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PubMed2000

Pigment epithelium-derived factor supports normal development of photoreceptor neurons and opsin expression after retinal pigment epithelium removal.

Dysfunction of the retinal pigment epithelium (RPE), its loss, or separation from the underlying neural retina results in severe photoreceptor degeneration. Pigment epithelium-derived factor (PEDF) is a glycoprotein with reported neuroprotective and differentiation properties that is secreted in abundance by RPE cells. The "pooling" of PEDF within the interphotoreceptor matrix places this molecule in a prime physical location to affect the underlying neural retina. The purpose of this study was to analyze the morphogenetic activity of PEDF in a model of photoreceptor dysmorphogenesis induced by removal of the RPE. Eyes were dissected from embryonic Xenopus laevis, and the RPE was removed before culturing in medium containing PEDF, PEDF plus anti-PEDF antibodies, or medium alone. Control retinas were maintained with an adherent RPE. Light and electron microscopic analysis was used to examine retinal ultrastructure. Opsin was localized immunocytochemically and quantified as an index of outer segment membranous material and photoreceptor protein expression. Removal of the RPE resulted in an aberrant assembly of photoreceptor outer segments, loss of fine subcellular ultrastructure in photoreceptors, and a reduction in opsin protein levels when compared with control retinas. The addition of PEDF prevented the dysmorphic photoreceptor changes induced by RPE removal. In particular, photoreceptor ultrastructure, outer segment membrane assembly, and steady-state levels of opsin were equivalent to control conditions. Anti-PEDF antibodies completely blocked the morphogenetic activity of PEDF. These results indicate that PEDF is able to mimic the supportive role of the RPE on photoreceptors during the final stages of retinal morphogenesis.

Animals↗
PubMed1991

Immunoelectron microscopic study of the opsin distribution in the photoreceptor cells of Drosophila melanogaster.

Distribution of opsin in the compound eye of Drosophila melanogaster was examined by post-embedding immunoelectron microscopy using a monoclonal antibody against the Drosophila Rh1 opsin and gold-conjugated secondary antibody. Numerous gold particles were observed on the rhabdomeric microvilli of R1-R6 retinular cells. In the retinular cell body, gold particles were distributed in rough endoplasmic reticulum, subrhabdomeric cisternae (SRC), multivesicular bodies, and secondary lysosomes. In the rdgA mutant, whose SRC are absent, density of gold particles on the rhabdomeric microvilli was about 20% of normal. These results suggest the involvement of SRC in opsin transport.

Animals↗
PubMed1990

A comparison of the ultrastructure and opsin immunocytochemistry of the pineal organ and retina of the deep-sea fish Chimaera monstrosa.

The pineal organ and retina of the rat-fish Chimaera monstrosa were compared by electron microscopy and immunocytochemistry using antisera against colour-specific opsins and paying special attention to pineal CSF-contacting neurons and retinal Landolt's clubs. In the retina, a large number of Landolt's clubs and two types of rod-like photoreceptors were found. The outer segments of the numerous electron-dense "tall rods" displayed strong immunoreactivity with the monoclonal OS-2 antibodies--first of all detecting green- and blue-sensitive pigments. These results point out the presence of a chrysopsin-like photopigment. A weak cross-reactivity with the COS-1 and rhodopsin antisera indicates that the photopigment in question has certain amino acid sequence homologies with red and green photopigments. The outer segments of the few electron-lucent "broad rods" reacted with the OS-2 antiserum intensely but weakly with the COS-1 antiserum, a result suggesting the presence of a (blue?) photopigment differing from that of the tall rods. Since in the pineal organ the outer segments of the photoreceptor cells were opsin-immunonegative with all four antisera used, it is suggested that they contain an essentially different (UV-blue?) pigment. The pineal CSF-contacting neurons and retinal Landolt's bipolars were found to be principally similar in cytology. Their ciliated (receptor) dendrite terminals protruding into the photoreceptor space lacked photoreceptor membranes and were opsin-immunonegative. They are supposed to perceive information (on ionic properties?) from the fluid of the pineal lumen and retinal photoreceptor space. On the other hand, by their synaptic connections the CSF-contacting neurons and Landolt's bipolars are considered to be secondary neurons of the light-perceiving pathway of both organs.

