Key enzymes of the retinoid (visual) cycle in vertebrate retina

Kiser, Philip D.; Golczak, Marcin; Maeda, Akiko; Palczewski, Krzysztof

doi:10.1016/j.bbalip.2011.03.005

Cited by 177Retinal Development and DisordersRetinoids in leukemia and cellular processesPhotoreceptor and optogenetics research

Key enzymes of the retinoid (visual) cycle in vertebrate retina

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Kiser, Philip D., Golczak, Marcin, Maeda, Akiko, Palczewski, Krzysztof·2012·Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids

DOI 10.1016/j.bbalip.2011.03.005PMC PMC3158816

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Abstract

A major goal in vision research over the past few decades has been to understand the molecular details of retinoid processing within the retinoid (visual) cycle. This includes the consequences of side reactions that result from delayed all-trans-retinal clearance and condensation with phospholipids that characterize a variety of serious retinal diseases. Knowledge of the basic retinoid biochemistry involved in these diseases is essential for development of effective therapeutics. Photoisomerization of the 11-cis-retinal chromophore of rhodopsin triggers a complex set of metabolic transformations collectively termed phototransduction that ultimately lead to light perception. Continuity of vision depends on continuous conversion of all-trans-retinal back to the 11-cis-retinal isomer. This process takes place in a series of reactions known as the retinoid cycle, which occur in photoreceptor and RPE cells. All-trans-retinal, the initial substrate of this cycle, is a chemically reactive aldehyde that can form toxic conjugates with proteins and lipids. Therefore, much experimental effort has been devoted to elucidate molecular mechanisms of the retinoid cycle and all-trans-retinal-mediated retinal degeneration, resulting in delineation of many key steps involved in regenerating 11-cis-retinal. Three particularly important reactions are catalyzed by enzymes broadly classified as acyltransferases, short-chain dehydrogenases/reductases and carotenoid/retinoid isomerases/oxygenases. This article is part of a Special Issue entitled: Retinoid and Lipid Metabolism.

