Component

Myo-inositol 1,4-bisphosphate

Context-specific entity; species, compartment and exposure are stated on each claim.

5 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. Submillimolar lithium chloride inhibited rat RnPIP hydrolysis of both PAP and Ins(1,4)P2.

    Lithium ion (Li+) → Rat bisphosphate nucleotidase 1 / RnPIP source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Rat recombinant enzyme; calcium also inhibited activity.
    limitations
    Not a quantitative human exposure-to-organ-injury model.
    nutrient_topic
    Lithium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Lithium
    plain_language
    One lithium-sensitive enzyme connects two metabolic branches.
    primary_references
    A novel mammalian lithium-sensitive enzyme with a dual enzymatic activity, 3'-phosphoadenosine 5'-phosphate phosphatase and inositol-polyphosphate 1-phosphatase. · 1999 · https://pubmed.ncbi.nlm.nih.gov/10347153/ · DOI 10.1074/jbc.274.23.16034

    Lithium: metal-sensitive enzymes, transport and cross-nutrient mechanisms (2026-09-19) · lines 120–126

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Rat recombinant enzyme; calcium also inhibited activity. · source_derived_draft · unverified_draft

    ## lithium-bpnt1-lithium One lithium-sensitive enzyme connects two metabolic branches. Submillimolar lithium chloride inhibited rat RnPIP hydrolysis of both PAP and Ins(1,4)P2. Model: Rat recombinant enzyme; calcium also inhibited activity. Limitations: Not a quantitative human exposure-to-organ-injury model. Evidence access: Primary abstract A novel mammalian lithium-sensitive enzyme with a dual enzymatic activity, 3'-phosphoadenosine 5'-phosphate phosphatase and inositol-polyphosphate 1-phosphatase. · 1999 · https://pubmed.ncbi.nlm.nih.gov/10347153/ · DOI 10.1074/jbc.274.23.16034
    Complete structured claim and evidence

  2. Cloned rat RnPIP hydrolyzed PAP and Ins(1,4)P2 in magnesium-dependent reactions.

    Rat bisphosphate nucleotidase 1 / RnPIP → 3-prime-Phosphoadenosine-5-prime-phosphate / PAP source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Cloned rat enzyme; biochemical substrate assays.
    limitations
    The paper proposes consequences for sulfotransferases/RNA processing; those downstream effects were not all tested.
    nutrient_topic
    Lithium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Lithium
    plain_language
    Clearing a sulfur-pathway by-product uses another metal-dependent enzyme.
    primary_references
    A novel mammalian lithium-sensitive enzyme with a dual enzymatic activity, 3'-phosphoadenosine 5'-phosphate phosphatase and inositol-polyphosphate 1-phosphatase. · 1999 · https://pubmed.ncbi.nlm.nih.gov/10347153/ · DOI 10.1074/jbc.274.23.16034

    Lithium: metal-sensitive enzymes, transport and cross-nutrient mechanisms (2026-09-19) · lines 112–118

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Cloned rat enzyme; biochemical substrate assays. · source_derived_draft · unverified_draft

    ## lithium-bpnt1-substrate Clearing a sulfur-pathway by-product uses another metal-dependent enzyme. Cloned rat RnPIP hydrolyzed PAP and Ins(1,4)P2 in magnesium-dependent reactions. Model: Cloned rat enzyme; biochemical substrate assays. Limitations: The paper proposes consequences for sulfotransferases/RNA processing; those downstream effects were not all tested. Evidence access: Primary abstract A novel mammalian lithium-sensitive enzyme with a dual enzymatic activity, 3'-phosphoadenosine 5'-phosphate phosphatase and inositol-polyphosphate 1-phosphatase. · 1999 · https://pubmed.ncbi.nlm.nih.gov/10347153/ · DOI 10.1074/jbc.274.23.16034
    Complete structured claim and evidence

  3. Lithium treatment increased mono/bis-phosphorylated inositol species in COS-7 cells, consistent with inhibited recycling.

