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PubMed1994

A human opsin-related gene that encodes a retinaldehyde-binding protein.

The ligand-binding property of a cytoplasmic membrane-bound protein from bovine retinal pigment epithelium (RPE) has been demonstrated. The putative RPE-retinal G protein coupled receptor (RGR) covalently binds both all-trans- and 11-cis-retinal after reduction by sodium borohydride. The 32-kDa receptor binds all-trans-retinal preferentially, rather than the 11-cis isomer. The amino acid sequence of the opsin-related protein in humans is 86% identical to that of bovine RGR, and a lysine residue, analogous to the retinaldehyde attachment site of rhodopsin, is conserved in the seventh transmembrane domain of RGR in both species. The human gene that encodes the novel retinaldehyde receptor spans 14.8 kb and is split into seven exons. The structure of the gene is distinct from that of the visual pigment genes. These findings support the notion that the rgr gene represents the earliest independent branch of the vertebrate opsin gene family. A second form of human RGR in retina is predicted by alternative splicing of its precursor mRNA. This RGR variant results from the alternative use of an internal acceptor splice site in the second intron of the human gene, and it contains an insertion of four amino acids in the connecting loop between the second and thrid transmembrane domains. Since RGR binds all-trans-retinal preferentially, one of its functions may be to catalyze isomerization of the chromophore by a retinochrome-like mechanism.

Amino Acid Sequence↗
PubMed1986

Identification of the sites in opsin modified by photoactivated azido[125I]iodobenzene.

Opsin labelled with photoactivated 1-azido-4-[125I]iodobenzene was proteolysed in situ with Staphylococcus aureus V8 proteinase to yield two radioactive membrane-bound fragments. These were separated, cleaved with CNBr and the resultant peptides sequenced in order to locate the radiolabelled residues. In the whole molecule, there was clear evidence for modification of at least 20 sites, identified as derivatives of cysteine, tryptophan, tyrosine, histidine and lysine residues. The probe primary reacted, therefore, with nucleophilic substituents. The positions of the modified sites relative to the confines of the phospholipid bilayer were consistent with all other studies on the disposition of the polypeptide chain. The location of these sites substantiated an earlier suggestion that not all the transmembrane segments should be regarded as continuous regular alpha-helices.

Amino Acid Sequence↗
PubMed2006

Exploring RPE as a source of photoreceptors: differentiation and integration of transdifferentiating cells grafted into embryonic chick eyes.

PURPOSE: To study the possibility of generating photoreceptors through programming RPE transdifferentiation by examining cell differentiation after transplantation into the developing chick eye. METHODS: RPE was isolated, and the cells were dissociated, cultured, and guided to transdifferentiate by infection with retrovirus expressing neuroD (RCAS-neuroD), using RCAS-green fluorescence protein (GFP) as a control. The cells were then harvested and microinjected into the developing eyes of day 5 to day 7 chick embryos, and their development and integration were analyzed. RESULTS: Cells from the control culture integrated into the host RPE. When grafted cells were present in large number, multilayered RPE-like tissues were formed, and the extra tissues consisted of grafted cells and host cells. None of the cells from the control culture expressed photoreceptor-specific genes. In contrast, most cells from RCAS-neuroD-infected culture remained depigmented. A large number of them expressed photoreceptor-specific genes, such as visinin and opsins. Antibodies against red opsin decorated the apical tips and the cell bodies of the grafted, transdifferentiating cells. In the subretinal space, visinin(+) cells aligned along the RPE or an RPE-like structure. When integrated into the host outer nuclear layer, grafted cells emanated elaborate, axonal arborization into the outer plexiform layer of the host retina. CONCLUSIONS: Cultured RPE cells retained their remarkable regenerative capabilities. Cells guided to transdifferentiate along the photoreceptor pathway by neuroD developed a highly ordered cellular structure and could integrate into the outer nuclear layer. These data suggest that, through genetic programming, RPE cells could be a potential source of photoreceptor cells.

Animals↗
PubMed2000

Ultraviolet and violet receptors express identical mRNA encoding an ultraviolet-absorbing opsin: identification and histological localization of two mRNAs encoding short-wavelength-absorbing opsins in the retina of the butterfly Papilio xuthus.