Animals↗
PubMed1986

Light and electron microscopy of S-antigen- and opsin-immunoreactive photoreceptors in the retina of turtle, chicken, and hedgehog.

S-antigen and opsin-immunoreactive sites were studied in the retina of turtle (Pseudemys scripta elegans), chicken (Gallus domesticus), and hedgehog, (Erinaceus roumanicus) by light-microscopic avidin-biotin-peroxidase and electron-microscopic protein A-gold and immunoglobulin-gold (immunogold) techniques. In general, S-antigen and opsin immunoreactions were exclusively localized to certain photoreceptors of the retinae studied. In turtle and chicken, strong S-antigen immunoreactivity was found in the outer and inner segments, perikarya and synaptic bases of rod photoreceptors. Some--apparently green--single cones also exhibited immunoreactive outer and inner segments. In hedgehog, the inner segments, perikarya and pedicles of rods displayed immunoreaction of varying intensities. In all three species there was an accumulation of immunogold particles on the distal portion of the inner segment, the connecting piece and the proximal portion of the outer segment. Opsin immunoreactivity was found in the outer segments of rod photoreceptors, and in those of--apparently green--single cones of turtle and chicken. The localization and significance of the S-antigen immunoreaction is discussed in connection with the occurrence of different photopigments in the retinae studied. The correlation of the presence of S-antigen and of either rhodopsin or porphyropsin in rod and--apparently green--single cone photoreceptors was emphasized.

Animals↗
PubMed1986

Immunocytochemical localization of opsin in the inner segment and ciliary plasma membrane of photoreceptors in retinas of rds mutant mice.

Homozygous 020/A mutant mice bearing the rds gene for slow inherited retinal degeneration have been observed to develop normal photoreceptor inner segments connecting cilia and synaptic contacts but fail to form outer segments. Their retinas are responsive to light, however. In order to assess the sources of these physiological responses we investigated the distribution of opsin in photoreceptors by means of immunoelectron microscopy. Opsin was detected in the inner segment plasma membrane and the distal ciliary plasma membrane. Antibody also bound to lamellar and vesicular membranes in the interphotoreceptor space and, in a small fraction of the photoreceptors, to membranes projecting from the distal cilium. These membranes may represent abortive formation of rod discs in this form of retinal degeneration. Failure to form an organized outer segment may contribute to the persistence of opsin in the inner segment plasma membranes of adult mutant mice.

Animals↗
PubMed1979

Renewal of opsin in the photoreceptor cells of the mosquito.

Mosquito rhodopsin is a digitonin-soluble membrane protein of molecular weight 39,000 daltons, as determined by sodium dodecyl sulfate gel electrophoresis. The rhodopsin undergoes a spectral transition from R515-520 to M480 after orange illumination. The visual pigment apoprotein, opsin, is the major membrane protein in the eye. Protein synthesis in the photoreceptor cells occurs in the perinuclear cytoplasm and the newly made protein is transported to the rhabdom. Light adaptation increases the rate of turnover of this rhabdomal protein. The turnover of electrophoretically isolated opsin is also stimulated by light adaptation. The changes observed in protein metabolism biochemically, are consistent with previous morphological observations of photoreceptor membrane turnover. The results agree with the hypothesis that the newly synthesized rhabdomal protein is opsin.

Adaptation, Physiological↗
PubMed1990

The structure of bacteriorhodopsin and its relevance to the visual opsins and other seven-helix G-protein coupled receptors.

