Component

Retinol dehydrogenase 10 / RDH10

Independent protein identity; organism and experimental state are specified on individual claims.

8 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. RDH10 coexpression increased DHRS3 retinaldehyde reductase activity even when RDH10 itself was catalytically inactive.

    Retinol dehydrogenase 10 / RDH10 → Dehydrogenase/reductase 3 / DHRS3 source_derived_draftungraded
    Experimental context and source evidence
    evidence_location
    Abstract
    experimental_model
    Human RDH10/DHRS3 coexpression in HEK293 and Sf9 cells, plus Dhrs3-null embryos.
    exposure
    Coexpression including inactive RDH10 constructs.
    limitations
    Does not identify an exact complex stoichiometry or require substrate channeling.
    nutrient_topic
    Vitamin A research collection; topical membership is not evidence of a direct dietary effect. · Vitamin A
    organism
    Homo sapiens recombinant proteins
    outcome
    RDH10 coexpression increased DHRS3 retinaldehyde reductase activity even when RDH10 itself was catalytically inactive.
    plain_language
    The partner enzyme also acts through a noncatalytic interaction.
    primary_references
    [va-adams-2014] The retinaldehyde reductase activity of DHRS3 is reciprocally activated by retinol dehydrogenase 10 to control retinoid homeostasis (2014). https://pmc.ncbi.nlm.nih.gov/articles/PMC4031538/ DOI: 10.1074/jbc.M114.552257
    tissue_or_cell_type
    Sf9 microsomes and HEK293 cells

    Vitamin A: forms, mechanisms, deficiency and excess (2026-09-17) · lines 531–543

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human RDH10/DHRS3 coexpression in HEK293 and Sf9 cells, plus Dhrs3-null embryos. · source_derived_draft · unverified_draft

    ### va-rdh10-activates-dhrs3 RDH10 coexpression increased DHRS3 retinaldehyde reductase activity even when RDH10 itself was catalytically inactive. Condition category: normal nutrient_topic: Vitamin A research collection; topical membership is not evidence of a direct dietary effect. plain_language: The partner enzyme also acts through a noncatalytic interaction. organism: Homo sapiens recombinant proteins tissue_or_cell_type: Sf9 microsomes and HEK293 cells experimental_model: Human RDH10/DHRS3 coexpression in HEK293 and Sf9 cells, plus Dhrs3-null embryos. limitations: Does not identify an exact complex stoichiometry or require substrate channeling. exposure: Coexpression including inactive RDH10 constructs. outcome: RDH10 coexpression increased DHRS3 retinaldehyde reductase activity even when RDH10 itself was catalytically inactive. evidence_location: Abstract [va-adams-2014] The retinaldehyde reductase activity of DHRS3 is reciprocally activated by retinol dehydrogenase 10 to control retinoid homeostasis (2014). https://pmc.ncbi.nlm.nih.gov/articles/PMC4031538/ DOI: 10.1074/jbc.M114.552257
    Complete structured claim and evidence

  2. Recombinant human RDH10 oxidized all-trans-retinol with NAD+ in microsomal assays.

    Retinol dehydrogenase 10 / RDH10 → All-trans-retinal source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    NAD-dependent retinol oxidation connects vitamin A metabolism to nicotinamide redox-cofactor availability.
    evidence_location
    Results: cofactor preference
    experimental_model
    Human RDH10 in Sf9 microsomes and siRNA perturbation in human cells.
    exposure
    1 micromolar retinol and 1 millimolar NAD+ versus NADP+.
    limitations
    Cofactor specificity does not establish an effect of dietary niacin deficiency.
    nutrient_topic
    Vitamin A research collection; topical membership is not evidence of a direct dietary effect. · Vitamin A
    organism
    Homo sapiens protein in Spodoptera frugiperda Sf9 cells
    outcome
    Recombinant human RDH10 oxidized all-trans-retinol with NAD+ in microsomal assays.
    plain_language
    RDH10 uses the oxidized nicotinamide cofactor to make retinal.
    primary_references
    [va-belyaeva-2008] Kinetic Analysis of Human Enzyme RDH10 Defines the Characteristics of a Physiologically Relevant Retinol Dehydrogenase (2008). https://pmc.ncbi.nlm.nih.gov/articles/PMC2459273/ DOI: 10.1074/jbc.M800019200
    tissue_or_cell_type
    Microsomes

    Vitamin A: forms, mechanisms, deficiency and excess (2026-09-17) · lines 487–500

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human RDH10 in Sf9 microsomes and siRNA perturbation in human cells. · source_derived_draft · unverified_draft