This paper describes the primary structures of two opsins of short-wavelength-absorbing visual pigments deduced from the mRNA sequences in the retina of the Japanese yellow swallowtail butterfly Papilio xuthus. A phylogenetic analysis of the amino acid sequences indicates that one of these visual pigments is of the ultraviolet-absorbing type and that the other is of the blue-absorbing type. We identified the photoreceptor cells that express these mRNAs by histological in situ hybridization. The mRNA of the ultraviolet type is expressed in two distinct photoreceptor types previously identified as ultraviolet and violet receptors, providing the first molecular biological evidence that different types of spectral receptor probably express a visual pigment with an identical amino acid sequence. The mRNA of the blue type is expressed exclusively in cells classified as blue receptors.

Amino Acid Sequence↗
PubMed1996

Histopathological and immunocytochemical demonstration of retinal degeneration in the squirrel monkey.

Here we describe the spontaneous appearance of a retinal degeneration in two squirrel monkeys (New World monkey). Since the retinal pathology sufficiently resembles that seen in human degenerative disorder, studies of degeneration in monkeys could contribute to the prevention and treatment of the human disorder. The histopathological examination of horizontal sections comprising the optic disc and the fovea revealed photoreceptor outer and inner segments only in the central fovea. The morphology of the photoreceptors and outer nuclear layer changed rapidly away from the central fovea. There was a loss of outer segments, a shortening of inner segments and disorganized and flattened cells were found in the outer nuclear layer. AO labelling not only detected opsin in the few areas where outer segments were present, but also in the inner segments and the outer nuclear layer. The OS-2 antibody failed to stain the outer segments of the blue sensitive cones. The COS-1 antibody stained many red/green sensitive cones in the fovea, but their density decreased quickly outside this region. Thus, we have detected retinal degeneration in two outbred squirrel monkeys who were being examined for other reasons unrelated to research in retinal degeneration. One was feral and the other was only two generations removed from the feral state. The identification of retinal degeneration in a non-human primate holds great promise for the development of a treatment for human retinitis pigmentosa because access to a primate model would be of invaluable importance for studying the biochemistry behind these disorders.

Animals↗
PubMed2003

Targeted knockdown of an opsin gene inhibits the swimming behaviour photoresponse of ascidian larvae.

The sequencing of the ascidian Ciona intestinalis genome was completed at the end of 2002. Effective targeted gene knockdown in this model chordate would greatly enhance understanding of how the genes affect the function of the neurons that underlie behaviour. We show here that antisense morpholinos (MOs) are effective and specific translational inhibitors in C. intestinalis larvae. The larvae developed from eggs injected with a Ci-opsin1 MO lost their photoresponse, which affected their swimming behaviour. Immunohistochemical analysis showed that the expression of Ci-opsin1, the visual pigments in the photoreceptor of the ocellus, had been lost in the larvae with the Ci-opsin1 MO. The inhibition of the photic behaviour of the knockdown larvae is solely due to the suppression of the synthesis of the visual pigments in the photoreceptors. These are the first results showing the knockdown of an ascidian gene and the elucidation of that gene's role in ascidian larval behaviour.

Animals↗
PubMed1996

Point mutations in bovine opsin can be classified in four groups with respect to their effect on the biosynthetic pathway of opsin.

Expression in vitro with the recombinant baculovirus expression system showed correct biosynthesis and post-translational processing of "wild-type' bovine opsin with regard to translocation, glycosylation, palmitoylation and targeting. However, several of these processes were severely affected by point mutations. From the overall results of 16 mutants reported here, four groups were distinguished. One group significantly affected neither biosynthesis nor folding of opsin (D83N, P291A, A299C-V300A-P303G). A second group produced a truncated protein (R69H, Y301F), suggesting that these positions are essential for a correct translational process. A third group affected membrane translocation as well as glycosylation, which can be interpreted as interference with the function of a transfer signal. Substitutions at positions Glu-113, Glu-122, Glu-134, Arg-135 and Lys-248 belong to this category. A fourth group induced structural changes in the protein that led to heterogeneous distribution in the plasma membrane (E113Q/D, W265F, Y268S). Taking any functional consequences of these mutations into consideration, it seems that point mutations can have mosaic effects and therefore should be examined at several levels (folding, targeting, functional parameters).

Amino Acid Sequence↗
PubMed2006

Novel retinylidene iminium salts for defining opsin shifts: synthesis and intrinsic chromophoric properties.

Retinal Schiff bases serve as chromophores in many photoactive proteins that carry out functions such as signalling and light-induced ion translocation. The retinal Schiff base can be found as neutral or protonated, as all-trans, 11-cis or 13-cis isomers and can adopt different conformations in the protein binding pocket. Here we present the synthesis and characterisation of isomeric retinylidene iminium salts as mimics blocked towards isomerisation at the C11 position and conformationally restrained. The intrinsic chromophoric properties are elucidated by gas phase absorption studies. These studies reveal a small blue-shift in the S0-->S1 absorption for the 11-locked derivative as compared to the unlocked one. The gas phase absorption spectra of all the cationic mimics so far investigated show almost no absorption in the blue region. This observation stresses the importance of protein interactions for colour tuning, which allows the human eye to perceive blue light.