Bacteriorhodopsin is a light-driven hydrogen-ion pump whose structure is known to about 6.0 A in three dimensions and 2.8 A in projection. It consists of seven transmembrane helices surrounding the chromophore, retinal. Halorhodopsin is a second member of the same family of membrane proteins, both of them from the cell membrane of halobacteria. Halorhodopsin is a light-driven chloride-ion pump but has very close homology to bacteriorhodopsin, especially around the retinal. In contrast, the visual opsins that are responsible for the primary step in visual transduction in all eukaryotes from Drosophila upwards, form a separate family with no direct sequence homology to the bacteriorhodopsin family. The visual opsin family now includes about 15 other receptor proteins, all of which active G-protein cascades, including the beta-adrenergic receptor as well as several others. Despite the lack of clear relations at the level of amino acid sequence, there are topographical similarities between the bacteriorhodopsin and the visual opsin families in the nature and site of chromophore attachment, the number of transmembrane helices and the positions of the amino and carboxyl termini in the membrane. These suggest that if the two were at one time closely related, they have diverged too far to have sequences that are detectably similar.

Amino Acid Sequence↗
PubMed2025

Opsins are Phospholipid Scramblases in All Domains of Life.

Opsins are highly abundant retinal proteins in the membranes of photoheterotrophic bacteria. However, some microbial genomes encode an opsin but lack the gene for the final enzyme in retinal synthesis. To account for this paradox, we hypothesized that bacterial opsins play a role in membrane structure and/or biogenesis independent from their potential for light-driven signaling or proton pumping. After purifying actinorhodopsin from a cell-free expression system and from E. coli membranes upon overexpression, we demonstrated both in vitro and in silico that actinorhodopsin from Nanopelagicus ca. is a phospholipid scramblase, serving in its pentameric state as a retinal-independent phospholipid diffusion channel. Phospholipid headgroups move along a transbilayer path between actinorhodopsin protomers, to equilibrate lipid content in the inner and outer leaflets. Two profound activities, membrane biosynthesis and capture of light energy, are thus facilitated by one ancient bacterial polypeptide. Light-dependent activity and light-independent phospholipid scrambling are shared functions of eukaryotic, archaeal, and bacterial rhodopsins.

ActR↗
PubMed1988

Characterization of a second gene involved in bacterio-opsin gene expression in a halophilic archaebacterium.

Southern blot analysis and nucleotide sequencing of DNA from three bacterio-opsin-deficient mutants of the archaebacterium Halobacterium halobium (M86, W105, and W109) revealed that they each contain an alteration in a region 2,000 to 3,800 base pairs (bp) upstream of the bacterio-opsin gene (bop). Nucleotide sequence analysis of this region, which is also located downstream of the previously characterized brp gene, revealed that it contains an open reading frame (ORF) of 2,022 bp. This 2,022-bp ORF has a start codon which overlaps the stop codon of the brp gene and is read in the same direction. The ORF could encode an acidic protein of 73,334 daltons (674 amino acids) with a predicted secondary structure typical of a soluble protein. Bop mutant M86 contains a 1,883-bp deletion extending from bp 351 of the ORF, to 197 bp beyond the stop codon. Mutant W105 has an ISH2 element integrated at bp 1239 of the ORF, and mutant W109 has an ISH26 element integrated at bp 1889. Our results suggest that the ORF is a gene (designated bat for bacterio-opsin activator gene) involved in bop gene expression.

Amino Acid Sequence↗
PubMed1989

Regulation of the bacterio-opsin gene of a halophilic archaebacterium.

The protein bacterio-opsin, complexed with retinal, functions as a light-driven proton pump in the purple membrane of the halophilic archaebacterium, Halobacterium halobium. Bacterio-opsin deficient mutants have been characterized in attempts to elucidate regulation of the gene encoding bacterio-opsin (bop). Analysis of the mutational defect in Bop mutants has revealed the existence of at least two genes that affect bop gene expression and (or) purple membrane formation: (i) the brp gene, located 526 base pairs upstream of the bop gene, is transcribed in the opposite orientation, and (ii) the bat gene, located 1602 base pairs upstream of the bop gene, is transcribed in the same orientation as the brp gene. The bat gene start codon overlaps the stop codon of the brp gene. The bat gene could encode an acidic protein of 73,000 Da (674 amino acids) with a predicted secondary structure typical of a soluble alpha--beta type protein. This type of secondary structure is in contrast to the hydrophobic structure predicted for the putative brp protein. Transcriptional analyses of the wild type, 11 Bop mutants, and a Bop revertant suggest that the bat gene has a more direct role than the brp gene in bop gene expression and is involved in activating bop and brp gene expression.