    Lithium ion (Li+) → Inositol monophosphates source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text
    experimental_model
    Monkey COS-7 cells; 10 mM LiCl, 24-hour metabolite assay.
    limitations
    Combined IP1–2 measurement; this exposure exceeds typical clinical serum concentrations.
    nutrient_topic
    Lithium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Lithium
    plain_language
    Blocking recycling lets upstream material accumulate.
    primary_references
    Lithium induces autophagy by inhibiting inositol monophosphatase. · 2005 · https://pubmed.ncbi.nlm.nih.gov/16186256/ · DOI 10.1083/jcb.200504035

    Lithium: metal-sensitive enzymes, transport and cross-nutrient mechanisms (2026-09-19) · lines 72–78

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Monkey COS-7 cells; 10 mM LiCl, 24-hour metabolite assay. · source_derived_draft · unverified_draft

    ## lithium-inositol-phosphate-accumulation Blocking recycling lets upstream material accumulate. Lithium treatment increased mono/bis-phosphorylated inositol species in COS-7 cells, consistent with inhibited recycling. Model: Monkey COS-7 cells; 10 mM LiCl, 24-hour metabolite assay. Limitations: Combined IP1–2 measurement; this exposure exceeds typical clinical serum concentrations. Evidence access: Primary full text Lithium induces autophagy by inhibiting inositol monophosphatase. · 2005 · https://pubmed.ncbi.nlm.nih.gov/16186256/ · DOI 10.1083/jcb.200504035
    Complete structured claim and evidence

  4. Purified calf-brain INPP1 showed cooperative magnesium dependence, with half-maximal stimulation near 0.3 mM.

    Mg2+ → Bovine inositol polyphosphate 1-phosphatase / INPP1 source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Calf-brain enzyme purification and kinetics.
    limitations
    In-vitro cofactor concentration is not a human blood target.
    nutrient_topic
    Lithium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Lithium
    plain_language
    A second recycling enzyme also depends on magnesium.
    primary_references
    Inositol polyphosphate 1-phosphatase from calf brain. Purification and inhibition by Li+, Ca2+, and Mn2+. · 1987 · https://pubmed.ncbi.nlm.nih.gov/2824473/

    Lithium: metal-sensitive enzymes, transport and cross-nutrient mechanisms (2026-09-19) · lines 48–54

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Calf-brain enzyme purification and kinetics. · source_derived_draft · unverified_draft

    ## lithium-inpp1-magnesium A second recycling enzyme also depends on magnesium. Purified calf-brain INPP1 showed cooperative magnesium dependence, with half-maximal stimulation near 0.3 mM. Model: Calf-brain enzyme purification and kinetics. Limitations: In-vitro cofactor concentration is not a human blood target. Evidence access: Primary abstract Inositol polyphosphate 1-phosphatase from calf brain. Purification and inhibition by Li+, Ca2+, and Mn2+. · 1987 · https://pubmed.ncbi.nlm.nih.gov/2824473/
    Complete structured claim and evidence

  5. Lithium inhibited bovine INPP1 differently by substrate: Ki about 6 mM for Ins(1,4)P2 versus 0.5–1 mM for Ins(1,3,4)P3.

    Lithium ion (Li+) → Bovine inositol polyphosphate 1-phosphatase / INPP1 source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Purified calf-brain INPP1.
    limitations
    Do not substitute signaling IP3, Ins(1,4,5)P3, for the distinct Ins(1,3,4)P3 substrate.
    nutrient_topic
    Lithium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Lithium
    plain_language
    The same enzyme can respond differently depending on its substrate.
    primary_references
    Inositol polyphosphate 1-phosphatase from calf brain. Purification and inhibition by Li+, Ca2+, and Mn2+. · 1987 · https://pubmed.ncbi.nlm.nih.gov/2824473/

    Lithium: metal-sensitive enzymes, transport and cross-nutrient mechanisms (2026-09-19) · lines 56–62

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Purified calf-brain INPP1. · source_derived_draft · unverified_draft

    ## lithium-inpp1-substrate-specific The same enzyme can respond differently depending on its substrate. Lithium inhibited bovine INPP1 differently by substrate: Ki about 6 mM for Ins(1,4)P2 versus 0.5–1 mM for Ins(1,3,4)P3. Model: Purified calf-brain INPP1. Limitations: Do not substitute signaling IP3, Ins(1,4,5)P3, for the distinct Ins(1,3,4)P3 substrate. Evidence access: Primary abstract Inositol polyphosphate 1-phosphatase from calf brain. Purification and inhibition by Li+, Ca2+, and Mn2+. · 1987 · https://pubmed.ncbi.nlm.nih.gov/2824473/
    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