Component

Inositol monophosphates

Inositol monophosphates. Species, exposure and limitations are retained in each linked claim.

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. 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

  2. Human inositol monophosphatase hydrolyzes inositol monophosphates to regenerate free inositol.

    IMPA1 (human inositol monophosphatase 1) → Inositol monophosphates source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/inositol-research/1332026.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "57cfa39b1fe68149ad3a1ea25ede4c979db0586ef14c905cbe402fe3f70ce9e5", "start_char": 0, "end_char": 1147, "text_sha256": "57cfa39b1fe68149ad3a1ea25ede4c979db0586ef14c905cbe402fe3f70ce9e5"}
    experimental_model
    Human enzyme crystallography and catalytic characterization
    exposure
    Structural analysis of the inositol recycling enzyme
    limitations
    Structure does not show that extra substrate bypasses a genetic enzyme defect in patients.
    nutrient_topic
    Inositol research collection; topical membership is not evidence of a direct dietary effect. · Inositol (stereoisomer family)
    organism
    Homo sapiens
    plain_language
    A recycling step removes the last phosphate so the inositol ring can be reused.
    primary_references
    [ino-p1332026] Structure of inositol monophosphatase, the putative target of lithium therapy. (1992). https://pubmed.ncbi.nlm.nih.gov/1332026/ DOI: 10.1073/pnas.89.21.10031
    tissue_or_cell_type
    Purified inositol monophosphatase

    Inositol: synthesis, signaling, mineral interactions and conditional deficiency (2026-09-17) · lines 236–247

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human enzyme crystallography and catalytic characterization · source_derived_draft · unverified_draft

    ### ino-impa-recycling Human inositol monophosphatase hydrolyzes inositol monophosphates to regenerate free inositol. Condition category: normal nutrient_topic: Inositol research collection; topical membership is not evidence of a direct dietary effect. plain_language: A recycling step removes the last phosphate so the inositol ring can be reused. organism: Homo sapiens tissue_or_cell_type: Purified inositol monophosphatase experimental_model: Human enzyme crystallography and catalytic characterization limitations: Structure does not show that extra substrate bypasses a genetic enzyme defect in patients. exposure: Structural analysis of the inositol recycling enzyme evidence_span: {"source_cache": "artifacts/inositol-research/1332026.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "57cfa39b1fe68149ad3a1ea25ede4c979db0586ef14c905cbe402fe3f70ce9e5", "start_char": 0, "end_char": 1147, "text_sha256": "57cfa39b1fe68149ad3a1ea25ede4c979db0586ef14c905cbe402fe3f70ce9e5"} [ino-p1332026] Structure of inositol monophosphatase, the putative target of lithium therapy. (1992). https://pubmed.ncbi.nlm.nih.gov/1332026/ DOI: 10.1073/pnas.89.21.10031
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. The human IMPase study supported lithium binding at the second metal site in its catalytic model.

    Lithium ion (Li+) → IMPA1 (human inositol monophosphatase 1) source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Human enzyme kinetics, fluorescence and structural modeling.
    limitations
    Binding-site assignment is model-supported; treatment benefit is not established by enzyme inhibition.
    nutrient_topic
    Lithium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Lithium
    plain_language
    Lithium can interrupt the recycling step.
    primary_references
    Mechanism of inositol monophosphatase, the putative target of lithium therapy. · 1994 · https://pubmed.ncbi.nlm.nih.gov/8016062/ · DOI 10.1073/pnas.91.13.5766

    Lithium: metal-sensitive enzymes, transport and cross-nutrient mechanisms (2026-09-19) · lines 40–46

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human enzyme kinetics, fluorescence and structural modeling. · source_derived_draft · unverified_draft

    ## lithium-impa-lithium Lithium can interrupt the recycling step. The human IMPase study supported lithium binding at the second metal site in its catalytic model. Model: Human enzyme kinetics, fluorescence and structural modeling. Limitations: Binding-site assignment is model-supported; treatment benefit is not established by enzyme inhibition. Evidence access: Primary abstract Mechanism of inositol monophosphatase, the putative target of lithium therapy. · 1994 · https://pubmed.ncbi.nlm.nih.gov/8016062/ · DOI 10.1073/pnas.91.13.5766
    Complete structured claim and evidence

  2. Kinetics, modeling and mutagenesis supported a two-metal catalytic model for human inositol monophosphatase.

    Mg2+ → IMPA1 (human inositol monophosphatase 1) source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Human enzyme structural/kinetic study, including Mn, Zn and Mg titrations.
    limitations
    Historical mechanistic model; not a universal count for all conformations or family members.
    nutrient_topic
    Lithium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Lithium
    plain_language
    Inositol recycling uses metal-dependent chemistry.
    primary_references
    Mechanism of inositol monophosphatase, the putative target of lithium therapy. · 1994 · https://pubmed.ncbi.nlm.nih.gov/8016062/ · DOI 10.1073/pnas.91.13.5766

    Lithium: metal-sensitive enzymes, transport and cross-nutrient mechanisms (2026-09-19) · lines 32–38

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human enzyme structural/kinetic study, including Mn, Zn and Mg titrations. · source_derived_draft · unverified_draft

    ## lithium-impa-metal Inositol recycling uses metal-dependent chemistry. Kinetics, modeling and mutagenesis supported a two-metal catalytic model for human inositol monophosphatase. Model: Human enzyme structural/kinetic study, including Mn, Zn and Mg titrations. Limitations: Historical mechanistic model; not a universal count for all conformations or family members. Evidence access: Primary abstract Mechanism of inositol monophosphatase, the putative target of lithium therapy. · 1994 · https://pubmed.ncbi.nlm.nih.gov/8016062/ · DOI 10.1073/pnas.91.13.5766
    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