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Only retinol dehydrogenases contribute to vision-related retinoid metabolism.
“However, only RDH’s contribute to vision-related metabolism of retinoids.”
From Chemistry of the Retinoid (Visual) Cycle (2014) · cites this paper as [287]
Section 3 says RDHs catalyze two reactions in the visual retinoid cycle, but the claim's 'only' is contrary to the paper. Section 2.4 calls LRAT indispensable to that cycle and says LRAT and RPE65 are required for 11-cis-retinoid production in the RPE. Page numbers are unavailable in our copy. (LLM, conf=0.94)
Checked by a reasoning model — may be wrong.
Experimental — accuracy not yet measured
In visual phototransduction, large quantities of vitamin A in the form of 11-cis-retinal are isomerized to all-trans-retinal and then quickly recycled back to 11-cis-retinal.
“In this process, large quantities of vitamin A in the form of 11-cis-retinal are being isomerized to all-trans-retinal and then quickly recycled back to 11-cis-retinal.”
From The Role of Vitamin A in Retinal Diseases (2022) · cites this paper as [46]
The Abstract and Introduction (page not provided) describe photoisomerization of 11-cis-retinal to all-trans-retinal and its regeneration through the retinoid cycle. The Introduction also describes high retinoid flux during intense light exposure, but does not establish that recycling back to 11-cis-retinal is quick. (LLM, conf=0.84)
Experimental — accuracy not yet measured
RPE65 is an isomerohydrolase that catalyses hydrolysis of esters and isomerizes all-trans-retinol to 11-cis-retinol.
“RPE65 is an isomerohydrolase that catalyses hydrolysis of esters and isomerizes all-trans-retinol to 11-cis-retinol [29,32,46].”
From The Role of Vitamin A in Retinal Diseases (2022) · cites this paper as [46]
Section 4.4.3 describes RPE65 as an isomerohydrolase that couples ester hydrolysis with retinoid isomerization. But Section 4.4.2 identifies retinyl esters—not free all-trans-retinol—as its natural substrates, so the claim misstates what RPE65 directly isomerizes. (LLM, conf=0.88)
Experimental — accuracy not yet measured
When all-trans-retinal is released from opsin, it binds phosphatidylethanolamine to form N-retinylidene-phosphatidylethanolamine, which is transported by ABCA4 across the membrane to the cytoplasmic side of the photoreceptor.
“When the all-trans-retinal is released from the opsin, on the luminal side of the photoreceptor membrane of rod discs and extracellular side in cones, it binds to the phosphatidylethanolamine to form N-retinylidene-phosphatidylethanolamine. The latter is transported by the ATP-binding cassette subfamily A member 4 transporter (ABCA4) across the membrane to the cytoplasmic side of the photoreceptor”
From The Role of Vitamin A in Retinal Diseases (2022) · cites this paper as [46]
The Introduction says that all-trans-retinal released from visual pigments can enter the disc lumen and is transferred toward the cytosol by ABCA4. Section 3.1 mentions conjugation of all-trans-retinal with phosphatidylethanolamine and says ABCA4 transports retinal or its metabolites, but the copy does not identify N-retinylidene-phosphatidylethanolamine as the transported molecule or establish the stated topology in cones. Page numbers were not available in the indexed passages. (LLM, conf=0.86)
Experimental — accuracy not yet measured
At the start of the visual cycle, all-trans-retinol enters the RPE through facilitated transport by STRA6 where it gets metabolized into a retinyl ester via the action of LRAT, which then converts to 11-cis retinol and subsequently 11-cis retinal through catalysis by RPE65 and RDH5.
“At the start of the visual cycle, all- trans-retinol enters the RPE through facilitated transport by STRA6 where it gets metabolized into a retinyl ester via the action of LRAT, which then converts to 11-cis retinol and subsequently 11-cis retinal through catalysis by RPE65 and retinol dehydrogenase 5 (RDH5), respectively [53].”
