Component

Geranylgeranyl diphosphate / GGPP

Geranylgeranyl diphosphate / GGPP. Species, exposure and limitations are retained in each linked claim.

7 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. Geranylgeranyl diphosphate reversed the statin-induced rise in endothelial nitric oxide synthase, while farnesyl diphosphate and low-density lipoprotein did not.

    Geranylgeranyl diphosphate / GGPP → Human endothelial nitric oxide synthase / eNOS / NOS3 source_derived_draftungraded
    Experimental context and source evidence
    duration
    Not stated here
    evidence_access
    Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
    experimental_model
    Human endothelial cells
    exposure
    Geranylgeranyl diphosphate 1 to 10 micromolar, farnesyl diphosphate 5 to 10 micromolar, L-mevalonate 200 micromolar or LDL 1 mg/ml added with mevastatin
    limitations
    This identifies which isoprenoid carries the effect; it does not establish that geranylgeranyl diphosphate is limiting at ordinary statin doses in a person.
    organism
    Human endothelial cells
    plain_language
    Geranylgeranyl diphosphate reversed the statin-induced rise in endothelial nitric oxide synthase, while farnesyl diphosphate and low-density lipoprotein did not.
    primary_references
    Post-transcriptional regulation of endothelial nitric oxide synthase mRNA stability by Rho GTPase. (1998). https://pubmed.ncbi.nlm.nih.gov/9727051/ DOI: 10.1074/jbc.273.37.24266
    route
    In vitro
    tissue
    Endothelial nitric oxide synthase expression and Rho membrane translocation

    Atorvastatin: mechanism of action from target occupancy to isoprenoids, transport, muscle and metabolism (2026-09-22) · lines 67–76

    Original AI-assisted curation of twelve primary studies resolved by PubMed title search and cross-checked against live PubMed metadata. Findings obtained with mevastatin, simvastatin or the statin class are recorded against those subjects. Study-specific citations, doses, negative findings and limitations retained. Not publisher full text. · supports · · source_derived_draft · unverified_draft

    ## ggpp-reverses-the-nos-response Geranylgeranyl diphosphate reversed the statin-induced rise in endothelial nitric oxide synthase, while farnesyl diphosphate and low-density lipoprotein did not. Model/species: Human endothelial cells Tissue/system: Endothelial nitric oxide synthase expression and Rho membrane translocation Exposure: Geranylgeranyl diphosphate 1 to 10 micromolar, farnesyl diphosphate 5 to 10 micromolar, L-mevalonate 200 micromolar or LDL 1 mg/ml added with mevastatin Route: In vitro Duration: Not stated here Limits: This identifies which isoprenoid carries the effect; it does not establish that geranylgeranyl diphosphate is limiting at ordinary statin doses in a person. Primary reference: Post-transcriptional regulation of endothelial nitric oxide synthase mRNA stability by Rho GTPase. (1998). https://pubmed.ncbi.nlm.nih.gov/9727051/ DOI: 10.1074/jbc.273.37.24266 Access: Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
    Complete structured claim and evidence

What acts on it

  1. The mevalonate pathway produces isoprenoids required for functions ranging from cholesterol synthesis to growth control, under feedback regulation that also governs low-density-lipoprotein receptors.

    Mevalonate → Geranylgeranyl diphosphate / GGPP source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
    experimental_model
    Review of mammalian mevalonate-pathway regulation
    exposure
    Not applicable
    limitations
    A review of regulatory architecture, not a measurement of any one statin's effect on any one isoprenoid pool.
    organism
    Review of mammalian mevalonate-pathway regulation
    plain_language
    The mevalonate pathway produces isoprenoids required for functions ranging from cholesterol synthesis to growth control, under feedback regulation that also governs low-density-lipoprotein receptors.
    primary_references
    Regulation of the mevalonate pathway. (1990). https://pubmed.ncbi.nlm.nih.gov/1967820/ DOI: 10.1038/343425a0
    route
    Not applicable
    tissue
    Isoprenoid and sterol end-products

    Atorvastatin: mechanism of action from target occupancy to isoprenoids, transport, muscle and metabolism (2026-09-22) · lines 24–32

    Original AI-assisted curation of twelve primary studies resolved by PubMed title search and cross-checked against live PubMed metadata. Findings obtained with mevastatin, simvastatin or the statin class are recorded against those subjects. Study-specific citations, doses, negative findings and limitations retained. Not publisher full text. · supports · · source_derived_draft · unverified_draft

