Component

Human cyclophilin A / PPIA

The cytosolic peptidyl-prolyl cis-trans isomerase that cyclosporine binds. Distinct from the mitochondrial matrix isomerase in this collection and from the ledger's PPIF node.

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

What it acts on

  1. Cyclophilin without cyclosporin A bound did not bind or inhibit calcineurin, and neither did FKBP alone, FKBP with rapamycin, or FKBP with the inactive analogue 506BD.

    Human cyclophilin A / PPIA → Calcineurin 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
    Purified mammalian proteins
    exposure
    Free cyclophilin; free FKBP; FKBP-rapamycin; FKBP-506BD
    limitations
    This is the control set that makes the complex the active species. It is recorded as a measured null rather than as an absence of evidence.
    organism
    Purified mammalian proteins
    plain_language
    Cyclophilin without cyclosporin A bound did not bind or inhibit calcineurin, and neither did FKBP alone, FKBP with rapamycin, or FKBP with the inactive analogue 506BD.
    primary_references
    Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexes. (1991). https://pubmed.ncbi.nlm.nih.gov/1715244/ DOI: 10.1016/0092-8674(91)90124-h
    route
    In vitro
    tissue
    Calcineurin phosphatase activity

    Cyclosporine: the complex that inhibits calcineurin, a second cyclophilin, and the transport step that decides exposure (2026-09-23) · lines 58–58

    Original AI-assisted curation of seven primary studies resolved by PubMed title search, with every abstract read and all DOIs cross-checked against live PubMed metadata on 2026-09-23. No reference carries a recorded retraction, erratum or expression of concern. Each of the seven is a separate laboratory and each carries its own lineage key, so none of them can be counted twice as independent support. Study-specific concentrations, kinetic constants and limitations retained. Not publisher full text. · supports · Purified mammalian proteins · source_derived_draft · unverified_draft

    Cyclophilin without cyclosporin A bound did not bind or inhibit calcineurin, and neither did FKBP alone, FKBP with rapamycin, or FKBP with the inactive analogue 506BD.
    Complete structured claim and evidence

What acts on it

  1. The immediate intracellular receptor of cyclosporin A is cyclophilin, a peptidyl-prolyl cis-trans isomerase, and drug binding inhibits that isomerase activity.

    Cyclosporine → Human cyclophilin A / PPIA 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 and mammalian immunophilin biochemistry
    exposure
    Cyclosporin A
    limitations
    The report states that inhibition of isomerase activity is not what produces the drug's effect; analysis of cyclosporin-resistant yeast mutants and other isomerase inhibitors pointed to an inhibitory drug-isomerase complex instead. Binding is recorded here without a direction, because binding a protein is not by itself raising or lowering it.
    organism
    Human and mammalian immunophilin biochemistry
    plain_language
    The immediate intracellular receptor of cyclosporin A is cyclophilin, a peptidyl-prolyl cis-trans isomerase, and drug binding inhibits that isomerase activity.
    primary_references
    Nuclear association of a T-cell transcription factor blocked by FK-506 and cyclosporin A. (1991). https://pubmed.ncbi.nlm.nih.gov/1715516/ DOI: 10.1038/352803a0
    route
    In vitro
    tissue
    T-lymphocyte signalling

    Cyclosporine: the complex that inhibits calcineurin, a second cyclophilin, and the transport step that decides exposure (2026-09-23) · lines 14–14

    Original AI-assisted curation of seven primary studies resolved by PubMed title search, with every abstract read and all DOIs cross-checked against live PubMed metadata on 2026-09-23. No reference carries a recorded retraction, erratum or expression of concern. Each of the seven is a separate laboratory and each carries its own lineage key, so none of them can be counted twice as independent support. Study-specific concentrations, kinetic constants and limitations retained. Not publisher full text. · supports · Human and mammalian immunophilin biochemistry · source_derived_draft · unverified_draft

    The immediate intracellular receptor of cyclosporin A is cyclophilin, a peptidyl-prolyl cis-trans isomerase, and drug binding inhibits that isomerase activity.
    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