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Gene Review

OPSN  -  opsin

Bos taurus

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Disease relevance of OPSN

  • Expression levels of functional bovine opsin in the insect cell line IPLB-Sf9 using recombinant baculovirus were shown not to depend on the use of novel transfer vectors (pAcRP23, pAcDZ1) that were reported to improve biosynthesis levels of other proteins in this system [1].
  • We found that binding of 11-cis-retinal to opsin mutants with single amino acid changes at Trp-265 (W265F,Y,A) and a retinitis pigmentosa mutant (A164V) was far from complete and required much higher concentrations of 11-cis-retinal [2].
  • The opsin gene is under the control of the immediate-early cytomegalovirus promoter/enhancer in an expression vector that also contains a selectable marker (Neo) governed by a relatively weak promoter [3].
  • Recombinant adeno-associated virus (rAAV) vectors incorporating a proximal bovine rod opsin promoter were used to transfer either hairpin or hammerhead ribozyme genes to photoreceptors [4].
  • In terms of formation of an intermediate addition compound and subsequent dehydration, the values for the individual rate constants for both bleached rod outer segments and cholate-solubilized opsin were found to compare very favorably [5].

High impact information on OPSN

  • We have isolated cDNA clones generated from the mRNA encoding the opsin apoprotein of bovine rhodopsin and used these cDNAs to isolate genomic DNA clones containing the complete opsin gene [6].
  • By deletion of selected segments from a bovine opsin complementary DNA clone and subsequent analysis of transcripts in a cell-free translation-translocation system, we have localized two out of four theoretically conceivable signal sequences required for the integration of opsin into microsomal membranes [7].
  • In vitro biosynthesis, core glycosylation, and membrane integration of opsin [8].
  • Immunocytochemical localization of opsin in outer segments and Golgi zones of frog photoreceptor cells. An electron microscope analysis of cross-linked albumin-embedded retinas [9].
  • Specific binding of anti-opsin antibodies indicates that opsin is localized in the disks of rod outer segments (ROS), as expected, and in the Golgi zone of the rod cell inner segments [9].

Chemical compound and disease context of OPSN


Biological context of OPSN

  • RNase protection assays specific for each cell type-specific gene were used to compare mRNA levels for bovine rod and blue cone gamma subunits of cGMP phosphodiesterase and rhodopsin and red cone opsin from before transcriptional induction (4 months gestation) to the adult [13].
  • The ability of rhodopsin to activate PDE may be inhibited by the phosphorylation of sites exposed on the opsin surface as a result of light-induced conformational changes [14].
  • Under the conditions used for cell growth in suspension, opsin is produced at saturated culture levels of more than 2 mg/liter [3].
  • In addition, systematic analysis of the chromophore-binding pocket in rhodopsin and cone pigments has led to an improved understanding of the mechanism of the opsin shift, and of particular molecular determinants underlying color vision in humans [15].
  • Upon photoisomerization, major structural rearrangements that involve protonation of the active site Glu113 and cytoplasmic acidic residues, including Glu134, lead to the formation of the active form of the receptor, metarhodopsin II b, which decays to opsin [16].

Anatomical context of OPSN

  • METHODS: Transgenic Drosophila expressing the bovine opsin gene (Rho) in photoreceptors were created [17].
  • The bovine opsin gene (Rho) was expressed in Drosophila, to examine the properties of a vertebrate opsin within invertebrate photoreceptor cells [17].
  • The resulting cell lines produce 100-200 micrograms of bovine opsin per liter of saturated tissue culture medium (10(9) cells) [18].
  • Addition of phospholipids, either from soybean or rod outer segment, prior to bleaching stabilized the initially formed opsin, resulting in much higher chromophore regeneration [19].
  • All five opsin polypeptide fragments were stably produced upon expression of the corresponding gene fragments in COS-1 cells [20].

Associations of OPSN with chemical compounds


Physical interactions of OPSN

  • The fact that 7-cis-rhodopsin can be readily converted to rhodopsin and to 9-cis-rhodopsin shows that the identical retinal binding site of opsin is involved in the three isomeric rhodopsins [26].
  • The quantum efficiency of photoisomerization for CRALBP X 11-cis-retinaldehyde was determined by comparing the rate of photoisomerization of 11-cis-retinaldehyde bound to purified CRALBP and opsin [27].
  • These results demonstrate that the sodium cholate (2 mg/ml) maintains opsin in a conformation very similar to that in the rod outer segment membrane and suggest that the cholate-opsin complex is an excellent model system for studies on opsin-membrane interactions [5].
  • To this end, studies revealed that protamine was binding to the particulate substrate in a ratio of protamine/opsin of 0.7:1 [28].

