Component

11-cis-retinol

11-cis retinoid alcohol; visual-cycle intermediate distinct from retinaldehyde.

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 acts on it

  1. CRALBP coexpression increased 11-cis-retinol production approximately threefold in homogenates of cells stably expressing chicken DES1.

    Cellular retinaldehyde-binding protein / CRALBP → 11-cis-retinol source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    false
    evidence_location
    Figure 5b
    experimental_model
    Chicken CRALBP transfection into stable DES1-expressing 293T cells
    exposure
    All-trans-retinol substrate; CRALBP plasmid versus empty-vector comparison.
    limitations
    An assay yield effect does not prove physiological transport or human supplementation benefit.
    nutrient
    Vitamin A · Vitamin A
    nutrient_topic
    Vitamin A expansion research collection; topical membership is not evidence of a direct dietary effect. · Vitamin A
    organism
    Gallus gallus proteins in Homo sapiens cells
    plain_language
    The binding protein shifted the measured output toward the visual-cycle alcohol.
    primary_references
    [vav-kaylor2013] Identification of DES1 as a vitamin A isomerase in Müller glial cells of the retina. (2013). https://pubmed.ncbi.nlm.nih.gov/23143414/ DOI: 10.1038/nchembio.1114
    tissue_or_cell_type
    cell homogenates

    Vitamin A expansion: reproduction, light-driven vision and shared mechanisms (2026-09-17) · lines 573–586

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Chicken CRALBP transfection into stable DES1-expressing 293T cells · source_derived_draft · unverified_draft

    ### vae-cralbp-des1-isomer-yield CRALBP coexpression increased 11-cis-retinol production approximately threefold in homogenates of cells stably expressing chicken DES1. Condition category: normal nutrient_topic: Vitamin A expansion research collection; topical membership is not evidence of a direct dietary effect. plain_language: The binding protein shifted the measured output toward the visual-cycle alcohol. organism: Gallus gallus proteins in Homo sapiens cells tissue_or_cell_type: cell homogenates experimental_model: Chicken CRALBP transfection into stable DES1-expressing 293T cells limitations: An assay yield effect does not prove physiological transport or human supplementation benefit. exposure: All-trans-retinol substrate; CRALBP plasmid versus empty-vector comparison. cross_nutrient: false evidence_location: Figure 5b nutrient: Vitamin A [vav-kaylor2013] Identification of DES1 as a vitamin A isomerase in Müller glial cells of the retina. (2013). https://pubmed.ncbi.nlm.nih.gov/23143414/ DOI: 10.1038/nchembio.1114
    Complete structured claim and evidence

  2. Homogenates of DES1-expressing HEK293T cells formed 11-cis-retinol from all-trans-retinol, alongside more abundant alternative cis isomers.

    Dihydroceramide desaturase 1 / DES1 → 11-cis-retinol source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    false
    evidence_location
    Figure 3a-d; Results: DES1 catalyzes equilibrium isomerization
    experimental_model
    Recombinant human DES1 expression; HPLC isomer analysis
    exposure
    Retinol isomerase assays in darkness at 37 degrees Celsius.
    limitations
    Activity in homogenates does not establish its quantitative contribution or necessity in an intact visual cycle.
    nutrient
    Vitamin A · Vitamin A
    nutrient_topic
    Vitamin A expansion research collection; topical membership is not evidence of a direct dietary effect. · Vitamin A
    organism
    Homo sapiens protein/cells
    plain_language
    DES1-associated activity made some 11-cis-retinol in biochemical assays.
    primary_references
    [vav-kaylor2013] Identification of DES1 as a vitamin A isomerase in Müller glial cells of the retina. (2013). https://pubmed.ncbi.nlm.nih.gov/23143414/ DOI: 10.1038/nchembio.1114
    tissue_or_cell_type
    HEK293T homogenates

    Vitamin A expansion: reproduction, light-driven vision and shared mechanisms (2026-09-17) · lines 558–571

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant human DES1 expression; HPLC isomer analysis · source_derived_draft · unverified_draft

