Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “Rod Opsins”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 433 records · Page 24Linked to original sources
PubMed2004

Opsin expression: new mechanism for modulating colour vision.

Each cone photoreceptor in the retina responds to light in a limited range of wavelengths, giving it a spectral phenotype. This phenotype is determined by the most prevalent of the photoreceptor's visual-pigment proteins (opsins) and is assumed to remain unchanged during an animal's lifetime. Here we show that in the Pacific pink salmon, Oncorhynchus gorbuscha, single cones can switch their spectral phenotype from ultraviolet to blue by regulating the production of the appropriate opsins as the fish grow older. This photoreceptor plasticity may operate to modulate colour vision as the salmon's lifestyle changes.

Animals↗
PubMed2001

Expression of opsin molecule in cultured murine melanocyte.

Recently, we demonstrated the expression of rhodopsin in the tail fin of the Xenopus tadpole, in which photosensitive melanophores exist (Miyashita et al, The photoreceptor molecules in Xenopus tadpole tail fin, in which melanophores exist. Zool Sci 18:671-674, 2001). The presence of opsin molecules in pigment cells of lower vertebrates raises the possibility that pigment cells in animal skin function as photosensors generally. To explore this possibility in higher vertebrates, we tried to detect photoreception molecules in mammalian melanocytes. We extracted total RNA from Melan a2, a cell line of immortal murine melanocyte, which is derived from C57BL mice. The DNA sequence obtained by reverse transcriptase-polymerase chain reaction (RT-PCR) amplification was homologous to the corresponding portion of the sequence of ocular rhodopsin of mice. Western blotting and fluorescent immunocytochemistry showed the existence of the opsin protein in the melanocytes. Another cell line, EL4, which is derived from lymphoma of C57BL/6N, scarcely expresses opsin mRNA, as judged by RT-PCR. Thus expression of the opsin gene is not ubiquitous among immortal cell lines. Detection of rhodopsin mRNA in murine tissues of C57BL/6N by RT-PCR showed its presence in the eye and skin but not in the liver. The role of the opsin molecule in melanocyte is not known at present, but this will provide additional insight into photoreception systems in animal skin.

Animals↗
PubMed1997

Modulation of opsin apoprotein activity by retinal. Dark activity of rhodopsin formed at low temperature.

The bovine opsin apoprotein activates transducin, although at a much reduced level than light-activated rhodopsin (Surya, A., Foster, K., and Knox, B. (1995) J. Biol. Chem. 270, 5024-5031). The ability of retinal to modulate opsin apoprotein activity was investigated using a guanyl nucleotide exchange assay on transducin. 11-cis-Retinal reacted with opsin at 22 degrees C to (a) reform pigment having maximal absorbance at 500 nm and (b) reduce opsin activity by >80%. Pigment formation also occurred at 0 degrees C with a t1/2 of 260 min. However, unlike rhodopsin formed at 22 degrees C (R22), the rhodopsin formed at 0 degrees C (R0) activated transducin with the same half-saturating concentration as opsin in an exhaustive binding assay. Thus, the formation of a protonated Schiff base associated with 500 nm absorbance does not by itself lead to the inactivation of opsin. The R0 conformation was partially inactivated by incubation at 22 degrees C (t1/2 = 61 +/- 9 min), suggesting that it may be an intermediate conformation in the regeneration of rhodopsin.

Animals↗
PubMed1997

Three opsin-encoding cDNAS from the compound eye of Manduca sexta.

Three distinct opsin-encoding cDNAs, designated MANOP1, MANOP2 and MANOP3, were isolated from the retina of the sphingid moth Manduca sexta. MANOP1 codes for a protein with 377 amino acid residues. It is similar in sequence to members of a phylogenetic group of long-wavelength-sensitive arthropod photopigments, most closely resembling the opsins of ants, a praying mantis, a locust and the honeybee. MANOP2 and MANOP3 opsins have 377 and 384 residues respectively. They belong to a related group of insect visual pigments that include the ultraviolet-sensitive rhodopsins of flies as well as other insect rhodopsins that are also thought to absorb at short wavelengths. The retina of Manduca sexta contains three rhodopsins, P520, P450 and P357, with absorbance peaks, respectively, at green, blue and ultraviolet wavelengths. There is evidence that MANOP1 encodes the opsin of P520. We suggest that MANOP2 encodes P357 and that MANOP3, representing a class of blue-sensitive insect photopigments, encodes P450.