Archaea↗
PubMed1991

Maintenance of opsin density in photoreceptor outer segments of retinoid-deprived rats.

Dietary deficiency in the retinoid precursors of the visual pigment chromophore 11-cis-retinal eventually results in selective degeneration of the photoreceptor cells of the vertebrate retina. Early effects of retinoid deficiency are depletion of rhodopsin from the retina and vesiculation of the photoreceptor outer segment disc membranes. Experiments were conducted to determine whether these early changes were accompanied by an alteration of the opsin content of the disc membranes. After being fed a retinoid-deficient diet containing retinoic acid for 26 weeks, the rhodopsin content of rat retinas was reduced by over 85%. Both the diameters and the lengths of the outer segments decreased significantly. However, immunocytochemical and freeze-fracture analyses indicated that retinoid deficiency did not lower opsin density in the outer-segment disc membranes. These findings indicate that in the rat, opsin synthesis and disc assembly are coordinated processes that remain coupled despite reduced availability of the vitamin A chromophore. The fact that disc size decreases and disc synthesis eventually ceases in retinoid-deprived rats indicates that specific retinoids are essential for disc morphogenesis. The mechanism by which these retinoids regulate disc assembly remains to be determined.

Analysis of Variance↗
PubMed1998

The cloning of GRK7, a candidate cone opsin kinase, from cone- and rod-dominant mammalian retinas.

PURPOSE: Desensitization in the rod cell of the mammalian retina is initiated when light-activated rhodopsin is phosphorylated by the G protein-coupled receptor kinase (GRK), GRK1, often referred to as rhodopsin kinase. A distinct kinase that specifically phosphorylates cone opsins in a similar manner has not been identified in mammals. To determine the existence of a cone opsin kinase, RNA from the retinas of cone- and rod-dominant mammals was analyzed by PCR. METHODS: RNA prepared from the retinas of two cone-dominant mammals, the thirteen-lined ground squirrel and the eastern chipmunk, and a rod-dominant mammal, the pig, was used to clone a new GRK family member by RT-PCR. The tissue distribution and localization of the kinase in retina were determined by Northern blot hybridization and in situ hybridization. The protein encoded by this cDNA was expressed in human embryonic kidney-293 (HEK-293) cells and compared with bovine GRK1 for its ability to phosphorylate bovine rhodopsin and to undergo autophosphorylation. RESULTS: The cDNA cloned from ground squirrel contains an open reading frame encoding a 548 amino-acid protein. Sequence analysis indicates that this protein is orthologous to GRK7 recently cloned from O. latipes, the medaka fish. Partial cDNA fragments of GRK7 were also cloned from RNA prepared from eastern chipmunk and pig retinas. In situ hybridization demonstrated widespread labeling in the photoreceptor layer of the ground squirrel retina, consistent with expression in cones. Recombinant ground squirrel GRK7 phosphorylates bovine rhodopsin in a light-dependent manner and can be autophosphorylated, similar to bovine GRK1. CONCLUSIONS: These results indicate that cone- and rod-dominant mammals both express GRK7. The presence of this kinase in cones in the ground squirrel and its ability to phosphorylate rhodopsin suggests that it could function in cone cells as a cone opsin kinase.

Amino Acid Sequence↗
PubMed1956

Acid-base properties of rhodopsin and opsin.

Purified preparations of cattle rhodopsin have been titrated to various pH, irradiated, and the pH changes followed thereafter until completed. In this way we have obtained the titration curves of rhodopsin, of the immediate product of irradiation, measured within 30 seconds; and of the final product of irradiation (opsin). The rhodopsin preparations display about 54 titratable groups per mole of pigment: about 34 base-binding and 20 acid-binding groups. In default of an absolute purification, one cannot be sure that all of these go with rhodopsin itself. Exposure to light induces an immediate rise of pH between pH 2 and 8, maximal at about pH 5. This-followed by its slow partial or complete reversal-is the only change of pH in the physiological range (6-7). It involves the exposure of 1 new acid-binding group per mole of rhodopsin with pK about 6.6, close therefore to that of the imidazole group of histidine. At acid and alkaline pH this immediate change is followed by slower changes, occupying up to 40 minutes at 20 degrees C. These changes are always in the direction of neutrality. They involve increases of 5 to 6 moles acid bound at acid pH, and 7 moles base bound at alkaline pH. They are associated with the irreversible denaturation of opsin in acid and alkaline solution, as evidenced by loss of its capacity to regenerate rhodopsin. Such frank denaturation procedures as the exposure of rhodopsin to alkali or heat in the dark result in comparable acid-base changes.