From Vitamin A Transporters in Visual Function: A Mini Review on Membrane Receptors for Dietary Vitamin A Uptake, Storage, and Transport to the Eye (2021) · cites this paper as [53]
Split into 2 atoms — 1 confirmed, 1 partially supported, 0 disputed, 0 misattributed, 0 unverifiable. Expand the claim to see per-atom verdicts.
Experimental — accuracy not yet measured

Interconversion of retinals and retinols is an integral part of the retinoid cycle.
“An integral part of the retinoid cycle is the interconversion of retinals and retinols.”
From Chemistry of the Retinoid (Visual) Cycle (2014) · cites this paper as [287]
Only RDH5, RDH8, RDH10, RDH11, RDH12, RDH13, RDH14, and retSDR1 have been proven to be expressed in retina or RPE.
“In fact only RDH5, RDH8, RDH10, RDH11, RDH12, RDH13, RDH14, and retSDR1 were proven to be expressed in the retina or RPE, and their roles have been studied in the context of the visual (retinoid) cycle.68,287”
From Chemistry of the Retinoid (Visual) Cycle (2014) · cites this paper as [287]
Complex machinery of transporters and enzymes is involved in the visual cycle.
“Complex machinery of transporters and enzymes is involved in this process (i.e., the visual cycle).”
From The Role of Vitamin A in Retinal Diseases (2022) · cites this paper as [46]
All-trans-retinal is converted to all-trans-retinol by all-trans-retinol dehydrogenases RDH8 in the outer segments and RDH12 in the inner segments of the photoreceptors.
“All-trans-retinal is released into the cytoplasm, where it can be converted to all-trans-retinol by all-trans-retinol dehydrogenases, RDH8 in the outer segments of the photoreceptors and RDH12 in the inner segments of the photoreceptors.”
From The Role of Vitamin A in Retinal Diseases (2022) · cites this paper as [46]
All-trans-retinal is continuously recycled back to 11-cis-retinal in the process called the visual cycle.
“The all-trans-retinal is continuously recycled back to the 11-cis-retinal in the process called the visual cycle.”
From The Role of Vitamin A in Retinal Diseases (2022) · cites this paper as [46]
The classical, or canonical, visual cycle involves regeneration of 11-cis-retinal in the RPE.
“The classical, or canonical visual cycle involves regeneration of 11-cis-retinal in the RPE.”
From The Role of Vitamin A in Retinal Diseases (2022) · cites this paper as [46]
IRBP helps transfer all-trans-retinol from photoreceptors to the RPE, where it can be converted back to 11-cis-retinal by LRAT, RPE65, RDH5 and RDH11.
“The IRBP helps transfer all-trans-retinol from photoreceptors to the RPE, where it can be converted back to 11-cis-retinal by the LRAT, RPE65, RDH5 and RDH11 enzymes as described above.”
From The Role of Vitamin A in Retinal Diseases (2022) · cites this paper as [46]
RDH8 contributes approximately 70% and RDH12 approximately 30% of all-trans-RDH activity.
“RDH8 contributes to approximately 70% and RDH12 to approximately 30% of all-trans-RDH activity.”
From The Role of Vitamin A in Retinal Diseases (2022) · cites this paper as [46]
Under physiological conditions the NAD/NADH ratio is near 1000, so RDHs binding this cofactor mainly contribute to retinol oxidation.
“Under physiological conditions the ratio between NAD/NADH is close to 1000;287 thus, RDH’s that bind this cofactor can contribute significantly only to retinol oxidation.”
From Chemistry of the Retinoid (Visual) Cycle (2014) · cites this paper as [287]
The citation is attached to the physiological NAD/NADH ratio of approximately 1000. Section 3 (Retinol dehydrogenases) discusses NAD-dependent reactions and retinol oxidation, but neither the supplied passages nor searches for the ratio and its proposed effect found a physiological NAD/NADH value in our copy. (LLM, conf=0.76)
Experimental — accuracy not yet measured

