The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

Rbp2  -  retinol binding protein 2, cellular

Rattus norvegicus

Synonyms: CRBP-II, Cellular retinol-binding protein II, Crbpii, Retinol-binding protein 2
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of Rbp2


High impact information on Rbp2


Chemical compound and disease context of Rbp2

  • Efficient incorporation of 6-fluorotryptophan (93%) was achieved by growing a tryptophan auxotroph of E. coli harboring a prokaryotic expression vector with a full-length rat CRBP II cDNA on defined medium supplemented with the analog [5].

Biological context of Rbp2


Anatomical context of Rbp2


Associations of Rbp2 with chemical compounds


Physical interactions of Rbp2

  • Cellular retinol-binding protein II (CRBP-II) and intestinal fatty acid-binding protein (I-FABP) are both expressed in small intestinal enterocytes and exhibit 31% sequence identity [13].

Other interactions of Rbp2

  • The solution structure and dynamics of CRBP I and CRBP II were compared by multidimensional NMR techniques [7].
  • X-ray diffraction data suggest that the unit cell parameters of crystalline apo-CRBP II resemble those of I-FABP [1].
  • Electrophoretic mobility-shift assay revealed that both PPARalpha-RXRalpha and PPARdelta-RXRalpha heterodimers, specifically and in a dose-dependent manner, bound to the two PPRE-like elements of the rat CRBPII gene as well as the known PPREs in the L-FABP and acyl-CoA oxidase genes [14].
  • These results suggest that the possible perinatal RA production by RALDHs might regulate various RA-target genes including CRBPII and RARalpha through RXRalpha or HNF-4 in the small intestine [15].

Analytical, diagnostic and therapeutic context of Rbp2

  • Pulse-chase experiments in chick embryonic duodenal organ culture strongly suggest that 1,25-dihydroxyvitamin D3 markedly decreases the synthesis of CRBP II, while not changing the degradation rate [16].
  • Our ability to express CRBP II in Escherichia coli and to construct individual tryptophan substitution mutants by site-directed mutagenesis has provided a useful model system for studying the fluorescence of a multi-tryptophan protein [17].
  • Force-feeding a diet containing linoleic acid produced an elevation of CRBP II mRNA levels in rats in both a dose-dependent (0.053-0.21 mol/L) and time-dependent (up to 6 h) manner [12].
  • Gel shift assay showed that the binding activity of rat jejunal nuclear protein to the nuclear receptor response elements located in the rat CRBPII gene (RXRE and RE3) was greater in rats fed high-fat diet than in those fed fat-free diet and were enhanced by addition of bacterially expressed PPARalpha protein [18].
  • Oral administration of corn oil in the animals fed vitamin A-free diet elicited approximately threefold accumulation of CRBP II mRNA within 6 h [19].


