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Retinoid-binding proteins: mediators of retinoid action
Open accessAbstract
Active vitamin A metabolites, known as retinoids, are essential for multiple physiological processes, ranging from vision to embryonic development. These small hydrophobic compounds associate in vivo with soluble proteins that are present in a variety of cells and in particular extracellular compartments, and which bind different types of retinoids with high selectivity and affinity. Traditionally, retinoid-binding proteins were viewed as transport proteins that act by solubilizing and protecting their labile ligands in aqueous spaces. It is becoming increasingly clear, however, that, in addition to this general role, retinoid-binding proteins have diverse and specific functions in regulating the disposition, metabolism and activities of retinoids. Some retinoid-binding proteins appear to act by sequestering their ligands, thereby generating concentration gradients that allow cells to take up retinoids from extracellular pools and metabolic steps to proceed in energetically unfavourable directions. Other retinoid-binding proteins regulate the metabolic fates of their ligands by protecting them from some enzymes while allowing metabolism by others. In these cases, delivery of a bound retinoid from the binding protein to the ‘correct’ enzyme is likely to be mediated by direct and specific interactions between the two proteins. One retinoid-binding protein was reported to enhance the ability of its ligand to regulate gene transcription by directly delivering this retinoid to the transcription factor that is activated by it. ‘Channelling’ of retinoids between their corresponding binding protein and a particular protein target thus seems to be a general theme through which some retinoid-binding proteins exert their effects.
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“CRBP I is expressed in many tissues, including the eye, whereas CRBP II expression is restricted to the intestine.”
From Chemistry of the Retinoid (Visual) Cycle (2014) · cites this paper as [494]
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“Two retinoid-binding proteins are specifically expressed in the eye.494”
From Chemistry of the Retinoid (Visual) Cycle (2014) · cites this paper as [494]
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“Two isoforms of the protein, CRBP I and CRBP II with ∼50% sequence identity depending on the species, exhibit differential tissue expression.494”
From Chemistry of the Retinoid (Visual) Cycle (2014) · cites this paper as [494]
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Metadata
- Authors
- NOY, N.
- Affiliations
- Cornell University (US)
- Corresponding author
- NOY, Noa
- ORCID
- NOY, Noa
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 2000-06-07
- Volume
- 348
- Issue
- 3
- Pages
- 481-495
- ISSN
- 0264-6021 (ISSN-L)
- 1470-8728
- PMC
- PMC1221089
- OpenAlex
- W2001405592
- Cited by
- 422
- References
- 146
- Citations by year
- 2026: 8 · 2025: 8 · 2024: 6 · 2023: 3 · 2022: 15 · 2021: 9 · 2020: 14 · 2019: 14 · 2018: 14 · 2017: 13 · 2016: 23 · 2015: 17 · 2014: 17 · 2013: 27 · 2012: 14
- FWCI
- 5.67
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Biochemical Journal (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5r01ey009296-07)
- National Eye Institute (EY09296)
- National Cancer Institute (CA 68150, R01CA068150)
- 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 › Protein Interaction Studies and Fluorescence Analysis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Cholesterol and Lipid Metabolism
- Keywords
- retinoid-binding proteins, retinoids, vitamin A metabolites, retinoid transport, vitamin A metabolism, concentration gradient, protein-protein interaction, transcriptional regulation, transcription factors
- MeSH terms
- Animals, Humans, Models, Molecular, Protein Conformation, Retinoids, Retinol-Binding Proteins
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