Amino Acid Sequence↗
PubMed1985

The Drosophila ninaE gene encodes an opsin.

The Drosophila ninaE gene was isolated by a multistep protocol on the basis of its homology to bovine opsin cDNA. The gene encodes the major visual pigment protein (opsin) contained in Drosophila photoreceptor cells R1-R6. The coding sequence is interrupted by four short introns. The positions of three introns are conserved with respect to positions in mammalian opsin genes. The nucleotide sequence has intermittent regions of homology to bovine opsin coding sequences. The deduced amino acid sequence reveals significant homology to vertebrate opsins; there is strong conservation of the retinal binding site and two other regions. The predicted protein secondary structure strikingly resembles that of mammalian opsins. We conclude the Drosophila and vertebrate opsin genes are derived from a common ancestor.

Amino Acid Sequence↗
PubMed1988

Phenotypic expression of photoreceptor and endocrine cell properties by cultured pineal cells of the newborn rat.

Pineal glands of newborn rats were dissociated and maintained under cell culture conditions. The phenotypic expression of both photoreceptor and endocrine cell properties was investigated using immunohistochemical techniques (specific antibodies against opsin or serotonin). After one week in culture, a number of small round cells appeared on top of a sheet of flat epithelium. Among those cells, opsin-like immunoreactive cells were observed. These cells showed a neuron-like morphology with neuritic processes and often formed rosettes. Immunoreactivity was found on the plasma membrane of both the soma and cell processes. Serotonin-like immunoreactive cells were also differentiated in culture with two different morphological types of cells being found. One type resembled cultured serotonin-containing amacrine cells of the retina, and the other type had a flat, polygonal shape similar to that of pinealocytes. Both types of immunoreactive cells possessed fine neuritic processes. These results indicated that cell culture of rat pineal gland cells allowed expression of some properties, such as opsin synthesis and neuron-like morphology with long neuritic processes, that were not expressed in the intact rat pineal gland.

Animals↗
PubMed2007

Opsin gene duplication and diversification in the guppy, a model for sexual selection.

Identification of genes that control variation in adaptive characters is a prerequisite for understanding the processes that drive sexual and natural selection. Male coloration and female colour perception play important roles in mate choice in the guppy (Poecilia reticulata), a model organism for studies of natural and sexual selection. We examined a potential source for the known variation in colour perception, by analysing genomic and complementary DNA sequences of genes that code for visual pigment proteins. We find high sequence variability, both within and between populations, and expanded copy number for long-wave sensitive (LWS) opsin genes. Alleles with non-synonymous changes that suggest dissimilar spectral tuning properties occur in the same population and even in the same individual, and the high frequency of non-synonymous substitutions argues for diversifying selection acting on these proteins. Therefore, variability in tuning amino acids is partitioned within individuals and populations of the guppy, in contrast to variability for LWS at higher taxonomic levels in cichlids, a second model system for differentiation owing to sexual selection. Since opsin variability parallels the extreme male colour polymorphism within guppy populations, we suggest that mate choice has been a major factor driving the coevolution of opsins and male ornaments in this species.

Alleles↗
PubMed2005

Retinoid X receptor (gamma) is necessary to establish the S-opsin gradient in cone photoreceptors of the developing mouse retina.

PURPOSE: The retinoid X receptors (RXRs) are members of the family of ligand-dependent nuclear hormone receptors. One of these genes, RXRgamma, is expressed in highly restricted regions of the developing central nervous system (CNS), including the retina. Although previous studies have localized RXRgamma to developing cone photoreceptors in several species, its function in these cells is unknown. A prior study showed that thyroid hormone receptor beta2 (TRbeta2) is necessary to establish proper cone patterning in mice by activating medium-wavelength (M) cone opsin and suppressing short-wavelength (S) cone opsin. Thyroid hormone receptors often regulate gene transcription as heterodimeric complexes with RXRs. METHODS: To determine whether RXRgamma cooperates with TRbeta2 to regulate cone opsin patterning, the developmental expression of RXRgamma was examined, and cone opsin expression in RXRgamma-null mice was analyzed. RESULTS: RXRgamma was expressed in postmitotic cones and was transiently downregulated at the time of S-opsin onset in both mouse and human cones. RXRgamma-null mice expressed S-opsin in all cones, similar to the TRbeta2-null mice. Unlike TRbeta2-null mice, which did not express M-opsin, RXRgamma-null mice had a normal pattern of M-opsin expression. CONCLUSIONS: RXRgamma is essential (along with TRbeta2) for suppressing S-opsin in all immature cones and in dorsal cones in the mature retina, but it is not necessary for M-opsin regulation. These results demonstrate a critical role for RXRs in regulating cell differentiation in the CNS and highlight a remarkable conservation of opsin regulation from Drosophila to mammals.