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Retinol dehydrogenase 12 detoxifies 4-hydroxynonenal in photoreceptor cells
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The Phenotype of Early-Onset Retinal Degeneration in Persons with RDH12 Mutations
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Lecithin Retinol Acyltransferase Contains Cysteine Residues Essential for Catalysis
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Cellular Retinol-binding Protein Type III Is Needed for Retinoid Incorporation into Milk*
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Evidence for RPE65‐independent vision in the cone‐dominated zebrafish retina
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Novel RDH12 mutations associated with Leber congenital amaurosis and cone-rod dystrophy: Biochemical and clinical evaluations
Sun, W., Gerth‐Kahlert, C., Maeda, A., Lodowski, D. T., Kraak, L. V. D., Saperstein, D. A., Héon, E., & Palczewski, K. (2007) · Vision Research · doi:10.1016/j.visres.2007.04.005 · Cited by 52 · see citing works
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The Upstream Region of the Rpe65 Gene Confers Retinal Pigment Epithelium-specific Expression in Vivo and in Vitro and Contains Critical Octamer and E-box Binding Sites
Boulanger, A., Liu, S., Henningsgaard, A. A., Yu, S., & Redmond, T. M. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m003441200 · Cited by 50 · see citing works
The specific binding of retinoic acid to RPE65 and approaches to the treatment of macular degeneration
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Characterization of Native Retinal Fluorophores Involved in Biosynthesis of A2E and Lipofuscin-associated Retinopathies
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Role of LRAT on the Retinoid Isomerase Activity and Membrane Association of Rpe65
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Characterization of Mouse Short-chain Aldehyde Reductase (SCALD), an Enzyme Regulated by Sterol Regulatory Element-binding Proteins
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Evaluation of Potential Therapies for a Mouse Model of Human Age-Related Macular Degeneration Caused by Delayed all- trans -Retinal Clearance
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Cloning and localization of RPE65 mRNA in salamander cone photoreceptor cells
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Evaluation of 9- cis -Retinyl Acetate Therapy in Rpe65 −/− Mice
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Functional Characterization of Mouse RDH11 as a Retinol Dehydrogenase Involved in Dark Adaptation in Vivo
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Kinetic mechanism of lecithin retinol acyl transferase
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Purified RPE65 shows isomerohydrolase activity after reassociation with a phospholipid membrane
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Fundus albipunctatus: A clinical study of the fundus lesions, the physiologic deficit, and the vitamin a metabolism
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Sequestration of Retinyl Esters Is Essential for Retinoid Signaling in the Zebrafish Embryo
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Aberrant Metabolites in Mouse Models of Congenital Blinding Diseases: Formation and Storage of Retinyl Esters
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Stereochemical inversion at C-15 accompanies the enzymic isomerization of all-trans- to 11-cis-retinoids
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RPE65 surface epitopes, protein interactions, and expression in rod- and cone-dominant species.
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Roles of Cysteine 161 and Tyrosine 154 in the Lecithin−Retinol Acyltransferase Mechanism
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Role of the 3′-Untranslated Region of RPE65 mRNA in the Translational Regulation of the RPE65 Gene: Identification of a Specific Translation Inhibitory Element
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Effects of Long-Term Administration of 9-cis-Retinyl Acetate on Visual Function in Mice
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An Acyl-covalent Enzyme Intermediate of Lecithin:Retinol Acyltransferase*
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Cloning of a Lignostilbene-α,β-dioxygenase Isozyme Gene fromPseudomonas paucimohilisTMY1009
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The necessity of an intact polyene for the biological isomerization of vitamin A
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CRALBP Ligand and Protein Interactions
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Small Molecule RPE65 Antagonists Limit the Visual Cycle and Prevent Lipofuscin Formation,
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Cloning of a Lignostilbene-α,β-dioxy-genase Gene from Pseudomonas paucimobilis TMY1009(Microbiology & Fermentation Industry)
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Microbial and Animal Rhodopsins: Structures, Functions, and Molecular Mechanisms
Ernst, O. P., Lodowski, D. T., Elstner, M., Hegemann, P., Brown, L. S., & Kandori, H. (2013) · Chemical Reviews · doi:10.1021/cr4003769 · Cited by 1,140 · see citing works
Chemistry of the Retinoid (Visual) Cycle
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Functions, Therapeutic Applications, and Synthesis of Retinoids and Carotenoids
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Mechanism of All-trans-retinal Toxicity with Implications for Stargardt Disease and Age-related Macular Degeneration
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Vitamin A Metabolism in Rod and Cone Visual Cycles
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Dissecting the transcriptome landscape of the human fetal neural retina and retinal pigment epithelium by single-cell RNA-seq analysis
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The retinaldehyde reductase DHRS3 is essential for preventing the formation of excess retinoic acid during embryonic development
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The pros and cons of vertebrate animal models for functional and therapeutic research on inherited retinal dystrophies
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The Role of Vitamin A in Retinal Diseases