    ## mevalonate-supplies-isoprenoids The mevalonate pathway produces isoprenoids required for functions ranging from cholesterol synthesis to growth control, under feedback regulation that also governs low-density-lipoprotein receptors. Model/species: Review of mammalian mevalonate-pathway regulation Tissue/system: Isoprenoid and sterol end-products Exposure: Not applicable Route: Not applicable Limits: A review of regulatory architecture, not a measurement of any one statin's effect on any one isoprenoid pool. Primary reference: Regulation of the mevalonate pathway. (1990). https://pubmed.ncbi.nlm.nih.gov/1967820/ DOI: 10.1038/343425a0 Access: Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
    Complete structured claim and evidence

  2. UBIAD1 synthesized MK-4 using GGPP as the isoprenyl side-chain source.

    Human UBIAD1 prenyltransferase → Geranylgeranyl diphosphate / GGPP source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/k2-research/25874989.fulltext.txt", "locator": "Exact primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "bbd73607ba2570aa383c81c189b29dd19f1cbd7bf7acdd8343ecf3ee7dc5faf8", "start_char": 24159, "end_char": 24399, "text_sha256": "b680e2031495b2fee24a56c799e8cb2f64bbac3c6a3cb0d33592051f2cf41b9f"}
    experimental_model
    Microsomal enzyme assays and mutagenesis
    exposure
    Prenyl donors, reductant, magnesium and lipophilic statins
    limitations
    In-vitro substrate and assay context. Residual microsomal magnesium prevents concluding that synthesis is magnesium-independent; no human supplementation effect was tested.
    nutrient_topic
    Vitamin K2 research collection; topical membership is not evidence of a direct dietary effect. · Vitamin K2 / menaquinone family
    organism
    Human UBIAD1 expressed in Sf9 insect cells
    plain_language
    MK-4 production needs a side-chain donor as well as the vitamin K ring.
    primary_references
    [k2-p25874989] Functional characterization of the vitamin K2 biosynthetic enzyme UBIAD1. (2015). https://pubmed.ncbi.nlm.nih.gov/25874989/ DOI: 10.1371/journal.pone.0125737
    tissue_or_cell_type
    Microsomal prenylation

    Vitamin K2: menaquinone forms, carboxylation, recycling and nutrient interactions (2026-09-17) · lines 201–212

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Microsomal enzyme assays and mutagenesis · source_derived_draft · unverified_draft

    ### k2-ggpp-sidechain UBIAD1 synthesized MK-4 using GGPP as the isoprenyl side-chain source. Condition category: normal nutrient_topic: Vitamin K2 research collection; topical membership is not evidence of a direct dietary effect. plain_language: MK-4 production needs a side-chain donor as well as the vitamin K ring. organism: Human UBIAD1 expressed in Sf9 insect cells tissue_or_cell_type: Microsomal prenylation experimental_model: Microsomal enzyme assays and mutagenesis limitations: In-vitro substrate and assay context. Residual microsomal magnesium prevents concluding that synthesis is magnesium-independent; no human supplementation effect was tested. exposure: Prenyl donors, reductant, magnesium and lipophilic statins evidence_span: {"source_cache": "artifacts/k2-research/25874989.fulltext.txt", "locator": "Exact primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "bbd73607ba2570aa383c81c189b29dd19f1cbd7bf7acdd8343ecf3ee7dc5faf8", "start_char": 24159, "end_char": 24399, "text_sha256": "b680e2031495b2fee24a56c799e8cb2f64bbac3c6a3cb0d33592051f2cf41b9f"} [k2-p25874989] Functional characterization of the vitamin K2 biosynthetic enzyme UBIAD1. (2015). https://pubmed.ncbi.nlm.nih.gov/25874989/ DOI: 10.1371/journal.pone.0125737
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Mevastatin inhibited Rho membrane translocation by about 60 percent and Rho GTP-binding activity by about 78 percent, both reversed by geranylgeranyl diphosphate but not by farnesyl diphosphate.

    Mevastatin → Rho membrane translocation and GTP binding source_derived_draftungraded
    Experimental context and source evidence
    duration
    Not stated here
    evidence_access
    Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
    experimental_model
    Human endothelial cells
    exposure
    Mevastatin with or without geranylgeranyl diphosphate or farnesyl diphosphate
    limitations
    Measured for Rho as a group by immunoblot and GTP-gamma-S binding, not resolved to individual Rho family members.
    organism
    Human endothelial cells
    plain_language
    Mevastatin inhibited Rho membrane translocation by about 60 percent and Rho GTP-binding activity by about 78 percent, both reversed by geranylgeranyl diphosphate but not by farnesyl diphosphate.
    primary_references
    Post-transcriptional regulation of endothelial nitric oxide synthase mRNA stability by Rho GTPase. (1998). https://pubmed.ncbi.nlm.nih.gov/9727051/ DOI: 10.1074/jbc.273.37.24266
    route
    In vitro
    tissue
    Rho GTPase membrane localisation and nucleotide binding

