ArticleThe Journal of biological chemistry2008
Kinetic analysis of human enzyme RDH10 defines the characteristics of a physiologically relevant retinol dehydrogenase.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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42 citing papers in PubMed, 69 citations in OpenAlex.
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- Human intestinal stromal cells promote homeostasis in normal mucosa but inflammation in Crohn's disease in a retinoic acid-deficient manner.Mucosal immunology · 2024Article
- The pathogenic role of retinoid nuclear receptor signaling in cancer and metabolic syndromes.The Journal of experimental medicine · 2024Review
- Raising NADCirculation · 2023Article
- T Cell-Intrinsic Vitamin A Metabolism and Its Signaling Are Targets for Memory T Cell-Based Cancer Immunotherapy.Frontiers in immunology · 2022Article
- A specific inhibitor of ALDH1A3 regulates retinoic acid biosynthesis in glioma stem cells.Communications biology · 2021Article
- Characterization of subunit interactions in the hetero-oligomeric retinoid oxidoreductase complex.The Biochemical journal · 2021Article
- 17-Beta Hydroxysteroid Dehydrogenase 13 Deficiency Does Not Protect Mice From Obesogenic Diet Injury.Hepatology (Baltimore, Md.) · 2021Article
- Generation of Retinaldehyde for Retinoic Acid Biosynthesis.Biomolecules · 2019Review
- Retinoic Acid Signaling Is Associated with Cell Proliferation, Muscle Cell Dedifferentiation, and Overall Rudiment Size during Intestinal Regeneration in the Sea Cucumber,Biomolecules · 2019Article
- Mice lacking the epidermal retinol dehydrogenases SDR16C5 and SDR16C6 display accelerated hair growth and enlarged meibomian glands.The Journal of biological chemistry · 2019Article
- 17-Beta Hydroxysteroid Dehydrogenase 13 Is a Hepatic Retinol Dehydrogenase Associated With Histological Features of Nonalcoholic Fatty Liver Disease.Hepatology (Baltimore, Md.) · 2019Article
- Yeast ENV9 encodes a conserved lipid droplet (LD) short-chain dehydrogenase involved in LD morphology.Current genetics · 2017Article
- Characterization of human short chain dehydrogenase/reductase SDR16C family members related to retinol dehydrogenase 10.Chemico-biological interactions · 2017Article
- The role of retinol dehydrogenase 10 in the cone visual cycle.Scientific reports · 2017Article
- The antagonistically bifunctional retinoid oxidoreductase complex is required for maintenance of all-The Journal of biological chemistry · 2017Article
- Review
- Review
- Coelimination and Survival in Gene Network Evolution: Dismantling the RA-Signaling in a Chordate.Molecular biology and evolution · 2016Article
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3 authors at 1 institution in 1 country.
Funding
Abstract
Human retinol dehydrogenase 10 (RDH10) was implicated in the oxidation of all-trans-retinol for biosynthesis of all-trans-retinoic acid, however, initial assays suggested that RDH10 prefers NADP(+) as a cofactor, undermining its role as an oxidative enzyme. Here, we present evidence that RDH10 is, in fact, a strictly NAD(+)-dependent enzyme with multisubstrate specificity that recognizes cis-retinols as well as all-trans-retinol as substrates. RDH10 has a relatively high apparent K(m) value for NAD(+) (~100 microm) but the lowest apparent K(m) value for all-trans-retinol (~0.035 microm) among all NAD(+)-dependent retinoid oxidoreductases. Due to its high affinity for all-trans-retinol, RDH10 exhibits a greater rate of retinol oxidation in the presence of cellular retinol-binding protein type I (CRBPI) than human microsomal RoDH4, but like RoDH4, RDH10 does not recognize retinol bound to CRBPI as a substrate. Consistent with its preference for NAD(+), RDH10 functions exclusively in the oxidative direction in the cells, increasing the levels of retinaldehyde and retinoic acid. Targeted small interfering RNA-mediated silencing of endogenous RDH10 or RoDH4 expression in human cells results in a significant decrease in retinoic acid production from retinol, identifying both human enzymes as physiologically relevant retinol dehydrogenases. The dual cis/trans substrate specificity suggests a dual physiological role for RDH10: in the biosynthesis of 11-cis-retinaldehyde for vision as well as the biosynthesis of all-trans-retinoic acid for differentiation and development.
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