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Gene Review

RLBP1  -  retinaldehyde binding protein 1

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High impact information on RLBP1


Biological context of RLBP1

  • The complete amino acid sequence of CRALBP from bovine retina has been determined by direct microanalysis of the protein [5].
  • These results provide a basis for a systematic higher resolution mutagenesis study directed toward correlating CRALBP structural domains with function [6].
  • Nick-translated bovine CRALBP cDNA probes were then used to clone from a human retinal cDNA library a 1317-base pair cDNA encoding human CRALBP [7].
  • Residues Gln-210 and Lys-221 are located within a region of CRALBP exhibiting sequence homology with the ligand binding cavity of yeast phosphatidylinositol-transfer protein [4].
  • Buried and solvent-exposed lysine residues were identified in bovine CRALBP by reductive methylation of the holoprotein followed by denaturation and reaction with [3H]acetic anhydride [4].

Anatomical context of RLBP1

  • However, CRALBP is also present in optic nerve and brain where its natural ligand and function are not yet known [4].
  • In adult rat and mouse optic nerves, the CRALBP(+) somata showed the same distribution as oligodendrocytes [8].
  • METHODS: An overlay assay was used to detect interactions of CRALBP with components of RPE microsomes [9].
  • Immunoperoxidase cytochemistry and double labeling immunofluorescence revealed CRALBP(+) cells in brain that resembled oligondendrocytes and not astrocytes, microglial cells, or pinealocytes [8].
  • Differential expression of the cellular retinaldehyde-binding protein in bovine ciliary epithelium [10].

Associations of RLBP1 with chemical compounds

  • Cellular retinaldehyde-binding protein (CRALBP) carries 11-cis-retinol or 11-cis-retinaldehyde as endogenous ligands and may function as a substrate carrier protein that modulates interaction of these retinoids with visual cycle enzymes [6].
  • The amino acid sequence deduced from the cDNA corresponds exactly to that determined by direct analysis of NH2-terminally acetylated bovine CRALBP (Crabb, J. W., Johnson, C. M., Carr, S. A., Armes, L. G., and Saari, J. C. (1988) J. Biol. Chem. 263, 18678-18687) [7].
  • Localization of CRALBP in RPE corroborates previous biochemical studies; its presence in the Müller cell suggests that this glial cell may play a hitherto unsuspected role in vitamin A metabolism in retina [1].
  • Ligand interactions determine the physiological role of CRALBP in the RPE where the protein is thought to function as a substrate carrier for 11-cis-retinol dehydrogenase in the synthesis of 11-cis-retinal for visual pigment regeneration [4].
  • Procedures are described for labeling CRALBP with 9-cis-retinaldehyde, 11-cis-retinaldehyde, or 11-cis-retinol [11].

Physical interactions of RLBP1


Other interactions of RLBP1


Analytical, diagnostic and therapeutic context of RLBP1


  1. Immunocytochemical localization of two retinoid-binding proteins in vertebrate retina. Bunt-Milam, A.H., Saari, J.C. J. Cell Biol. (1983) [Pubmed]
  2. Isomerization of 11-cis-retinoids to all-trans-retinoids in vitro and in vivo. McBee, J.K., Van Hooser, J.P., Jang, G.F., Palczewski, K. J. Biol. Chem. (2001) [Pubmed]
  3. Preferential release of 11-cis-retinol from retinal pigment epithelial cells in the presence of cellular retinaldehyde-binding protein. Stecher, H., Gelb, M.H., Saari, J.C., Palczewski, K. J. Biol. Chem. (1999) [Pubmed]
  4. Cellular retinaldehyde-binding protein ligand interactions. Gln-210 and Lys-221 are in the retinoid binding pocket. Crabb, J.W., Nie, Z., Chen, Y., Hulmes, J.D., West, K.A., Kapron, J.T., Ruuska, S.E., Noy, N., Saari, J.C. J. Biol. Chem. (1998) [Pubmed]
  5. The complete primary structure of the cellular retinaldehyde-binding protein from bovine retina. Crabb, J.W., Johnson, C.M., Carr, S.A., Armes, L.G., Saari, J.C. J. Biol. Chem. (1988) [Pubmed]
  6. Topological and epitope mapping of the cellular retinaldehyde-binding protein from retina. Crabb, J.W., Gaur, V.P., Garwin, G.G., Marx, S.V., Chapline, C., Johnson, C.M., Saari, J.C. J. Biol. Chem. (1991) [Pubmed]
  7. Cloning of the cDNAs encoding the cellular retinaldehyde-binding protein from bovine and human retina and comparison of the protein structures. Crabb, J.W., Goldflam, S., Harris, S.E., Saari, J.C. J. Biol. Chem. (1988) [Pubmed]
  8. Cellular retinaldehyde-binding protein is expressed by oligodendrocytes in optic nerve and brain. Saari, J.C., Huang, J., Possin, D.E., Fariss, R.N., Leonard, J., Garwin, G.G., Crabb, J.W., Milam, A.H. Glia (1997) [Pubmed]
  9. Cellular retinaldehyde-binding protein interacts with ERM-binding phosphoprotein 50 in retinal pigment epithelium. Nawrot, M., West, K., Huang, J., Possin, D.E., Bretscher, A., Crabb, J.W., Saari, J.C. Invest. Ophthalmol. Vis. Sci. (2004) [Pubmed]
  10. Differential expression of the cellular retinaldehyde-binding protein in bovine ciliary epithelium. Martin-Alonso, J.M., Ghosh, S., Hernando, N., Crabb, J.W., Coca-Prados, M. Exp. Eye Res. (1993) [Pubmed]
  11. Purification of cellular retinaldehyde-binding protein from bovine retina and retinal pigment epithelium. Saari, J.C., Bredberg, D.L. Exp. Eye Res. (1988) [Pubmed]
  12. Photochemistry and stereoselectivity of cellular retinaldehyde-binding protein from bovine retina. Saari, J.C., Bredberg, D.L. J. Biol. Chem. (1987) [Pubmed]
  13. Properties and immunocytochemical localization of three retinoid-binding proteins from bovine retina. Saari, J.C., Bunt-Milam, A.H., Bredberg, D.L., Garwin, G.G. Vision Res. (1984) [Pubmed]
  14. Promotion of the release of 11-cis-retinal from cultured retinal pigment epithelium by interphotoreceptor retinoid-binding protein. Carlson, A., Bok, D. Biochemistry (1992) [Pubmed]
  15. Retinoid-binding proteins in cone-dominant retinas. Anderson, D.H., Neitz, J., Saari, J.C., Kaska, D.D., Fenwick, J., Jacobs, G.H., Fisher, S.K. Invest. Ophthalmol. Vis. Sci. (1986) [Pubmed]
  16. Transplantation of retinal pigment epithelium using viable cryopreserved cells. Durlu, Y.K., Tamai, M. Cell transplantation. (1997) [Pubmed]
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