    Atorvastatin: mechanism of action from target occupancy to isoprenoids, transport, muscle and metabolism (2026-09-22) · lines 78–87

    Original AI-assisted curation of twelve primary studies resolved by PubMed title search and cross-checked against live PubMed metadata. Findings obtained with mevastatin, simvastatin or the statin class are recorded against those subjects. Study-specific citations, doses, negative findings and limitations retained. Not publisher full text. · supports · · source_derived_draft · unverified_draft

    ## statin-inhibits-rho-membrane-translocation Mevastatin inhibited Rho membrane translocation by about 60 percent and Rho GTP-binding activity by about 78 percent, both reversed by geranylgeranyl diphosphate but not by farnesyl diphosphate. Model/species: Human endothelial cells Tissue/system: Rho GTPase membrane localisation and nucleotide binding Exposure: Mevastatin with or without geranylgeranyl diphosphate or farnesyl diphosphate Route: In vitro Duration: Not stated here Limits: Measured for Rho as a group by immunoblot and GTP-gamma-S binding, not resolved to individual Rho family members. Primary reference: Post-transcriptional regulation of endothelial nitric oxide synthase mRNA stability by Rho GTPase. (1998). https://pubmed.ncbi.nlm.nih.gov/9727051/ DOI: 10.1074/jbc.273.37.24266 Access: Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
    Complete structured claim and evidence

  2. Mevastatin increased endothelial nitric oxide synthase messenger RNA by about 305 percent and protein by about 180 percent in human endothelial cells.

    Mevastatin → Human endothelial nitric oxide synthase / eNOS / NOS3 source_derived_draftungraded
    Experimental context and source evidence
    duration
    Not stated here
    evidence_access
    Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
    experimental_model
    Human endothelial cells
    exposure
    Mevastatin 1 to 10 micromolar
    limitations
    The statin tested was mevastatin, not atorvastatin, and this is an expression change in cultured cells rather than a vascular outcome.
    organism
    Human endothelial cells
    plain_language
    Mevastatin increased endothelial nitric oxide synthase messenger RNA by about 305 percent and protein by about 180 percent in human endothelial cells.
    primary_references
    Post-transcriptional regulation of endothelial nitric oxide synthase mRNA stability by Rho GTPase. (1998). https://pubmed.ncbi.nlm.nih.gov/9727051/ DOI: 10.1074/jbc.273.37.24266
    route
    In vitro
    tissue
    Endothelial nitric oxide synthase expression

    Atorvastatin: mechanism of action from target occupancy to isoprenoids, transport, muscle and metabolism (2026-09-22) · lines 56–65

    Original AI-assisted curation of twelve primary studies resolved by PubMed title search and cross-checked against live PubMed metadata. Findings obtained with mevastatin, simvastatin or the statin class are recorded against those subjects. Study-specific citations, doses, negative findings and limitations retained. Not publisher full text. · supports · · source_derived_draft · unverified_draft

    ## statin-raises-endothelial-nos Mevastatin increased endothelial nitric oxide synthase messenger RNA by about 305 percent and protein by about 180 percent in human endothelial cells. Model/species: Human endothelial cells Tissue/system: Endothelial nitric oxide synthase expression Exposure: Mevastatin 1 to 10 micromolar Route: In vitro Duration: Not stated here Limits: The statin tested was mevastatin, not atorvastatin, and this is an expression change in cultured cells rather than a vascular outcome. Primary reference: Post-transcriptional regulation of endothelial nitric oxide synthase mRNA stability by Rho GTPase. (1998). https://pubmed.ncbi.nlm.nih.gov/9727051/ DOI: 10.1074/jbc.273.37.24266 Access: Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
    Complete structured claim and evidence

  3. Statin treatment reduced host protein prenylation including prenylation of Rho GTPases, and reduced respiratory syncytial virus infection in vitro through combined cholesterol and isoprenoid effects.

    Statin therapy as a drug class → Prenylation of Rho-family GTPases source_derived_draftungraded
    Experimental context and source evidence
    duration
    Not stated here
    evidence_access
    Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
    experimental_model
    Live-cell high-content screen in human cell culture
    exposure
    Statins, and separately perillyl alcohol as a geranylgeranyltransferase inhibitor
    limitations
    The screen tested statins as a class without attributing the result to atorvastatin, and respiratory syncytial virus infection itself globally upregulated prenylation, so the baseline was not a resting cell.
    organism
    Live-cell high-content screen in human cell culture
    plain_language
    Statin treatment reduced host protein prenylation including prenylation of Rho GTPases, and reduced respiratory syncytial virus infection in vitro through combined cholesterol and isoprenoid effects.
    primary_references
    Statin-mediated disruption of Rho GTPase prenylation and activity inhibits respiratory syncytial virus infection. (2021). https://pubmed.ncbi.nlm.nih.gov/34716403/ DOI: 10.1038/s42003-021-02754-2
    route
    In vitro
    tissue
    Host protein prenylation and virus production