Computer Simulation↗
PubMed1988

Immune responsiveness to retinal S-antigen and opsin in serpiginous choroiditis and other retinal diseases.

The immune responsiveness to bovine retinal S-antigen and opsin has been investigated in some retinal disorders by means of in vitro lymphocyte proliferation, leukocyte migration inhibition and enzyme linked immune sorbent assays (ELISA). Sensitisation to S-antigen was observed in serpiginous choroiditis, but not in acute posterior multifocal placoid pigment epitheliopathy (APMPPE) or retinitis pigmentosa. No significant immune responsiveness was detected to opsin in any of the three diseases. Elevated antibody titers to S-antigen were observed in some individual patients and healthy subjects. However, none of the patient groups exhibited an elevated antibody titer as compared to the control group. Although serpiginous choroiditis and APMPPE share some prominent clinical characteristics, the sensitisation in the former disease may perhaps be attributed to more severe and prolonged damage of the photoreceptor cells and blood-retina barrier. A combination of previous and present results suggests that in immunological investigations of retinitis pigmentosa patients it is more effective to use human than bovine S-antigen as test antigen because a species specific epitope seems to be involved.

Antibody Formation↗
PubMed1989

Regeneration of bovine and octopus opsins in situ with natural and artificial retinals.

We consider the problem of color regulation in visual pigments for both bovine rhodopsin (lambda max = 500 nm) and octopus rhodopsin (lambda max = 475 nm). Both pigments have 11-cis-retinal (lambda max = 379 nm, in ethanol) as their chromophore. These rhodopsins were bleached in their native membranes, and the opsins were regenerated with natural and artificial chromophores. Both bovine and octopus opsins were regenerated with the 9-cis- and 11-cis-retinal isomers, but the octopus opsin was additionally regenerated with the 13-cis and all-trans isomers. Titration of the octopus opsin with 11-cis-retinal gave an extinction coefficient for octopus rhodopsin of 27,000 +/- 3000 M-1 cm-1 at 475 nm. The absorption maxima of bovine artificial pigments formed by regenerating opsin with the 11-cis dihydro series of chromophores support a color regulation model for bovine rhodopsin in which the chromophore-binding site of the protein has two negative charges: one directly hydrogen bonded to the Schiff base nitrogen and another near carbon-13. Formation of octopus artificial pigments with both all-trans and 11-cis dihydro chromophores leads to a similar model for octopus rhodopsin and metarhodopsin: there are two negative charges in the chromophore-binding site, one directly hydrogen bonded to the Schiff base nitrogen and a second near carbon-13. The interaction of this second charge with the chromophore in octopus rhodopsin is weaker than in bovine, while in metarhodopsin it is as strong as in bovine.

Animals↗
PubMed2005

Eyeshine and spectral tuning of long wavelength-sensitive rhodopsins: no evidence for red-sensitive photoreceptors among five Nymphalini butterfly species.

Spectral tuning of rhodopsins commonly refers to the effects of opsin amino acid substitutions on the wavelength for peak sensitivity of the rhodopsin absorption spectrum. Nymphalini butterflies provide an opportunity for identifying some of the amino acid substitutions responsible for insect rhodopsin spectral tuning because the majority of photoreceptor cells (R3-9) in the adult retina express only a single long wavelength-sensitive (LWS) opsin mRNA transcript. Therefore, the opsin genotype can be directly correlated with its phenotype. We determined the LWS opsin gene sequence from cDNA of the mourning cloak Nymphalis antiopa, and from genomic DNA of the malachite Siproeta stelenes and the peacock Inachis io. Using an epi-microspectrophotometer we examined each butterfly's eyeshine for photochemical evidence of multiple LWS rhodopsins and found only one. We then performed partial-bleaching experiments to obtain absorbance spectra for the LWS rhodopsins of all three species as well as from another nymphalid, the buckeye Junonia coenia. The isolated LWS opsin gene sequences varied in length from 1437-1612 bp and encode rhodopsins R522 (S. stelenes), R530 (I. io), R534 (N. antiopa) and, together with a previously published sequence, R510 (J. coenia). Comparative sequence analysis indicates that the S. stelenes rhodopsin is slightly blue-shifted compared to the typical 530 nm lepidopteran rhodopsin because of the presence of a S138A substitution at a homologous site that in mammalian MWS/LWS rhodopsins causes a 5 nm blue-shift. The difference in peak absorption between R522 of S. stelenes and R530 of Inachis io is therefore largely accounted for by this substitution. This suggests that spectral tuning mechanisms employing the S138A may have evolved in parallel in mammalian and butterfly MWS/LWS rhodopsins across 500 million years of evolution.