Enzymatic interactions of OPSN

  • In this work we test this idea by determining whether two constitutively active opsin mutants are phosphorylated by rhodopsin kinase [29].

Other interactions of OPSN

  • The extent of regeneration was graded with the quantities of IRBP and opsin introduced into the RPE-eyecup [30].
  • We found that opsin mutants where Lys-296 is replaced either by Glu (K296E) or by Gly (K296G) are not substrates of rhodopsin kinase in the absence of chromophore [29].
  • The influence of compounds that might modulate the reaction was also examined. alpha-Lactalbumin, a modifier of the galactosyltransferase in milk, acted as a competitive inhibitor of the galactosylation of opsin [31].
  • RNase protection assays were used to follow rhodopsin and red cone opsin mRNA levels during bovine fetal development as a function of retinal position [32].
  • With the use of antisera against bovine retinal S-antigen and bovine opsin the authors demonstrate that in cerebellar medulloblastomas certain tumor cells display immunocytochemical properties characteristic of retinal photoreceptors and pinealocytes [33].

Analytical, diagnostic and therapeutic context of OPSN


  1. In vitro expression of bovine opsin using recombinant baculovirus: the role of glutamic acid (134) in opsin biosynthesis and glycosylation. Jansen, J.J., Mulder, W.R., De Caluwé, G.L., Vlak, J.M., De Grip, W.J. Biochim. Biophys. Acta (1991) [Pubmed]
  2. Structure and function in rhodopsin: kinetic studies of retinal binding to purified opsin mutants in defined phospholipid-detergent mixtures serve as probes of the retinal binding pocket. Reeves, P.J., Hwa, J., Khorana, H.G. Proc. Natl. Acad. Sci. U.S.A. (1999) [Pubmed]
  3. Structure and function in rhodopsin: high level expression of a synthetic bovine opsin gene and its mutants in stable mammalian cell lines. Reeves, P.J., Thurmond, R.L., Khorana, H.G. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
  4. Ribozyme rescue of photoreceptor cells in P23H transgenic rats: long-term survival and late-stage therapy. LaVail, M.M., Yasumura, D., Matthes, M.T., Drenser, K.A., Flannery, J.G., Lewin, A.S., Hauswirth, W.W. Proc. Natl. Acad. Sci. U.S.A. (2000) [Pubmed]
  5. Characterization of the recombination reaction of rhodopsin. Henselman, R.A., Cusanovich, M.A. Biochemistry (1976) [Pubmed]
  6. Isolation, sequence analysis, and intron-exon arrangement of the gene encoding bovine rhodopsin. Nathans, J., Hogness, D.S. Cell (1983) [Pubmed]
  7. Bovine opsin has more than one signal sequence. Friedlander, M., Blobel, G. Nature (1985) [Pubmed]
  8. In vitro biosynthesis, core glycosylation, and membrane integration of opsin. Goldman, B.M., Blobel, G. J. Cell Biol. (1981) [Pubmed]
  9. Immunocytochemical localization of opsin in outer segments and Golgi zones of frog photoreceptor cells. An electron microscope analysis of cross-linked albumin-embedded retinas. Papermaster, D.S., Schneider, B.G., Zorn, M.A., Kraehenbuhl, J.P. J. Cell Biol. (1978) [Pubmed]
  10. Structure and function in rhodopsin: a tetracycline-inducible system in stable mammalian cell lines for high-level expression of opsin mutants. Reeves, P.J., Kim, J.M., Khorana, H.G. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  11. Histidine tagging both allows convenient single-step purification of bovine rhodopsin and exerts ionic strength-dependent effects on its photochemistry. Janssen, J.J., Bovee-Geurts, P.H., Merkx, M., DeGrip, W.J. J. Biol. Chem. (1995) [Pubmed]
  12. A comparison of the efficiency of G protein activation by ligand-free and light-activated forms of rhodopsin. Melia, T.J., Cowan, C.W., Angleson, J.K., Wensel, T.G. Biophys. J. (1997) [Pubmed]
  13. Parallel regulation of fetal gene expression in different photoreceptor cell types. van Ginkel, P.R., Hauswirth, W.W. J. Biol. Chem. (1994) [Pubmed]
  14. Activation of rhodopsin phosphorylation is triggered by the lumirhodopsin-metarhodopsin I transition. Paulsen, R., Bentrop, J. Nature (1983) [Pubmed]
  15. Rhodopsin: a prototypical G protein-coupled receptor. Sakmar, T.P. Prog. Nucleic Acid Res. Mol. Biol. (1998) [Pubmed]