    ### va-rdh10-retinol-oxidation Recombinant human RDH10 oxidized all-trans-retinol with NAD+ in microsomal assays. Condition category: normal nutrient_topic: Vitamin A research collection; topical membership is not evidence of a direct dietary effect. plain_language: RDH10 uses the oxidized nicotinamide cofactor to make retinal. organism: Homo sapiens protein in Spodoptera frugiperda Sf9 cells tissue_or_cell_type: Microsomes experimental_model: Human RDH10 in Sf9 microsomes and siRNA perturbation in human cells. limitations: Cofactor specificity does not establish an effect of dietary niacin deficiency. exposure: 1 micromolar retinol and 1 millimolar NAD+ versus NADP+. outcome: Recombinant human RDH10 oxidized all-trans-retinol with NAD+ in microsomal assays. evidence_location: Results: cofactor preference cross_nutrient: NAD-dependent retinol oxidation connects vitamin A metabolism to nicotinamide redox-cofactor availability. [va-belyaeva-2008] Kinetic Analysis of Human Enzyme RDH10 Defines the Characteristics of a Physiologically Relevant Retinol Dehydrogenase (2008). https://pmc.ncbi.nlm.nih.gov/articles/PMC2459273/ DOI: 10.1074/jbc.M800019200
    Complete structured claim and evidence

  3. Silencing endogenous RDH10 reduced retinoic-acid production from retinol in human cells.

    Retinol dehydrogenase 10 / RDH10 → All-trans-retinoic-acid biosynthesis source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_location
    Experimental Procedures: siRNA-mediated Knockdowns; Results: endogenous SDR silencing
    experimental_model
    Human RDH10 in Sf9 microsomes and siRNA perturbation in human cells.
    exposure
    RDH10 siRNA at 100 nanomolar, two transfections 24 hours apart; 10 micromolar retinol for 24 hours after silencing.
    limitations
    Residual activity and other enzymes prevent an exclusive RDH10 interpretation.
    nutrient_topic
    Vitamin A research collection; topical membership is not evidence of a direct dietary effect. · Vitamin A
    organism
    Homo sapiens
    outcome
    Silencing endogenous RDH10 reduced retinoic-acid production from retinol in human cells.
    plain_language
    Reducing precursor oxidation lowered downstream active retinoid production.
    primary_references
    [va-belyaeva-2008] Kinetic Analysis of Human Enzyme RDH10 Defines the Characteristics of a Physiologically Relevant Retinol Dehydrogenase (2008). https://pmc.ncbi.nlm.nih.gov/articles/PMC2459273/ DOI: 10.1074/jbc.M800019200
    tissue_or_cell_type
    HEK293 cells
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Vitamin A: forms, mechanisms, deficiency and excess (2026-09-17) · lines 502–514

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human RDH10 in Sf9 microsomes and siRNA perturbation in human cells. · source_derived_draft · unverified_draft

    ### va-rdh10-silencing-ra Silencing endogenous RDH10 reduced retinoic-acid production from retinol in human cells. Condition category: machinery_impairment nutrient_topic: Vitamin A research collection; topical membership is not evidence of a direct dietary effect. plain_language: Reducing precursor oxidation lowered downstream active retinoid production. organism: Homo sapiens tissue_or_cell_type: HEK293 cells experimental_model: Human RDH10 in Sf9 microsomes and siRNA perturbation in human cells. limitations: Residual activity and other enzymes prevent an exclusive RDH10 interpretation. exposure: RDH10 siRNA at 100 nanomolar, two transfections 24 hours apart; 10 micromolar retinol for 24 hours after silencing. outcome: Silencing endogenous RDH10 reduced retinoic-acid production from retinol in human cells. evidence_location: Experimental Procedures: siRNA-mediated Knockdowns; Results: endogenous SDR silencing [va-belyaeva-2008] Kinetic Analysis of Human Enzyme RDH10 Defines the Characteristics of a Physiologically Relevant Retinol Dehydrogenase (2008). https://pmc.ncbi.nlm.nih.gov/articles/PMC2459273/ DOI: 10.1074/jbc.M800019200
    Complete structured claim and evidence

What acts on it

  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. DHRS3 coexpression enhanced RDH10 retinol dehydrogenase activity independently of DHRS3 catalytic activity.

    Dehydrogenase/reductase 3 / DHRS3 → Retinol dehydrogenase 10 / RDH10 source_derived_draftungraded
    Experimental context and source evidence
    evidence_location
    Abstract
    experimental_model
    Human RDH10/DHRS3 coexpression in HEK293 and Sf9 cells, plus Dhrs3-null embryos.
    exposure
    Coexpression including inactive DHRS3 constructs.
    limitations
    Net retinoic-acid output depends on both opposing reactions and cellular conditions.
    nutrient_topic
    Vitamin A research collection; topical membership is not evidence of a direct dietary effect. · Vitamin A
    organism
    Homo sapiens recombinant proteins
    outcome
    DHRS3 coexpression enhanced RDH10 retinol dehydrogenase activity independently of DHRS3 catalytic activity.
    plain_language
    The two enzymes mutually stimulate one another.
    primary_references
    [va-adams-2014] The retinaldehyde reductase activity of DHRS3 is reciprocally activated by retinol dehydrogenase 10 to control retinoid homeostasis (2014). https://pmc.ncbi.nlm.nih.gov/articles/PMC4031538/ DOI: 10.1074/jbc.M114.552257
    tissue_or_cell_type
    Sf9 microsomes and HEK293 cells