Amino Acid Sequence↗
PubMed1999

Extraretinal photoreceptors at the compound eye's posterior margin in Drosophila melanogaster.

Many invertebrates have supplementary extraocular photoreceptors that often are implicated in circadian rhythms. An extraretinal group of candidate photoreceptors in the fruit fly, Drosophila melanogaster, has been revealed previously at the posterior margin of the compound eye by using a photoreceptor-specific monoclonal antibody (Hofbauer and Buchner [1989] Naturwissen 76:335-336), but it never has been characterized. Here, we report the fine structure of this cell cluster reported by Hofbauer and Buchner, which is called "eyelet," as well as the further candidacy of their visual pigment and neurotransmitter. Eyelet forms a specialized, pigmented organ with cells that have numerous microvilli arranged into coherent rhabdomeres. The presence of rhabdomeric microvilli is a defining feature of a photoreceptor, reported here for the first time in eyelet. The rhabdomeres exhibit Rh6 opsin-like immunoreactivity, which provides evidence that the photoreceptors are functional: they fail to immunostain with antibodies against NINAE (Rh1), Rh4, or Rh5. The photoreceptors have been shown previously to exhibit histamine-like immunoreactivity, but they also stain with a monoclonal antiserum raised against Drosophila choline acetyltransferase (ChAT), suggesting that the photoreceptors not only may contain histamine but also can synthesize acetylcholine. A ChAT-immunoreactive axon bundle originating from eyelet terminates in the cortex of the anterior medulla. This bundle also is seen with reduced silver stains. Electron microscopic examination revealed four axon profiles of similar size in this bundle, indicating that eyelet contains at least four photoreceptors. The pathway of eyelet's axon bundle coincides with the precocious pathway of Bolwig's nerve that arises from the larval organ of sight. The origin and possible function of eyelet are discussed.

Animals↗
PubMed1996

Primate photopigments and primate color vision.

The past 15 years have brought much progress in our understanding of several basic features of primate color vision. There has been particular success in cataloging the spectral properties of the cone photopigments found in retinas of a number of primate species and in elucidating the relationship between cone opsin genes and their photopigment products. Direct studies of color vision show that there are several modal patterns of color vision among groupings of primates: (i) Old World monkeys, apes, and humans all enjoy trichromatic color vision, although the former two groups do not seem prone to the polymorphic variations in color vision that are characteristic of people; (ii) most species of New World monkeys are highly polymorphic, with individual animals having any of several types of dichromatic or trichromatic color vision; (iii) less is known about color vision in prosimians, but evidence suggests that at least some diurnal species have dichromatic color vision; and (iv) some nocturnal primates may lack color vision completely. In many cases the photopigments and photopigment gene arrangements underlying these patterns have been revealed and, as a result, hints are emerging about the evolution of color vision among the primates.

Animals↗
PubMed2005

A non-canonical photopigment, melanopsin, is expressed in the differentiating ganglion, horizontal, and bipolar cells of the chicken retina.

Vertebrate melanopsin is a photopigment in the eye, required for photoentrainment. Melanopsin is more closely related to opsin proteins found in invertebrates, than to the other photo-pigments. Although the invertebrate melanopsin-like protein is localized in rhabdomeric photoreceptors in the invertebrate eye, it has been shown to be expressed in a subset of retinal ganglion cells in the mouse and in horizontal cells in the frog, indicating its diversified expression pattern in vertebrates. Here we show that two types of melanopsin transcripts are expressed in the developing chicken retina. Melanopsin is firstly expressed by a small subset of ganglion cells, and then prominently expressed by horizontal cells and later by bipolar cells in the developing chicken retina. This suggests that a subset of ganglion, horizontal, and bipolar cells in the chicken retina may have rhabdomeric properties in their origins.

Amino Acid Sequence↗
PubMed1981

Effects of detergent micelles on the recombination reaction of opsin and 11-cis-retinal.