  16. Mechanisms of opsin activation. Buczyłko, J., Saari, J.C., Crouch, R.K., Palczewski, K. J. Biol. Chem. (1996) [Pubmed]
  17. Heterologous expression of bovine rhodopsin in Drosophila photoreceptor cells. Ahmad, S.T., Natochin, M., Barren, B., Artemyev, N.O., O'Tousa, J.E. Invest. Ophthalmol. Vis. Sci. (2006) [Pubmed]
  18. Production of bovine rhodopsin by mammalian cell lines expressing cloned cDNA: spectrophotometry and subcellular localization. Nathans, J., Weitz, C.J., Agarwal, N., Nir, I., Papermaster, D.S. Vision Res. (1989) [Pubmed]
  19. Structure and function in rhodopsin: the fate of opsin formed upon the decay of light-activated metarhodopsin II in vitro. Sakamoto, T., Khorana, H.G. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
  20. In vivo assembly of rhodopsin from expressed polypeptide fragments. Ridge, K.D., Lee, S.S., Yao, L.L. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
  21. G protein-coupled receptor rhodopsin: a prospectus. Filipek, S., Stenkamp, R.E., Teller, D.C., Palczewski, K. Annu. Rev. Physiol. (2003) [Pubmed]
  22. Primary photochemical event in vision: proton translocation. Peters, K., Applebury, M.L., Rentzepis, P.M. Proc. Natl. Acad. Sci. U.S.A. (1977) [Pubmed]
  23. Structure and function in rhodopsin: expression of functional mammalian opsin in Saccharomyces cerevisiae. Mollaaghababa, R., Davidson, F.F., Kaiser, C., Khorana, H.G. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
  24. Rapid-flow resonance Raman spectroscopy of photolabile molecules: rhodopsin and isorhodopsin. Mathies, R., Oseroff, A.R., Stryer, L. Proc. Natl. Acad. Sci. U.S.A. (1976) [Pubmed]
  25. Palmitoylation of bovine opsin and its cysteine mutants in COS cells. Karnik, S.S., Ridge, K.D., Bhattacharya, S., Khorana, H.G. Proc. Natl. Acad. Sci. U.S.A. (1993) [Pubmed]
  26. Photochemical studies of 7-cis-rhodopsin at low temperatures. Nature and properties of the bathointermediate. Kawamura, S., Miyatani, S., Matsumoto, H., Yoshizawa, T., Liu, R.S. Biochemistry (1980) [Pubmed]
  27. Photochemistry and stereoselectivity of cellular retinaldehyde-binding protein from bovine retina. Saari, J.C., Bredberg, D.L. J. Biol. Chem. (1987) [Pubmed]
  28. The phospho-opsin phosphatase from bovine rod outer segments. An insight into the mechanism of stimulation of type-2A protein phosphatase activity by protamine. King, A.J., Andjelkovic, N., Hemmings, B.A., Akhtar, M. Eur. J. Biochem. (1994) [Pubmed]
  29. Opsins with mutations at the site of chromophore attachment constitutively activate transducin but are not phosphorylated by rhodopsin kinase. Robinson, P.R., Buczyłko, J., Ohguro, H., Palczewski, K. Proc. Natl. Acad. Sci. U.S.A. (1994) [Pubmed]
  30. Interphotoreceptor retinoid-binding protein promotes rhodopsin regeneration in toad photoreceptors. Okajima, T.I., Pepperberg, D.R., Ripps, H., Wiggert, B., Chader, G.J. Proc. Natl. Acad. Sci. U.S.A. (1990) [Pubmed]
  31. In vitro galactosylation of rhodopsin and opsin: kinetics, properties and characterization. Ju, J.M., Kean, E.L. Exp. Eye Res. (1992) [Pubmed]
  32. Topographical regulation of cone and rod opsin genes: parallel, position dependent levels of transcription. van Ginkel, P.R., Timmers, A.M., Szél, A., Hauswirth, W.W. Brain Res. Dev. Brain Res. (1995) [Pubmed]
  33. Immunocytochemical evidence of molecular photoreceptor markers in cerebellar medulloblastomas. Korf, H.W., Czerwionka, M., Reiner, J., Schachenmayr, W., Schalken, J.J., de Grip, W., Gery, I. Cancer (1987) [Pubmed]
  34. Characterization of rhodopsin mutants that bind transducin but fail to induce GTP nucleotide uptake. Classification of mutant pigments by fluorescence, nucleotide release, and flash-induced light-scattering assays. Ernst, O.P., Hofmann, K.P., Sakmar, T.P. J. Biol. Chem. (1995) [Pubmed]
  35. The catalytic subunit of phosphatase 2A dephosphorylates phosphoopsin. Palczewski, K., Hargrave, P.A., McDowell, J.H., Ingebritsen, T.S. Biochemistry (1989) [Pubmed]
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