    Atorvastatin: mechanism of action from target occupancy to isoprenoids, transport, muscle and metabolism (2026-09-22) · lines 89–98

    Original AI-assisted curation of twelve primary studies resolved by PubMed title search and cross-checked against live PubMed metadata. Findings obtained with mevastatin, simvastatin or the statin class are recorded against those subjects. Study-specific citations, doses, negative findings and limitations retained. Not publisher full text. · supports · · source_derived_draft · unverified_draft

    ## statin-reduces-rho-gtpase-prenylation Statin treatment reduced host protein prenylation including prenylation of Rho GTPases, and reduced respiratory syncytial virus infection in vitro through combined cholesterol and isoprenoid effects. Model/species: Live-cell high-content screen in human cell culture Tissue/system: Host protein prenylation and virus production Exposure: Statins, and separately perillyl alcohol as a geranylgeranyltransferase inhibitor Route: In vitro Duration: Not stated here Limits: The screen tested statins as a class without attributing the result to atorvastatin, and respiratory syncytial virus infection itself globally upregulated prenylation, so the baseline was not a resting cell. Primary reference: Statin-mediated disruption of Rho GTPase prenylation and activity inhibits respiratory syncytial virus infection. (2021). https://pubmed.ncbi.nlm.nih.gov/34716403/ DOI: 10.1038/s42003-021-02754-2 Access: Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
    Complete structured claim and evidence

  4. Mutational analysis assigned conserved domain IV to magnesium/isoprenyl-side-chain interactions.

    Human UBIAD1 prenyltransferase → Mg2+ source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/k2-research/25874989.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "a3eb5f4c56ca7a3e70a32c020bba09f4fec5e91048b13a188017bf221f713a68", "start_char": 0, "end_char": 1777, "text_sha256": "a3eb5f4c56ca7a3e70a32c020bba09f4fec5e91048b13a188017bf221f713a68"}
    experimental_model
    Microsomal enzyme assays and mutagenesis
    exposure
    Prenyl donors, reductant, magnesium and lipophilic statins
    limitations
    In-vitro substrate and assay context. Residual microsomal magnesium prevents concluding that synthesis is magnesium-independent; no human supplementation effect was tested.
    nutrient_topic
    Vitamin K2 research collection; topical membership is not evidence of a direct dietary effect. · Vitamin K2 / menaquinone family
    organism
    Human UBIAD1 expressed in Sf9 insect cells
    plain_language
    Magnesium-related enzyme chemistry is recorded separately from a claim that oral magnesium improves K2 status.
    primary_references
    [k2-p25874989] Functional characterization of the vitamin K2 biosynthetic enzyme UBIAD1. (2015). https://pubmed.ncbi.nlm.nih.gov/25874989/ DOI: 10.1371/journal.pone.0125737
    tissue_or_cell_type
    Microsomal prenylation

    Vitamin K2: menaquinone forms, carboxylation, recycling and nutrient interactions (2026-09-17) · lines 214–225

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Microsomal enzyme assays and mutagenesis · source_derived_draft · unverified_draft

    ### k2-ubiad1-magnesium-site Mutational analysis assigned conserved domain IV to magnesium/isoprenyl-side-chain interactions. Condition category: normal nutrient_topic: Vitamin K2 research collection; topical membership is not evidence of a direct dietary effect. plain_language: Magnesium-related enzyme chemistry is recorded separately from a claim that oral magnesium improves K2 status. organism: Human UBIAD1 expressed in Sf9 insect cells tissue_or_cell_type: Microsomal prenylation experimental_model: Microsomal enzyme assays and mutagenesis limitations: In-vitro substrate and assay context. Residual microsomal magnesium prevents concluding that synthesis is magnesium-independent; no human supplementation effect was tested. exposure: Prenyl donors, reductant, magnesium and lipophilic statins evidence_span: {"source_cache": "artifacts/k2-research/25874989.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "a3eb5f4c56ca7a3e70a32c020bba09f4fec5e91048b13a188017bf221f713a68", "start_char": 0, "end_char": 1777, "text_sha256": "a3eb5f4c56ca7a3e70a32c020bba09f4fec5e91048b13a188017bf221f713a68"} [k2-p25874989] Functional characterization of the vitamin K2 biosynthetic enzyme UBIAD1. (2015). https://pubmed.ncbi.nlm.nih.gov/25874989/ DOI: 10.1371/journal.pone.0125737
    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