Substrate specificities and 13-cis-retinoic acid inhibition of human, mouse and bovine cis-retinol dehydrogenases
Abstract
Recent studies of the human, mouse and bovine genes for 11-cis-retinol dehydrogenase (11cRDH) and human and mouse 9-cis-retinol dehydrogenase (9cRDH) suggest that they are homologs of the same enzyme. This conclusion is inconsistent with earlier literature indicating that 11cRDH is expressed solely in the eye and does not utilize 9-cis-retinol as a substrate. We have compared directly the kinetic properties of recombinant human and mouse 9cRDH with those of bovine 11cRDH for 9-cis- and 11-cis-retinol and investigated the inhibitory properties of 13-cis-retinoic acid on each of these enzymes. Human and mouse 9cRDH and bovine 11cRDH have very similar kinetic properties towards 9-cis- and 11-cis-retinol oxidation and they respond identically to 13-cis-retinoic acid inhibition. Our biochemical data are consistent with the conclusion that 9cRDH and 11cRDH are the same enzyme.
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Isotretinoin reduces the accumulation of toxic byproducts of the visual cycle, such as A2E.
“However, on the other hand, it reduces the accumulation of toxic byproducts of the visual cycle, such as N-retinyl-N-retinylidene ethanolamine (A2E) [16,17,18].”
From The Role of Vitamin A in Retinal Diseases (2022) · cites this paper as [17]
Isotretinoin impairs the chromophore 11-cis-retinal and slows rhodopsin regeneration, which can cause night blindness.
“This impairs chromophore, 11-cis-retinal, and slows rhodopsin (RHO) regeneration which can cause night blindness.”
From The Role of Vitamin A in Retinal Diseases (2022) · cites this paper as [17]
In the RPE, isotretinoin inhibits two key visual cycle enzymes, RPE65 and 11-cis-retinol dehydrogenase.
“In retina in the retinal pigment epithelium (RPE), isotretinoin inhibits two key visual cycle enzymes, RPE-specific 65 kDa protein (RPE65) [16] and 11-cis-retinol dehydrogenase [17,18] (Figure 1).”
From The Role of Vitamin A in Retinal Diseases (2022) · cites this paper as [17]
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References 18 · Cited by 34
- Authors
- Gamble, M. V., Mata, N. L., Tsin, A. T., Mertz, J. R., & Blaner, W. S.
- Affiliations
- Columbia University (US)
- The University of Texas at San Antonio (US)
- New England College of Optometry (US)
- Corresponding author
- Blaner, William S.
- Venue
- Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
- Publisher
- Elsevier BV
- Published
- 2000-01
- Volume
- 1476
- Issue
- 1
- Pages
- 3-8
- ISSN
- 0167-4838 (ISSN-L)
- OpenAlex
- W2095778218
- Cited by
- 34
- References
- 18
- Citations by year
- 2025: 2 · 2022: 1 · 2021: 1 · 2016: 1 · 2013: 3 · 2012: 1
- FWCI
- 1.81
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- National Institute of Diabetes and Digestive and Kidney Diseases (R01 DK 52444, R01DK052444, T32 DK07328, T32DK007328)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Retinoids in leukemia and cellular processes
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Retinal Development and Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Aldose Reductase and Taurine
- Keywords
- isotretinoin, enzyme inhibition, substrate specificity, enzyme kinetics, retinol oxidation, enzyme homology, vitamin A metabolism, recombinant enzyme
- MeSH terms
- Alcohol Oxidoreductases, Animals, Cattle, Humans, Kinetics, Substrate Specificity, Vitamin A, Isotretinoin, Mice
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