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Structure and Function of Retinoid-Binding Proteins

  • Chapter
Fat-Soluble Vitamins

Part of the book series: Subcellular Biochemistry ((SCBI,volume 30))

Abstract

Biological processes which require compounds derived from vitamin A (retinol) include morphogenesis, spermatogenesis, the maintenance of epithelial tissue, and vision. For the last process the light-activated cis-trans isomerization of rhodopsin-bound retinaldehyde triggers a cascade of events which ultimately results in the hydrolysis of cyclic GMP. For morphogenesis, spermatogenesis, and the maintenance of epithelial tissue it is presumably retinoic acid that is the active metabolite. Both 9-cis and all-trans retinoic acid are transcriptional activators which exert their effects through binding to nuclear proteins that are members of the superfamily that includes the steroid hormone receptors. Various proteins mediate the transport and metabolism of the hydrophobic vitamin and consequently modulate the concentration of retinoic acid available to the nucleus. Both extracellular and intracellular retinoid-binding proteins have been identified in numerous cell types. In addition, the eye has retinoid binding proteins which are distinct for that organ: a cellular retinaldehyde-binding protein (CRalBP) and a interstitial/interphotoreceptor retinoid-binding protein (I-RBP).

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Authors and Affiliations

  1. Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, Tennessee, 37232-0146, USA

    Marcia E. Newcomer, R. Scott Jamison & David E. Ong

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  1. Marcia E. Newcomer
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  2. R. Scott Jamison
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  3. David E. Ong
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Editors and Affiliations

  1. King’s College London, University of London, London, UK

    Peter J. Quinn

  2. Department of Environmental and Occupational Health, and Department of Pharmacology, University of Pittsburgh, Pittsburgh, Pennsylvania, USA

    Valerian E. Kagan

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Newcomer, M.E., Jamison, R.S., Ong, D.E. (1998). Structure and Function of Retinoid-Binding Proteins. In: Quinn, P.J., Kagan, V.E. (eds) Fat-Soluble Vitamins. Subcellular Biochemistry, vol 30. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-1789-8_3

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  • DOI: https://doi.org/10.1007/978-1-4899-1789-8_3

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