  1. Crystallization of rat cellular retinol binding protein II. Preliminary X-ray data obtained from the apoprotein expressed in Escherichia coli. Sacchettini, J.C., Stockhausen, D., Li, E., Banaszak, L.J., Gordon, J.I. J. Biol. Chem. (1987) [Pubmed]
  2. Rat cellular retinol-binding protein II: use of a cloned cDNA to define its primary structure, tissue-specific expression, and developmental regulation. Li, E., Demmer, L.A., Sweetser, D.A., Ong, D.E., Gordon, J.I. Proc. Natl. Acad. Sci. U.S.A. (1986) [Pubmed]
  3. In vivo isomerization of retinoic acids. Rapid isomer exchange and gene expression. Kojima, R., Fujimori, T., Kiyota, N., Toriya, Y., Fukuda, T., Ohashi, T., Sato, T., Yoshizawa, Y., Takeyama, K., Mano, H. J. Biol. Chem. (1994) [Pubmed]
  4. Differential binding of retinol analogs to two homologous cellular retinol-binding proteins. Rong, D., Lovey, A.J., Rosenberger, M., d'Avignon, A., Ponder, J., Li, E. J. Biol. Chem. (1993) [Pubmed]
  5. Nuclear magnetic resonance studies of 6-fluorotryptophan-substituted rat cellular retinol-binding protein II produced in Escherichia coli. Analysis of the apoprotein and the holoprotein containing bound all-trans-retinol and all-trans-retinal. Li, E., Quian, S.J., Nader, L., Yang, N.C., d'Avignon, A., Sacchettini, J.C., Gordon, J.I. J. Biol. Chem. (1989) [Pubmed]
  6. The structure and dynamics of rat apo-cellular retinol-binding protein II in solution: comparison with the X-ray structure. Lu, J., Lin, C.L., Tang, C., Ponder, J.W., Kao, J.L., Cistola, D.P., Li, E. J. Mol. Biol. (1999) [Pubmed]
  7. Two homologous rat cellular retinol-binding proteins differ in local conformational flexibility. Lu, J., Cistola, D.P., Li, E. J. Mol. Biol. (2003) [Pubmed]
  8. Fluorine nuclear magnetic resonance analysis of the ligand binding properties of two homologous rat cellular retinol-binding proteins expressed in Escherichia coli. Li, E., Qian, S.J., Winter, N.S., d'Avignon, A., Levin, M.S., Gordon, J.I. J. Biol. Chem. (1991) [Pubmed]
  9. Alteration of the binding specificity of cellular retinol-binding protein II by site-directed mutagenesis. Cheng, L., Qian, S.J., Rothschild, C., d'Avignon, A., Lefkowith, J.B., Gordon, J.I., Li, E. J. Biol. Chem. (1991) [Pubmed]
  10. Comparison of the ligand binding properties of two homologous rat apocellular retinol-binding proteins expressed in Escherichia coli. Levin, M.S., Locke, B., Yang, N.C., Li, E., Gordon, J.I. J. Biol. Chem. (1988) [Pubmed]
  11. Characterization of rat cellular retinol-binding protein II expressed in Escherichia coli. Li, E., Locke, B., Yang, N.C., Ong, D.E., Gordon, J.I. J. Biol. Chem. (1987) [Pubmed]
  12. Unsaturated fatty acids regulate gene expression of cellular retinol-binding protein, type II in rat jejunum. Suruga, K., Suzuki, R., Goda, T., Takase, S. J. Nutr. (1995) [Pubmed]
  13. Ligand-protein electrostatic interactions govern the specificity of retinol- and fatty acid-binding proteins. Jakoby, M.G., Miller, K.R., Toner, J.J., Bauman, A., Cheng, L., Li, E., Cistola, D.P. Biochemistry (1993) [Pubmed]
  14. Modulation of the expression of peroxisome proliferator-activated receptor-dependent genes through disproportional expression of two subtypes in the small intestine. Mochizuki, K., Suruga, K., Kitagawa, M., Takase, S., Goda, T. Arch. Biochem. Biophys. (2001) [Pubmed]
  15. Developmental changes of the expression of the genes regulated by retinoic acid in the small intestine of rats. Ogura, Y., Suruga, K., Takase, S., Goda, T. Life Sci. (2005) [Pubmed]
  16. Regulation of cellular retinol binding protein type II by 1,25-dihydroxyvitamin D3. Finlay, J.A., Strom, M., Ong, D.E., DeLuca, H.F. Biochemistry (1990) [Pubmed]
  17. Fluorescence studies of rat cellular retinol binding protein II produced in Escherichia coli: an analysis of four tryptophan substitution mutants. Locke, B.C., MacInnis, J.M., Qian, S., Gordon, J.I., Li, E., Fleming, G.R., Yang, N.C. Biochemistry (1992) [Pubmed]
  18. Transcriptional regulation of cellular retinol-binding protein, type II gene expression in small intestine by dietary fat. Suruga, K., Mochizuki, K., Kitagawa, M., Goda, T., Horie, N., Takeishi, K., Takase, S. Arch. Biochem. Biophys. (1999) [Pubmed]
  19. Dietary fatty acids are possible key determinants of cellular retinol-binding protein II gene expression. Takase, S., Tanaka, K., Suruga, K., Kitagawa, M., Igarashi, M., Goda, T. Am. J. Physiol. (1998) [Pubmed]
WikiGenes - Universities