    Vitamin A: forms, mechanisms, deficiency and excess (2026-09-17) · lines 545–557

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human RDH10/DHRS3 coexpression in HEK293 and Sf9 cells, plus Dhrs3-null embryos. · source_derived_draft · unverified_draft

    ### va-dhrs3-activates-rdh10 DHRS3 coexpression enhanced RDH10 retinol dehydrogenase activity independently of DHRS3 catalytic activity. Condition category: normal nutrient_topic: Vitamin A research collection; topical membership is not evidence of a direct dietary effect. plain_language: The two enzymes mutually stimulate one another. organism: Homo sapiens recombinant proteins tissue_or_cell_type: Sf9 microsomes and HEK293 cells experimental_model: Human RDH10/DHRS3 coexpression in HEK293 and Sf9 cells, plus Dhrs3-null embryos. limitations: Net retinoic-acid output depends on both opposing reactions and cellular conditions. exposure: Coexpression including inactive DHRS3 constructs. outcome: DHRS3 coexpression enhanced RDH10 retinol dehydrogenase activity independently of DHRS3 catalytic activity. evidence_location: Abstract [va-adams-2014] The retinaldehyde reductase activity of DHRS3 is reciprocally activated by retinol dehydrogenase 10 to control retinoid homeostasis (2014). https://pmc.ncbi.nlm.nih.gov/articles/PMC4031538/ DOI: 10.1074/jbc.M114.552257
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Six3-Cre-directed Rdh10 deletion left mouse cone dark adaptation comparable to controls after pigment bleaching in isolated retinas and intact eyes.

    Retina-directed RDH10 loss → Cone dark adaptation source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    cross_nutrient
    false
    evidence_location
    Figure 7A-B; Results: retina RDH10 and dark adaptation
    experimental_model
    Six3-Cre Rdh10-flox homozygotes on Gnat1-null background
    exposure
    Approximately 90% pigment bleach; Figure 7A-B.
    limitations
    Müller-specific mutants were not separately tested for dark adaptation; whole-retina results must not be relabeled as that experiment.
    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
    Mus musculus
    plain_language
    Removing neural-retinal RDH10 did not impair the tested cone recovery.
    primary_references
    [vav-xue2017] The role of retinol dehydrogenase 10 in the cone visual cycle. (2017). https://pubmed.ncbi.nlm.nih.gov/28539612/ DOI: 10.1038/s41598-017-02549-8
    tissue_or_cell_type
    neural retina; intact-eye and transretinal ERG
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Vitamin A expansion: reproduction, light-driven vision and shared mechanisms (2026-09-17) · lines 648–661

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Six3-Cre Rdh10-flox homozygotes on Gnat1-null background · source_derived_draft · unverified_draft

    ### vae-rdh10-retinal-deletion-recovery Six3-Cre-directed Rdh10 deletion left mouse cone dark adaptation comparable to controls after pigment bleaching in isolated retinas and intact eyes. Condition category: machinery_impairment nutrient_topic: Vitamin A expansion research collection; topical membership is not evidence of a direct dietary effect. plain_language: Removing neural-retinal RDH10 did not impair the tested cone recovery. organism: Mus musculus tissue_or_cell_type: neural retina; intact-eye and transretinal ERG experimental_model: Six3-Cre Rdh10-flox homozygotes on Gnat1-null background limitations: Müller-specific mutants were not separately tested for dark adaptation; whole-retina results must not be relabeled as that experiment. exposure: Approximately 90% pigment bleach; Figure 7A-B. cross_nutrient: false evidence_location: Figure 7A-B; Results: retina RDH10 and dark adaptation nutrient: Vitamin A [vav-xue2017] The role of retinol dehydrogenase 10 in the cone visual cycle. (2017). https://pubmed.ncbi.nlm.nih.gov/28539612/ DOI: 10.1038/s41598-017-02549-8
    Complete structured claim and evidence

