca4ec8441b54580959225dcf3dfee60a50ea519ccac5e2cb6488d"}
    experimental_model
    Lysosome isolation, genetic perturbation and coimmunoprecipitation
    exposure
    Low-dose berberine experiments; AXIN1 loss, PEN2 perturbation and UHRF1 overexpression
    limitations
    Cancer-cell signaling model; low laboratory concentration is not proof of a mechanism at every human tissue exposure. Different dose/context from respiratory inhibition studies.
    nutrient_topic
    Berberine research collection; topical membership is not evidence of a direct dietary effect. · Berberine
    organism
    Human HCT-116 cells
    plain_language
    The interaction between two separately stored proteins changed.
    primary_references
    [berberine-p37144221] Berberine stimulates lysosomal AMPK independent of PEN2 and maintains cellular AMPK activity through inhibiting the dephosphorylation regulator UHRF1. (2023). https://pubmed.ncbi.nlm.nih.gov/37144221/ DOI: 10.3389/fphar.2023.1148611
    tissue_or_cell_type
    Lysosomal AMPK and UHRF1 regulation

    Berberine: metabolism, nutrient connections and drug interactions (2026-09-17) · lines 402–413

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Lysosome isolation, genetic perturbation and coimmunoprecipitation · source_derived_draft · unverified_draft

    ### berberine-uhrf1-association Berberine reduced association between UHRF1 and AMPK alpha 1. Condition category: normal nutrient_topic: Berberine research collection; topical membership is not evidence of a direct dietary effect. plain_language: The interaction between two separately stored proteins changed. organism: Human HCT-116 cells tissue_or_cell_type: Lysosomal AMPK and UHRF1 regulation experimental_model: Lysosome isolation, genetic perturbation and coimmunoprecipitation limitations: Cancer-cell signaling model; low laboratory concentration is not proof of a mechanism at every human tissue exposure. Different dose/context from respiratory inhibition studies. exposure: Low-dose berberine experiments; AXIN1 loss, PEN2 perturbation and UHRF1 overexpression evidence_span: {"source_cache": "artifacts/berberine-research/37144221.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e146553474cca4ec8441b54580959225dcf3dfee60a50ea519ccac5e2cb6488d", "start_char": 0, "end_char": 1212, "text_sha256": "e146553474cca4ec8441b54580959225dcf3dfee60a50ea519ccac5e2cb6488d"} [berberine-p37144221] Berberine stimulates lysosomal AMPK independent of PEN2 and maintains cellular AMPK activity through inhibiting the dephosphorylation regulator UHRF1. (2023). https://pubmed.ncbi.nlm.nih.gov/37144221/ DOI: 10.3389/fphar.2023.1148611
    Complete structured claim and evidence

  2. At concentrations reached in plasma after administration of salsalate or of aspirin at high doses, salicylate activates AMP-activated protein kinase by binding at the same site as the synthetic activator A-769662 to cause allosteric activation and inhibition of dephosphorylation of the activating phosphorylation site threonine-172, and in knockout mice the effects of salicylate to increase fat utilisation and to lower plasma fatty acids in vivo were lost.

    Salicylate / salicylic acid → AMP-activated protein kinase complexes source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    biomarker_context Imported condition classification; unverified.
    evidence_span
    {"source_cache": "artifacts/aspirin-research/22517326.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "1a48863bf252421416f67d62acb18c9f44f170075c5aff6f775eba14bba2b1b4", "start_char": 0, "end_char": 887, "text_sha256": "1a48863bf252421416f67d62acb18c9f44f170075c5aff6f775eba14bba2b1b4"}
    experimental_model
    Allosteric activation and dephosphorylation assays with AMP-activated protein kinase knockout mice
    exposure
    Salicylate at concentrations reached in plasma after salsalate or high-dose aspirin, against the synthetic activator A-769662
    limitations
    The knockout arm ties the whole-animal effect to the kinase. The concentrations are those of high-dose salicylate therapy, not of antiplatelet aspirin, which the authors state explicitly.
    nutrient_topic
    Aspirin research collection; topical membership is not evidence of a direct clinical effect, and aspirin is recorded separately from salicylate, the metabolite it becomes. · Aspirin / acetylsalicylic acid
    organism
    Human enzyme and mouse
    plain_language
    The old plant compound switches on the cell’s energy sensor directly, at doses far above a daily aspirin.
    primary_references
    [asa-p22517326] The ancient drug salicylate directly activates AMP-activated protein kinase. (2012). https://pubmed.ncbi.nlm.nih.gov/22517326/ DOI: 10.1126/science.1215327
    tissue_or_cell_type
    AMP-activated protein kinase
    trigger_kind
    biomarker_context Imported condition classification; unverified.

    Aspirin: the serine it acetylates, the enzyme that acetylation creates, the dose that separates platelet from vessel wall, and the metabolite that is a different drug (2026-09-22) · lines 494–505

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Allosteric activation and dephosphorylation assays with AMP-activated protein kinase knockout mice · source_derived_draft · unverified_draft

    ### asa-salicylate-activates-ampk At concentrations reached in plasma after administration of salsalate or of aspirin at high doses, salicylate activates AMP-activated protein kinase by binding at the same site as the synthetic activator A-769662 to cause allosteric activation and inhibition of dephosphorylation of the activating phosphorylation site threonine-172, and in knockout mice the effects of salicylate to increase fat utilisation and to lower plasma fatty acids in vivo were lost. Condition category: biomarker_context nutrient_topic: Aspirin research collection; topical membership is not evidence of a direct clinical effect, and aspirin is recorded separately from salicylate, the metabolite it becomes. plain_language: The old plant compound switches on the cell’s energy sensor directly, at doses far above a daily aspirin. organism: Human enzyme and mouse tissue_or_cell_type: AMP-activated protein kinase experimental_model: Allosteric activation and dephosphorylation assays with AMP-activated protein kinase knockout mice limitations: The knockout arm ties the whole-animal effect to the kinase. The concentrations are those of high-dose salicylate therapy, not of antiplatelet aspirin, which the authors state explicitly. exposure: Salicylate at concentrations reached in plasma after salsalate or high-dose aspirin, against the synthetic activator A-769662 evidence_span: {"source_cache": "artifacts/aspirin-research/22517326.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "1a48863bf252421416f67d62acb18c9f44f170075c5aff6f775eba14bba2b1b4", "start_char": 0, "end_char": 887, "text_sha256": "1a48863bf252421416f67d62acb18c9f44f170075c5aff6f775eba14bba2b1b4"} [asa-p22517326] The ancient drug salicylate directly activates AMP-activated protein kinase. (2012). https://pubmed.ncbi.nlm.nih.gov/22517326/ DOI: 10.1126/science.1215327
    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