Lecithin:Retinol Acyltransferase: A Key Enzyme Involved in the Retinoid (visual) Cycle
Open accessAbstract
Lecithin:retinol acyltransferase (LRAT) catalyzes the acyl transfer from the sn-1 position of phosphatidylcholine (PC) to all-trans-retinol, creating fatty acid retinyl esters (palmitoyl, stearoyl, and some unsaturated derivatives). In the eye, these retinyl esters are substrates for the 65 kDa retinoid isomerase (RPE65). LRAT is well characterized biochemically, and recent structural data from closely related family members of the NlpC/P60 superfamily and a chimeric protein have established its catalytic mechanism. Mutations in the LRAT gene are responsible for approximately 1% of reported cases of Leber congenital amaurosis (LCA). Lack of functional LRAT, expressed in the retinal pigmented epithelium (RPE), results in loss of the visual chromophore and photoreceptor degeneration. LCA is a rare hereditary retinal dystrophy with an early onset associated with mutations in one of 21 known genes. Protocols have been devised to identify therapeutics that compensate for mutations in RPE65, also associated with LCA. The same protocols can be adapted to combat dystrophies associated with LRAT. Improvement in the visual function of clinical recipients of therapy with recombinant adeno-associated virus (rAAV) vectors incorporating the RPE65 gene provides a proof of concept for LRAT, which functions in the same cell type and metabolic pathway as RPE65. In parallel, a clinical trial that employs oral 9-cis-retinyl acetate to replace the missing chromophore in RPE65 and LRAT causative disease has proven to be effective and free of adverse effects. This article summarizes the biochemistry of LRAT and examines chromophore replacement as a treatment for LCA caused by LRAT mutations.
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Inside the RPE, CRBP1 shuttles all-trans-retinol to LRAT, which converts all-trans-retinol to all-trans retinyl esters.
“Inside the RPE, CRBP1 shuttles all-trans-retinol to the enzyme retinol:lecithin acyltransferase (LRAT) which converts all-trans-retinol to all-trans retinyl esters [44,45].”
From The Role of Vitamin A in Retinal Diseases (2022) · cites this paper as [45]
Section 2.1 (Retinoid Cycle; page not provided) says all-trans-retinol reaches the RPE and is esterified there by LRAT. It identifies IRBP as transporting retinol to the RPE, but does not say that CRBP1 shuttles it to LRAT inside the RPE; that part of the claim is unsupported by our copy. (LLM, conf=0.86)
Experimental — accuracy not yet measuredPathogenic variants in LRAT cause LCA and RP.
“Pathogenic variants in LRAT gene cause LCA and RP [45,179,180].”
From The Role of Vitamin A in Retinal Diseases (2022) · cites this paper as [45]
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- [49]Fan J Rohrer B Frederick JM Baehr W Crouch RK 2008 Rpe65−/− and Lrat−/− mice: comparable models of leber congenital amaurosis Invest Ophthalmol Visual Sci 49 2384 2389 18296659 PMC2641010
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The Role of Vitamin A in Retinal Diseases
Sajovic, J., Meglič, A., Glavač, D., Markelj, Š., Hawlina, M., & Fakin, A. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23031014 · Cited by 109 · see citing works
“Inside the RPE, CRBP1 shuttles all-trans-retinol to the enzyme retinol:lecithin acyltransferase (LRAT) which converts all-trans-retinol to all-trans retinyl esters [44,45].”
BackgroundA novel LRAT mutation affecting splicing in a family with early onset retinitis pigmentosa
Chen, Y., Huang, L., Jiao, X., Riazuddin, S., Riazuddin, S. A., & Fielding Hetmancik, J. (2018) · Human Genomics · doi:10.1186/s40246-018-0165-3 · Cited by 18 · see citing works
- Authors
- Sears, A. E., & Palczewski, K.
- Affiliations
- Case Western Reserve University (US)
- Corresponding author
- Palczewski, Krzysztof
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2016-05-23
- Volume
- 55
- Issue
- 22
- Pages
- 3082-3091
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- PMC
- PMC5555363
- OpenAlex
- W2402884687
- Cited by
- 40
- References
- 68
- Citations by year
- 2026: 5 · 2025: 7 · 2024: 7 · 2023: 4 · 2022: 2 · 2021: 2 · 2020: 5 · 2019: 2 · 2018: 4 · 2017: 2
- FWCI
- 0.24
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Biochemistry (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- eScholarship (California Digital Library) (submittedVersion)
- Funders
- National Eye Institute (EY021126)
- 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
- Health Sciences › Medicine › Ophthalmology › Retinal Diseases and Treatments
- Keywords
- LRAT, retinoid cycle, retinyl esters, phosphatidylcholine, Leber congenital amaurosis, RPE65, retinal pigment epithelium, photoreceptor degeneration, retinal dystrophy, recombinant adeno-associated virus vectors, enzyme mechanism
- MeSH terms
- Acyltransferases, Amino Acid Sequence, Animals, Eye Diseases, Eye Proteins, Humans, Retinoids, Sequence Homology, Amino Acid
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