Component
Dehydrogenase/reductase 3 / DHRS3
Independent protein identity; organism and experimental state are specified on individual claims.
3 recorded relationships. Experimental role, claim status and evidence remain attached to each record.
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.
Other things that act on it
Enzymes, hormones, genes, and other components with a recorded effect. These are not nutrients, so they do not count toward the arrows above. Each finding names the chapter that recorded it.
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.
What it acts on
DHRS3 coexpression enhanced RDH10 retinol dehydrogenase activity independently of DHRS3 catalytic activity.
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 evidenceRDH10-activated DHRS3 reduced all-trans-retinal to retinol preferentially using NADPH.
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
What acts on it
RDH10 coexpression increased DHRS3 retinaldehyde reductase activity even when RDH10 itself was catalytically inactive.
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
The events it takes part in
A mechanism often involves more than two components. These are the full events, with every participant and its role.
Situations it appears in
Low-supply and faulty-machinery situations recorded in the chapters where this component plays a part.
In the sources
Preserved passages that mention this component, quoted exactly. Open one to read it in context.
Open hypotheses
Proposed ideas that involve this component. They are labeled as hypotheses and do not change any recorded statement.
This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.