  2. Ectopic RDH10 expression did not enable bleached mouse rods to recover sensitivity when supplied with 9-cis-retinol.

    Rod-expressed transgenic RDH10 → Rod dark adaptation source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    false
    evidence_location
    Figure 9C; Results: ectopic RDH10 expression
    experimental_model
    Rod RDH10 transgenesis; single-cell suction recordings
    exposure
    100 micromolar 9-cis-retinol after approximately 50% pigment bleach.
    limitations
    Expression was mosaic; the substrate was 9-cis-retinol, not 11-cis-retinol. This tests sufficiency in rods, not necessity in cones.
    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
    Mus musculus
    plain_language
    Adding RDH10 alone did not let rods use the supplied retinol isomer.
    primary_references
    [vav-xue2017] The role of retinol dehydrogenase 10 in the cone visual cycle. (2017). https://pubmed.ncbi.nlm.nih.gov/28539612/ DOI: 10.1038/s41598-017-02549-8
    tissue_or_cell_type
    isolated rods

    Vitamin A expansion: reproduction, light-driven vision and shared mechanisms (2026-09-17) · lines 663–676

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Rod RDH10 transgenesis; single-cell suction recordings · source_derived_draft · unverified_draft

    ### vae-rdh10-rod-transgene-9cis-retinol Ectopic RDH10 expression did not enable bleached mouse rods to recover sensitivity when supplied with 9-cis-retinol. Condition category: normal nutrient_topic: Vitamin A expansion research collection; topical membership is not evidence of a direct dietary effect. plain_language: Adding RDH10 alone did not let rods use the supplied retinol isomer. organism: Mus musculus tissue_or_cell_type: isolated rods experimental_model: Rod RDH10 transgenesis; single-cell suction recordings limitations: Expression was mosaic; the substrate was 9-cis-retinol, not 11-cis-retinol. This tests sufficiency in rods, not necessity in cones. exposure: 100 micromolar 9-cis-retinol after approximately 50% pigment bleach. cross_nutrient: false evidence_location: Figure 9C; Results: ectopic RDH10 expression nutrient: Vitamin A [vav-xue2017] The role of retinol dehydrogenase 10 in the cone visual cycle. (2017). https://pubmed.ncbi.nlm.nih.gov/28539612/ DOI: 10.1038/s41598-017-02549-8
    Complete structured claim and evidence

  3. RDH10-activated DHRS3 reduced all-trans-retinal to retinol preferentially using NADPH.

    Dehydrogenase/reductase 3 / DHRS3 → All-trans-retinol source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    NADPH supports a retinoid buffering reaction.
    evidence_location
    Figure 5 and Table 1
    experimental_model
    Human RDH10/DHRS3 coexpression in HEK293 and Sf9 cells, plus Dhrs3-null embryos.
    exposure
    DHRS3 coexpressed with RDH10; retinal plus NADPH.
    limitations
    Cofactor dependency is not a dietary niacin intervention.
    nutrient_topic
    Vitamin A research collection; topical membership is not evidence of a direct dietary effect. · Vitamin A
    organism
    Homo sapiens proteins in Sf9 and HEK293 systems
    outcome
    RDH10-activated DHRS3 reduced all-trans-retinal to retinol preferentially using NADPH.
    plain_language
    This reverse step restrains retinal available for acid production.
    primary_references
    [va-adams-2014] The retinaldehyde reductase activity of DHRS3 is reciprocally activated by retinol dehydrogenase 10 to control retinoid homeostasis (2014). https://pmc.ncbi.nlm.nih.gov/articles/PMC4031538/ DOI: 10.1074/jbc.M114.552257
    tissue_or_cell_type
    Microsomal/cellular retinoid system

    Vitamin A: forms, mechanisms, deficiency and excess (2026-09-17) · lines 516–529

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human RDH10/DHRS3 coexpression in HEK293 and Sf9 cells, plus Dhrs3-null embryos. · source_derived_draft · unverified_draft

    ### va-dhrs3-retinal-reduction RDH10-activated DHRS3 reduced all-trans-retinal to retinol preferentially using NADPH. Condition category: normal nutrient_topic: Vitamin A research collection; topical membership is not evidence of a direct dietary effect. plain_language: This reverse step restrains retinal available for acid production. organism: Homo sapiens proteins in Sf9 and HEK293 systems tissue_or_cell_type: Microsomal/cellular retinoid system experimental_model: Human RDH10/DHRS3 coexpression in HEK293 and Sf9 cells, plus Dhrs3-null embryos. limitations: Cofactor dependency is not a dietary niacin intervention. exposure: DHRS3 coexpressed with RDH10; retinal plus NADPH. outcome: RDH10-activated DHRS3 reduced all-trans-retinal to retinol preferentially using NADPH. evidence_location: Figure 5 and Table 1 cross_nutrient: NADPH supports a retinoid buffering reaction. [va-adams-2014] The retinaldehyde reductase activity of DHRS3 is reciprocally activated by retinol dehydrogenase 10 to control retinoid homeostasis (2014). https://pmc.ncbi.nlm.nih.gov/articles/PMC4031538/ DOI: 10.1074/jbc.M114.552257
    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