Cytochrome P450s in the Regulation of Cellular Retinoic Acid Metabolism
Open accessAbstract
The active metabolite of vitamin A, retinoic acid (RA), is a powerful regulator of gene transcription. RA is also a therapeutic drug. The oxidative metabolism of RA by certain members of the cytochrome P450 (CYP) superfamily helps to maintain tissue RA concentrations within appropriate bounds. The CYP26 family—CYP26A1, CYP26B1, and CYP26C1—is distinguished by being both regulated by and active toward all-trans-RA (at-RA) while being expressed in different tissue-specific patterns. The CYP26A1 gene is regulated by multiple RA response elements. CYP26A1 is essential for embryonic development, whereas CYP26B1 is essential for postnatal survival as well as germ cell development. Enzyme kinetic studies have demonstrated that several CYP proteins are capable of metabolizing at-RA; however, it is likely that CYP26A1 plays a major role in RA clearance. Thus, pharmacological approaches to limiting the activity of CYP26 enzymes may extend the half-life of RA and could be useful clinically in the future.
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All-trans-retinoic acid formation is irreversible, and excess is cleared by CYP26 oxidation and/or UGT glucuronidation.
“Because all-trans-retinoic acid formation is irreversible, an excess of this active retinoid can be cleared only by its further conversion to more polar metabolites through oxidation by cytochrome P450 (CYP26) and/or glucuronidation by UDP-glucuronosyl transferases (UGTs).137,138”
From Chemistry of the Retinoid (Visual) Cycle (2014) · cites this paper as [138]
The Introduction’s “Initial Studies on Retinoic Acid Oxidation” section describes CYP26 oxidation of all-trans-retinoic acid to polar metabolites followed by UDP-glucuronosyl transferase conjugation. Our copy does not state that formation of all-trans-retinoic acid is irreversible, and the “Other CYP Families” section describes additional CYP enzymes capable of oxidizing it, so the claim’s exclusivity is not supported. No page numbers were available for these passages. (LLM, conf=0.85)
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- Authors
- Catharine Ross, A., & Zolfaghari, R.
- Affiliations
- Pennsylvania State University (US)
- ORCID
- Zolfaghari, Reza
- Venue
- Annual Review of Nutrition
- Publisher
- Annual Reviews
- Published
- 2011-08-21
- Volume
- 31
- Issue
- 1
- Pages
- 65-87
- ISSN
- 0199-9885 (ISSN-L)
- 1545-4312
- PMC
- PMC3789243
- OpenAlex
- W2167484695
- Cited by
- 296
- References
- 124
- Citations by year
- 2026: 19 · 2025: 8 · 2024: 18 · 2023: 16 · 2022: 16 · 2021: 16 · 2020: 34 · 2019: 24 · 2018: 14 · 2017: 18 · 2016: 24 · 2015: 21 · 2014: 22 · 2013: 24 · 2012: 19
- FWCI
- 1.97
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Annual Review of Nutrition (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health
- National Cancer Institute (CA90214, R01CA090214)
- National Institute of Diabetes and Digestive and Kidney Diseases (R01DK041479)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Retinoids in leukemia and cellular processes
- Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Pharmacology › Pharmacogenetics and Drug Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Peroxisome Proliferator-Activated Receptors
- Keywords
- retinoic acid, cytochrome P450, CYP26A1, CYP26B1, CYP26C1, retinoic acid metabolism, all-trans retinoic acid, vitamin A, transcriptional regulation, embryonic development, germ cell development, enzyme kinetics
- MeSH terms
- Retinoic Acid 4-Hydroxylase, Animals, Biotransformation, Cell Differentiation, Cytochrome P-450 Enzyme System, Humans, Isoenzymes, Liver, Stem Cells, Tretinoin, Gene Expression Regulation, Enzymologic, Embryonic Development, Retinoid X Receptors, Biocatalysis
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