Acid-Base Equilibrium↗
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↗
PubMed1985

Opsin-like immunoreaction in the retinae and pineal organs of four mammalian species.

Opsin-like immunoreactivity was observed in the retinae and pineal organs of the mouse, rat and guinea pig, and the pineal organ of the cat. In the retina the immunoreaction was restricted to photoreceptor cells, which displayed immunostaining in their perikarya and outer and inner segments. Distinct pinealocytes endowed with characteristic processes were labelled in the pineal organs of the mouse and cat. However, in the cat the number of immunoreactive pinealocytes was very limited. In the pineal organs of the rat and guinea pig immunoreaction was very weak and diffuse. No immunoreaction was observed when the antibody was preabsorbed with purified bovine (rhod)opsin. These findings are in accord with the results of previous studies indicating molecular similarities between retinal photoreceptors and pinealocytes in mammals.

Animals↗
PubMed2004

A gene of the opsin family in the carotenoid gene cluster of Fusarium fujikuroi.

Opsins are membrane photoreceptors closely related to the heat-shock proteins of the HSP30 family. Their functions include light-driven ion pumping in archaea and light detection in algae and animals, using the apocarotenoid retinal as a light-absorbing prosthetic group. We describe a gene of Fusarium fujikuroi, carO, coding for a polypeptide resembling opsins and HSP30-like proteins and contiguous to the genes of the carotenoid pathway, carRA and carB. Transcription of carO is induced by light and is deregulated in carotenoid-overproducing mutants. The same regulation pattern is exhibited by carRA and carB; and common conserved DNA elements are found in the three promoters. Heat shock resulted in a modest induction of carO transcription, similar to the one exhibited by carB, confirming a common regulation. Targeted mutagenesis of carO produced no apparent phenotypic modification, including no change in the photoinduction of carotenoid biosynthesis.

Amino Acid Sequence↗
PubMed1986

In vivo incorporation of [2-3H]-myo-inositol into frog opsin.

The in vivo incorporation of [2-3H]-myo-inositol into frog retinal rod outer segment membranes was examined. About 25% of the recovered radioactivity was found to be protein-associated. Following acid hydrolysis of this material and extraction with hexane, all the radioactivity remained in the aqueous phase, indicating that the label was not in fatty acids. Following ion exchange column chromatography of the hydrolysate, the major radioactive compound comigrated on TLC with an internal standard of [U-14C]-myo-inositol. SDS polyacrylamide gel electrophoresis of unextracted membranes indicated that the majority of the label was associated with opsin. These results indicate that [2-3H]-myo-inositol was incorporated in vivo into opsin, presumably with retention of its chemical identity.

Animals↗
PubMed1989

Affinity labeling of bovine opsin by trans-retinoyl chloromethane.

All-trans-retinoyl chloromethane is a potent irreversible inactivator of bovine opsin in retinal rod outer segments. The inactivation appears to be due to specific modification of the apoprotein at the 11-cis-retinaldehyde binding site. The reaction follows pseudo first order kinetics at 37 degrees C. A moderate dissociation constant for the initial reversible complex of 6.1 mM could be derived with a first order rate constant of 1.8x10(-1) min-1 for the conversion to the irreversible inactivated form. Native rhodopsin or rhodopsin regenerated from opsin by addition of 11-cis-retinaldehyde is completely protected against inactivation by trans-retinoyl chloromethane. All-trans-retinaldehyde does not provide this protection for the irreversible inactivation.

Affinity Labels↗