Retinoic acid-binding protein, cellular,

Vitamin A absorbs UV light between 300 and 350 nm. After acute exposure to UVA or UVB a dose-dependent decrease of vitamin A was shown in mouse59 and humans.84 UV irradiation markedly reduced mRNA and protein of the nuclear retinoid receptors RARy and RXRa in humans and led to a near loss of retinoic acid induction of the RAR/RXR target genes and the cellular retinoic acid binding protein II thus effectively causing additionally a functional vitamin A deficiency.85... 

Anhydroretinol binds to plasma and intracellular RBPs, but not to the cellular retinoic acid binding proteins (CRABPs) or retinoid receptors. In experimental animals, it protects against the development of chemically induced tumors while showing none of the toxic effects of other retinoids. 

There are two cellular retinoic acid binding proteins ... 

Retinoic acid may either enter the target cell from the circulation or may be formed intraceUularly by oxidation of retinol. A number of tissues - but not muscle, kidneys, small intestines, liver, lungs, or spleen - have a cellular retinoic acid binding protein (CRABP) that is distinct from CRBP. Testis and... 

Delva L, Bastie JN, Rochette-Egly C, Kraiba R, Balitrand N, Despouy G, Chambon P, and Chomienne C (1999) Physical and functional interactions between cellular retinoic acid binding protein II and the retinoic acid-dependent nuclear complex. Molecular and Cell Biology 19,7158-67. 

Momoi T, Hanaoka K, and Momoi M (1990) Spatial and temporal expression of cellular retinoic acid binding protein (CRABP) along the anteroposterior axis in the central nervous system of mouse embryos. Biochemical and Biophysical Research Communications 169, 991-6. 

A Novel Method for Measuring the Binding Properties of the Site-Directed Mutants of the Proteins That Bind Hydrophobic Ligands Application to Cellular Retinoic Acid Binding Proteins... 

Many hydrophobic molecules such as vitamin A, vitamin D and steroid hormones play vital roles in a variety of cellular processes. Because of the low solubility of these molecules in water, it has been difficult to measure the binding properties of the site-directed mutants of the proteins that interact with these hydrophobic ligands such as cellular retinoic acid binding proteins (CRABPs) (Zhang et al. 1992 Chen et al. 1995). This has greatly hampered the studies of the quantitative structure-function relationships of these important proteins. 

Cellular retinoic acid-binding protein II CRABPII Not determined Giguere et al. (1990)... 

Budhu A, Gillilan R, Noy N. 2001. Localization of the RAR interaction domain of cellular retinoic acid binding protein II. J. Biol. Chem. 305 939 49... 

Dong D, Ruuska SE, Levinthal DJ, Noy N. 1999. Distinct roles for cellular retinoic acid binding proteins I and II in regulating signaling by retinoic acid. J. Biol. Chem. 274 23695-98... 

Wolf G. 2000. Cellular retinoic acid binding protein II a coactivator of the transactivation by the retinoic acid receptor complex RAR, RXR. Nutr. Rev. 58 151-53... 

Retinoic acids, particularly trans-RA, bind with high affinity to cellular retinoic acid binding proteins I and II (CRABPI and CRABPII). Like the CRBPs, CRABPs are widely ex-... 

Oxidation of retinol produces retinoic acid tretinoin). The reaction is irreversible. Retinoic acid enters the portal blood, is transported bound to albumin, and is not stored to any great extent. The concentration of retinoic acid in plasma is normally 3-4 ng/mL. A biologically active metabolite, 5,6-epoxyretinoic acid, has been isolated from the intestinal mucosa of vitamin A-deficient rats following administration of H-retinoic acid. Several tissues have specific cellular retinoic acid-binding proteins (CRABPs). 

Maden, M., Horton, C., Graham, A., Leonard, L., Pizzey, J., Siegenthaler, G., Lumsden, A., Eriksson, U. 1992. Domains of cellular retinoic acid-binding protein I (CRABP I) expression in the hindbrain and neural crest of the mouse embryo. Mech. Dev. 37, 13-23. 

Fund., Genet., 13, 87 (1992). Mutating the Charged Residues in the Binding Pocket of Cellular Retinoic Acid-Binding Protein Simultaneously Reduces Its Binding Affinity to Retinoic Acid and Increases Its Thermostability. 

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