    ### vae-des1-retinol-isomerization Homogenates of DES1-expressing HEK293T cells formed 11-cis-retinol from all-trans-retinol, alongside more abundant alternative cis isomers. Condition category: normal nutrient_topic: Vitamin A expansion research collection; topical membership is not evidence of a direct dietary effect. plain_language: DES1-associated activity made some 11-cis-retinol in biochemical assays. organism: Homo sapiens protein/cells tissue_or_cell_type: HEK293T homogenates experimental_model: Recombinant human DES1 expression; HPLC isomer analysis limitations: Activity in homogenates does not establish its quantitative contribution or necessity in an intact visual cycle. exposure: Retinol isomerase assays in darkness at 37 degrees Celsius. cross_nutrient: false evidence_location: Figure 3a-d; Results: DES1 catalyzes equilibrium isomerization nutrient: Vitamin A [vav-kaylor2013] Identification of DES1 as a vitamin A isomerase in Müller glial cells of the retina. (2013). https://pubmed.ncbi.nlm.nih.gov/23143414/ DOI: 10.1038/nchembio.1114
    Complete structured claim and evidence

  3. DES1-targeted siRNA reduced 11-cis-retinol formation from all-trans-retinol in homogenates of primary chicken Müller cultures compared with nonsilencing RNA.

    DES1 siRNA reduction → 11-cis-retinol source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    cross_nutrient
    false
    evidence_location
    Supplementary Figure 8; Results: RNAi knockdown
    experimental_model
    Targeted RNA interference with nonsilencing control
    exposure
    Approximately 50% DES1 expression reduction; retinol-substrate homogenate assay.
    limitations
    Neither complete gene deletion nor a physiological necessity test in an intact retina.
    nutrient
    Vitamin A · Vitamin A
    nutrient_topic
    Vitamin A expansion research collection; topical membership is not evidence of a direct dietary effect. · Vitamin A
    organism
    Gallus gallus
    plain_language
    Reducing DES1 lowered the culture preparation’s isomerase output.
    primary_references
    [vav-kaylor2013] Identification of DES1 as a vitamin A isomerase in Müller glial cells of the retina. (2013). https://pubmed.ncbi.nlm.nih.gov/23143414/ DOI: 10.1038/nchembio.1114
    tissue_or_cell_type
    primary Müller cultures
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Vitamin A expansion: reproduction, light-driven vision and shared mechanisms (2026-09-17) · lines 588–601

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Targeted RNA interference with nonsilencing control · source_derived_draft · unverified_draft

    ### vae-des1-sirna-isomerization DES1-targeted siRNA reduced 11-cis-retinol formation from all-trans-retinol in homogenates of primary chicken Müller cultures compared with nonsilencing RNA. Condition category: machinery_impairment nutrient_topic: Vitamin A expansion research collection; topical membership is not evidence of a direct dietary effect. plain_language: Reducing DES1 lowered the culture preparation’s isomerase output. organism: Gallus gallus tissue_or_cell_type: primary Müller cultures experimental_model: Targeted RNA interference with nonsilencing control limitations: Neither complete gene deletion nor a physiological necessity test in an intact retina. exposure: Approximately 50% DES1 expression reduction; retinol-substrate homogenate assay. cross_nutrient: false evidence_location: Supplementary Figure 8; Results: RNAi knockdown nutrient: Vitamin A [vav-kaylor2013] Identification of DES1 as a vitamin A isomerase in Müller glial cells of the retina. (2013). https://pubmed.ncbi.nlm.nih.gov/23143414/ DOI: 10.1038/nchembio.1114
    Complete structured claim and evidence

  4. Recombinant RPE65 catalyzed conversion of all-trans-retinyl esters to 11-cis-retinol in visual-cycle reconstitution.

    RPE65 retinoid isomerohydrolase → 11-cis-retinol source_derived_draftungraded
    Experimental context and source evidence
    experimental_model
    Recombinant enzyme reconstitution
    limitations
    Production of the aldehyde requires a subsequent oxidation step.
    nutrient_topic
    Vitamin A research collection; topical membership is not evidence of a direct dietary effect. · Vitamin A
    organism
    QBI-293A human cells and COS-1 monkey cells
    plain_language
    RPE65 converts the ester pool into the cis alcohol needed for chromophore renewal.
    primary_references
    [moiseyev-2005] RPE65 is the isomerohydrolase in the retinoid visual cycle (2005). https://pubmed.ncbi.nlm.nih.gov/16116091/ DOI: 10.1073/pnas.0503460102
    tissue_or_cell_type
    RPE visual-cycle biochemical model