When detergent-solubilized proteins interact with hydrophobic or amphiphilic molecules in the presence of detergent micelles, the solubility of the latter species in the micelles must be included in both thermodynamic and kinetic treatments. In this paper, we derive equations which describe the distribution of species present at equilibrium for a system in which a detergent-solubilized protein binds a hydrophobic (or amphiphilic) ligand. We have applied the formalism developed in this paper to the reaction describing the formation of rhodopsin from its apoprotein and 11-cis-retinal. Qualitatively, the results demonstrate that a significant portion of the observed decrease in the extent of recombination for rhodopsin solubilized in either sodium cholate or Tween 80 may be attributed to the partition of retinal into detergent micelles and that a detergent-induced protein denaturation need not be invoked to explain the data. We also discuss results for rhodopsin solubilized in a nonionic detergent (octaethylene glycol n-dodecyl ether) in which the detergent is clearly causing irreversible loss of the capability to recombine with 11-cis-retinal.

Detergents↗
PubMed1990

Autoimmune responsiveness to retinal IRBP, S-antigen and opsin in proliferative vitreoretinopathy.

Proliferative vitreoretinopathy (PVR) was induced in rabbits by intravitreal injection of homologous fibroblasts. During the 8 weeks after injection the immune responsiveness to three purified retinal autoantigens was studied. From 2 weeks after injection, animals that developed serious forms of PVR exhibited definite mitotic responses of their lymphocytes to stimulation by the retinal antigens. These responses could consistently be demonstrated for S-antigen and interphotoreceptor retinoid-binding protein (IRBP) during the subsequent period of examination. Marked responses were also noted to opsin, however, their occurrence was more variable. In mild forms of PVR or in controls the responses were weak or absent. This showed that the elevated cellular reactivities were induced by the development of PVR and not by some other experimental factor. Humoral immune responses to the three antigens were absent (as assayed by ELISA). The control groups did not exhibit any elevated immune responsiveness. There appears to be accumulating evidence that inflammation may play a role in the development of PVR. The present results indicate that cellular autoimmune responses to photoreceptor antigens are a secondary phenomenon in PVR, nevertheless, they may be an important factor in the subsequent development of severe PVR. This autosensitization may consequently be taken into consideration in the treatment of complicated human PVR.

Animals↗
PubMed1988

Identification of proteins in retinas and IPM from eyes with retinitis pigmentosa.

Opsin, the alpha-subunit of transducin, S-antigen, interphotoreceptor retinoid-binding protein (IRBP) and cathepsin D were assessed in autopsy eyes from patients with retinitis pigmentosa (RP) and normal autopsy eyes. Immunochemical methods were used to determine the presence of these proteins on Western blots of retinal homogenates from five RP donors and on blots of interphotoreceptor matrix (IPM) preparations from six other RP eyes. The amounts of immunoreactive opsin, S-antigen, alpha-transducin, and IRBP appeared below normal in retinas from RP eyes. All six IPM samples from patients with advanced RP had reduced amounts of S-antigen and no detectable IRBP or transducin. Cathepsin D (an RPE protein) was present in IPM or RP eyes in amounts comparable to that in IPMs from normal eyes. Small amounts of cathepsin D were also detected in retinas from both normal and RP eyes. These studies show that proteins specific to the photoreceptor-pigment epithelium complex in normal eyes can be detected in autopsy eyes from patients with RP and suggest that the observed reductions in photoreceptor-specific proteins occur as a consequence of photoreceptor loss.

Adult↗
PubMed1993

Photoreceptor-specific protein expression of mouse retina in organ culture and retardation of rd degeneration in vitro by a combination of basic fibroblast and nerve growth factors.

Previously we have presented the morphological features of a neonatal mouse retinal explant kept in culture for 3 to 4 weeks. To further evaluate the organotypic parameters of the tissue we have examined the presence of opsin, S-antigen, and interphotoreceptor retinoid-binding protein (IRBP) in the same experimental paradigm, using light microscopic immunocytochemistry. In vitro, opsin and S-antigen staining is found in photoreceptor somata from genetically normal explants and those derived from mice with the rd or the rds mutation. When present, inner and outer segments label more intensely. No IRBP staining has been found in cell bodies of any genotype. However, some labeling is found in the plexiform layers and in the inner segments. The results indicate that photoreceptor proteins are continuously produced in vitro. This further establishes the organotypic nature of the retinal explant in culture. The administration of growth factors to these explants has been investigated. Neither basic fibroblast growth factor nor nerve growth factor alone has affected the explants phenotype. However, the combination of these proteins has significantly retarded rd cell loss in vitro.

Animals↗