ArticleChemico-biological interactions2017
Characterization of human short chain dehydrogenase/reductase SDR16C family members related to retinol dehydrogenase 10.
Article in Chemico-biological interactions, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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18 citing papers in PubMed, 26 citations in OpenAlex.
- Cervical cancer molecular subtype identification and prognosis classification by a metabolism-related gene expression.Translational cancer research · 2025Article
- Tissue-Specific Expression of the PorcineAnimals : an open access journal from MDPI · 2025Article
- Epidermal retinol dehydrogenases cyclically regulate stem cell markers and clock genes and influence hair composition.Communications biology · 2024Article
- SDR16C5 promotes proliferation and migration and inhibits apoptosis in pancreatic cancer.Open life sciences · 2023Article
- All-trans retinoic acid regulates the expression of MMP-2 and TGF-β2International journal of ophthalmology · 2023Article
- Vitamin A in Skin and Hair: An Update.Nutrients · 2022Review
- Novel acetylation-related gene signatures for predicting the prognosis of patients with colorectal cancer.Human cell · 2022Article
- Mechanisms of Feedback Regulation of Vitamin A Metabolism.Nutrients · 2022Review
- Enhanced Loss of Retinoic Acid Network Genes inCells · 2022Article
- Reorganization of Metabolism during Cardiomyogenesis Implies Time-Specific Signaling Pathway Regulation.International journal of molecular sciences · 2021Article
- Retinoids in Cutaneous Squamous Cell Carcinoma.Nutrients · 2021Review
- Dietary Vitamin A Impacts Refractory Telogen.Frontiers in cell and developmental biology · 2021Article
- Post-natal all-trans-retinoic acid biosynthesis.Methods in enzymology · 2020Article
- Generation of Retinaldehyde for Retinoic Acid Biosynthesis.Biomolecules · 2019Review
- Mice lacking the epidermal retinol dehydrogenases SDR16C5 and SDR16C6 display accelerated hair growth and enlarged meibomian glands.The Journal of biological chemistry · 2019Article
- Recent insights on the role and regulation of retinoic acid signaling during epicardial development.Genesis (New York, N.Y. : 2000) · 2019Review
- The antagonistically bifunctional retinoid oxidoreductase complex is required for maintenance of all-The Journal of biological chemistry · 2017Article
- Review
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5 authors at 1 institution in 1 country.
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Abstract
All-trans-retinoic acid (RA) is a bioactive derivative of vitamin A that serves as an activating ligand for nuclear transcription factors, retinoic acid receptors. RA biosynthesis is initiated by the enzymes that oxidize retinol to retinaldehyde. It is well established that retinol dehydrogenase 10 (RDH10, SDR16C4), which belongs to the 16C family of the short chain dehydrogenase/reductase (SDR) superfamily of proteins, is the major enzyme responsible for the oxidation of retinol to retinaldehyde for RA biosynthesis during embryogenesis. However, several lines of evidence point towards the existence of additional retinol dehydrogenases that contribute to RA biosynthesis in vivo. In close proximity to RDH10 gene on human chromosome 8 are located two genes that are phylogenetically related to RDH10. The predicted protein products of these genes, retinol dehydrogenase epidermal 2 (RDHE2, SDR16C5) and retinol dehydrogenase epidermal 2-similar (RDHE2S, SDR16C6), share 59% and 56% sequence similarity with RDH10, respectively. Previously, we showed that the single ortholog of the human RDHE2 and RDHE2S in frogs, Xenopus laevis rdhe2, oxidizes retinol to retinaldehyde and is essential for frog embryonic development. In this study, we explored the potential of each of the two human proteins to contribute to RA biosynthesis. The results of this study demonstrate that human RDHE2 exhibits a relatively low but reproducible activity when expressed in either HepG2 or HEK293 cells. Expression of the native RDHE2 is downregulated in the presence of elevated levels of RA. On the other hand, the protein encoded by the human RDHE2S gene is unstable when expressed in HEK293 cells. RDHE2S protein produced in Sf9 cells is stable but has no detectable catalytic activity towards retinol. We conclude that the human RDHE2S does not contribute to RA biosynthesis, whereas the low-activity RA-sensitive human RDHE2 may have a role in adjusting the cellular levels of RA in accord with specific physiological conditions.
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