    Vitamin A: forms, mechanisms, deficiency and excess (2026-09-17) · lines 666–675

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

    ### a-vision-rpe65-isomerization Recombinant RPE65 catalyzed conversion of all-trans-retinyl esters to 11-cis-retinol in visual-cycle reconstitution. Condition category: normal nutrient_topic: Vitamin A research collection; topical membership is not evidence of a direct dietary effect. plain_language: RPE65 converts the ester pool into the cis alcohol needed for chromophore renewal. organism: QBI-293A human cells and COS-1 monkey cells tissue_or_cell_type: RPE visual-cycle biochemical model experimental_model: Recombinant enzyme reconstitution limitations: Production of the aldehyde requires a subsequent oxidation step. [moiseyev-2005] RPE65 is the isomerohydrolase in the retinoid visual cycle (2005). https://pubmed.ncbi.nlm.nih.gov/16116091/ DOI: 10.1073/pnas.0503460102
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. HEK293T cells coexpressing bovine RGR and RDH10 generated more 11-cis-retinol from all-trans-retinol during illumination than cells expressing either protein alone.

    Retinal G protein-coupled receptor / RGR opsin → Retinol dehydrogenase 10 / RDH10 source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    false
    evidence_location
    Figure 1A; STAR Methods: Expression of RGR and RDH10
    experimental_model
    Recombinant bovine RGR/RDH10 coexpression
    exposure
    30-minute illumination; 5 micromolar all-trans-retinol; assay medium contained 250 micromolar NADPH.
    limitations
    Coupled output does not prove every proposed intermediate reaction or RDH10 necessity in intact retina. Added NADPH is an assay component, not a demonstrated dietary requirement.
    nutrient
    Vitamin A · Vitamin A
    nutrient_topic
    Vitamin A expansion research collection; topical membership is not evidence of a direct dietary effect. · Vitamin A
    organism
    Bos taurus proteins in Homo sapiens cells
    plain_language
    The two proteins supported light-dependent retinol recycling together in cultured cells.
    primary_references
    [vav-morshedian2019] Light-Driven Regeneration of Cone Visual Pigments through a Mechanism Involving RGR Opsin in Müller Glial Cells. (2019). https://pubmed.ncbi.nlm.nih.gov/31056353/ DOI: 10.1016/j.neuron.2019.04.004
    tissue_or_cell_type
    HEK293T culture

    Vitamin A expansion: reproduction, light-driven vision and shared mechanisms (2026-09-17) · lines 468–481

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant bovine RGR/RDH10 coexpression · source_derived_draft · unverified_draft

    ### vae-rgr-rdh10-coupled-retinol HEK293T cells coexpressing bovine RGR and RDH10 generated more 11-cis-retinol from all-trans-retinol during illumination than cells expressing either protein alone. Condition category: normal nutrient_topic: Vitamin A expansion research collection; topical membership is not evidence of a direct dietary effect. plain_language: The two proteins supported light-dependent retinol recycling together in cultured cells. organism: Bos taurus proteins in Homo sapiens cells tissue_or_cell_type: HEK293T culture experimental_model: Recombinant bovine RGR/RDH10 coexpression limitations: Coupled output does not prove every proposed intermediate reaction or RDH10 necessity in intact retina. Added NADPH is an assay component, not a demonstrated dietary requirement. exposure: 30-minute illumination; 5 micromolar all-trans-retinol; assay medium contained 250 micromolar NADPH. cross_nutrient: false evidence_location: Figure 1A; STAR Methods: Expression of RGR and RDH10 nutrient: Vitamin A [vav-morshedian2019] Light-Driven Regeneration of Cone Visual Pigments through a Mechanism Involving RGR Opsin in Müller Glial Cells. (2019). https://pubmed.ncbi.nlm.nih.gov/31056353/ DOI: 10.1016/j.neuron.2019.04.004
    Complete structured claim and evidence