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“Their dysfunction subsequently leads to decreased synthesis of 11-cis-retinal, which may result in reduced autofluorescence signal [46,47,60,149,150].”
BackgroundInfluential
Noninvasive two-photon microscopy imaging of mouse retina and retinal pigment epithelium through the pupil of the eye
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Retinoids and Retinal Diseases
Kiser, P. D., & Palczewski, K. (2016) · Annual Review of Vision Science · doi:10.1146/annurev-vision-111815-114407 · Cited by 108 · see citing works
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Vitamin A and Vision
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Ferroptosis drives photoreceptor degeneration in mice with defects in all-trans-retinal clearance
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Mechanisms of Transport and Delivery of Vitamin A and Carotenoids to the Retinal Pigment Epithelium
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Retinal Photodamage Mediated by All‐trans‐retinal†
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Genome-wide association analyses identify 139 loci associated with macular thickness in the UK Biobank cohort
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Retinal Pigmented Epithelial Cells Obtained from Human Induced Pluripotent Stem Cells Possess Functional Visual Cycle Enzymes in Vitro and in Vivo*
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CCL3 Production by Microglial Cells Modulates Disease Severity in Murine Models of Retinal Degeneration
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Melanopsin and Mechanisms of Non-visual Ocular Photoreception
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Structural Basis for the Acyltransferase Activity of Lecithin:Retinol Acyltransferase-like Proteins
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Molecular Basis for Vitamin A Uptake and Storage in Vertebrates
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“Thus, the same basic catalytic mechanism allows accommodating numerous enzymatic activities [95].”
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Chemistry and Biology of the Initial Steps in Vision: The Friedenwald Lecture
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The molecular aspects of absorption and metabolism of carotenoids and retinoids in vertebrates
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Tsin, A. T. C., Betts-Obregon, B. S., & Grigsby, J. G. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.aw118.003228 · Cited by 62 · see citing works
Chrysin Ameliorates Malfunction of Retinoid Visual Cycle through Blocking Activation of AGE-RAGE-ER Stress in Glucose-Stimulated Retinal Pigment Epithelial Cells and Diabetic Eyes
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The role of the retinoids in schizophrenia: genomic and clinical perspectives
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Mechanisms of Feedback Regulation of Vitamin A Metabolism
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Gene therapy and the adeno‐associated virus in the treatment of genetic and acquired ophthalmic diseases in humans: Trials, future directions and safety considerations
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Two-photon microscopy reveals early rod photoreceptor cell damage in light-exposed mutant mice
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Melanopsin Is Highly Resistant to Light and Chemical Bleaching in Vivo
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Vitamin A Transporters in Visual Function: A Mini Review on Membrane Receptors for Dietary Vitamin A Uptake, Storage, and Transport to the Eye
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RIM1/2-Mediated Facilitation of Cav1.4 Channel Opening Is Required for Ca2+-Stimulated Release in Mouse Rod Photoreceptors
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Inherent Instability of the Retinitis Pigmentosa P23H Mutant Opsin
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Cellular and Molecular Biological Approaches to Interpreting Ancient Biomarkers
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Kinetic, Energetic, and Mechanical Differences between Dark-State Rhodopsin and Opsin
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Stem‐cell‐based therapies for retinal degenerative diseases: Current challenges in the establishment of new treatment strategies
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Authors: Kiser, P. D., Golczak, M., Maeda, A., & Palczewski, K.
Affiliations: Case Western Reserve University (US)
Corresponding author: Maeda, Akiko
Palczewski, Krzysztof
ORCID: Kiser, Philip D.
Golczak, Marcin
Palczewski, Krzysztof
Venue: Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids
Publisher: Elsevier BV
Published: 2012-01
Volume: 1821
Issue: 1
Pages: 137-151
ISSN: 1388-1981 (ISSN-L)
DOI: 10.1016/j.bbalip.2011.03.005
PMC: PMC3158816
OpenAlex: W2000229924
Cited by: 177
References: 197
Citations by year: 2026: 12 · 2025: 6 · 2024: 8 · 2023: 7 · 2022: 13 · 2021: 10 · 2020: 9 · 2019: 14 · 2018: 12 · 2017: 12 · 2016: 13 · 2015: 12 · 2014: 16 · 2013: 16 · 2012: 12
FWCI: 1.39
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids (publishedVersion)
PubMed (publishedVersion)
Europe PMC (PubMed Central) (acceptedVersion)
PubMed Central (acceptedVersion)
Funders: National Institutes of Health (EY008061, P30 EY11373)
Foundation Fighting Blindness
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Retinal Development and Disorders
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Retinoids in leukemia and cellular processes
Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Photoreceptor and optogenetics research
Keywords: retinoid cycle, visual cycle, all-trans-retinal, 11-cis-retinal regeneration, rhodopsin, phototransduction, retinal degeneration, acyltransferase, short-chain dehydrogenase/reductase, oxygenase, photoreceptors, retinal pigment epithelium, vitamin A metabolism
MeSH terms: Retinoid Isomerohydrolase, Acyltransferases, Alcohol Oxidoreductases, Animals, Carrier Proteins, Eye Proteins, Humans, Phospholipids, Retina, Retinal Diseases, Retinaldehyde, Retinoids, Rhodopsin, Vision, Ocular, cis-trans-Isomerases, Photoreceptor Cells, Vertebrate, Mice, Rats

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Key enzymes of the retinoid (visual) cycle in vertebrate retina

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