  2. Bovine RDH5 expressed in COS cells oxidized 11-cis-retinol using NAD+; NADP did not support the tested activity.

    11-cis-retinol dehydrogenase / RDH5 → 11-cis-retinal source_derived_draftungraded
    Experimental context and source evidence
    experimental_model
    Recombinant p32/RDH5 activity assay
    limitations
    Cofactor specificity is biochemical; no niacin-deficiency phenotype was tested.
    nutrient_topic
    Vitamin A research collection; topical membership is not evidence of a direct dietary effect. · Vitamin A
    organism
    Bos taurus protein; COS cells
    plain_language
    RDH5 oxidizes the cis alcohol into the visual chromophore.
    primary_references
    [simon-1995] The retinal pigment epithelial-specific 11-cis retinol dehydrogenase belongs to the family of short chain alcohol dehydrogenases (1995). https://pubmed.ncbi.nlm.nih.gov/7836368/ DOI: 10.1074/jbc.270.3.1107
    tissue_or_cell_type
    RPE-derived enzyme

    Vitamin A: forms, mechanisms, deficiency and excess (2026-09-17) · lines 723–732

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant p32/RDH5 activity assay · source_derived_draft · unverified_draft

    ### a-vision-rdh5-oxidation Bovine RDH5 expressed in COS cells oxidized 11-cis-retinol using NAD+; NADP did not support the tested activity. Condition category: normal nutrient_topic: Vitamin A research collection; topical membership is not evidence of a direct dietary effect. plain_language: RDH5 oxidizes the cis alcohol into the visual chromophore. organism: Bos taurus protein; COS cells tissue_or_cell_type: RPE-derived enzyme experimental_model: Recombinant p32/RDH5 activity assay limitations: Cofactor specificity is biochemical; no niacin-deficiency phenotype was tested. [simon-1995] The retinal pigment epithelial-specific 11-cis retinol dehydrogenase belongs to the family of short chain alcohol dehydrogenases (1995). https://pubmed.ncbi.nlm.nih.gov/7836368/ DOI: 10.1074/jbc.270.3.1107
    Complete structured claim and evidence

  3. FeSO4 restored chelator-inhibited RPE65 isomerohydrolase activity in bovine microsomes and recombinant assays; ferric salts did not.

    Ferrous iron → RPE65 retinoid isomerohydrolase source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    Iron availability at RPE65 enables formation of the cis-retinoid visual-cycle intermediate.
    experimental_model
    Chelation and metal rescue
    limitations
    This is enzyme-cofactor evidence, not a human iron-deficiency threshold.
    nutrient_topic
    Vitamin A research collection; topical membership is not evidence of a direct dietary effect. · Vitamin A
    organism
    Bos taurus; recombinant RPE65 in human 293A cells
    plain_language
    Ferrous iron is required for this vitamin A recycling enzyme.
    primary_references
    [moiseyev-2006] RPE65 is an iron(II)-dependent isomerohydrolase in the retinoid visual cycle (2006). https://pubmed.ncbi.nlm.nih.gov/16319067/ DOI: 10.1074/jbc.M508903200
    tissue_or_cell_type
    RPE microsomes and cultured-cell preparations

    Vitamin A: forms, mechanisms, deficiency and excess (2026-09-17) · lines 677–687

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Chelation and metal rescue · source_derived_draft · unverified_draft

    ### a-vision-rpe65-iron FeSO4 restored chelator-inhibited RPE65 isomerohydrolase activity in bovine microsomes and recombinant assays; ferric salts did not. Condition category: normal nutrient_topic: Vitamin A research collection; topical membership is not evidence of a direct dietary effect. plain_language: Ferrous iron is required for this vitamin A recycling enzyme. organism: Bos taurus; recombinant RPE65 in human 293A cells tissue_or_cell_type: RPE microsomes and cultured-cell preparations experimental_model: Chelation and metal rescue limitations: This is enzyme-cofactor evidence, not a human iron-deficiency threshold. cross_nutrient: Iron availability at RPE65 enables formation of the cis-retinoid visual-cycle intermediate. [moiseyev-2006] RPE65 is an iron(II)-dependent isomerohydrolase in the retinoid visual cycle (2006). https://pubmed.ncbi.nlm.nih.gov/16319067/ DOI: 10.1074/jbc.M508903200
    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.

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