Animals↗
PubMed1994

Visual pigments in the pineal complex of the Japanese quail, Japanese grass lizard and bullfrog: immunocytochemistry and HPLC analysis.

We investigated localization of visual pigments in the pineal complex of Japanese quail, Japanese grass lizards and bullfrogs immunocytochemically by use of the antiserum against bovine rhodopsin (Rh-As) and monoclonal antibodies against chicken iodopsin (Io-mAb). We also analyzed retinoids, chromophores of visual pigments, by a high performance liquid chromatography (HPLC). The outer segments and cell membranes of some photoreceptor cells in the pineal organ of the Japanese quail exhibited immunoreactivity to Rh-As, but there are also many immunonegative cells. The number of immunoreactive cells among individuals varied. Immunoreactivity to Io-mAb was weak or did not exist. The HPLC analysis revealed peaks of 11-cis and all-trans isomers of retinal in the oxime extracts of the pineal organ of Japanese quail and chickens. In the pineal of Japanese grass lizards, the outer segments of some cells were immunopositive to Io-mAb, but there were no cells immunoreactive to Rh-As. The parietal eye exhibited a well-developed lens and photoreceptor cells, but the outer segments of photoreceptor cells were immunonegative to both Rh-As and Io-mAb. In bullfrogs, three types of cells were identified in both the pineal and frontal organ; (1) immunopositive to Rh-As, (2) immunopositive to Io-mAb and (3) immunonegative to either of the antibodies. In the pineal organ of bullfrogs, 11-cis and all-trans retinal and 11-cis 3-dehydroretinal were detected, and 11-cis and all-trans retinal were also detected in the frontal organ. We detected 11-cis and all-trans retinal in the ventral part of diencephalon including the hypothalamus. Thus, the chromophore is the same between the retinal and pineal visual pigments, but the expression of opsins is different between the retina and pineal complex, which probably reflects the different function of each organ.

Animals↗
PubMed2005

Pteropsin: a vertebrate-like non-visual opsin expressed in the honey bee brain.

Insects have excellent color vision based on the expression of different opsins in specific sets of photoreceptive cells. Opsins are members of the rhodopsin superfamily of G-protein coupled receptors, and are transmembrane proteins found coupled to light-sensitive chromophores in animal photoreceptors. Diversification of opsins during animal evolution provided the basis for the development of wavelength-specific behavior and color vision, but with the exception of the recently discovered non-visual melanopsins, vertebrate and invertebrate opsins have generally been viewed as representing distinct lineages. We report a novel lineage of insect opsins, designated pteropsins. On the basis of sequence analysis and intron location, pteropsins are more closely related to vertebrate visual opsins than to invertebrate opsins. Of note is that the pteropsins are missing entirely from the genome of drosophilid flies. In situ hybridization studies of the honey bee, Apis mellifera, revealed that pteropsin is expressed in the brain of this species and not in either the simple or compound eyes. It was also possible, on the basis of in situ hybridization studies, to assign different long wavelength opsins to the compound eyes (AmLop1) and ocelli (AmLop2). Insect pteropsin might be orthologous to a ciliary opsin recently described from the annelid Platynereis, and therefore represents the presence of this vertebrate-like light-detecting system in insects.

Animals↗
PubMed1997

A novel and ancient vertebrate opsin.

We describe the identification of a novel opsin gene isolated from the eyes of Atlantic salmon. The cDNA sequence predicts a protein that has the key features of an opsin, but shows only 32-42% amino acid identity to the known opsin families. Phylogenetic analysis suggests that this opsin is a member of a hitherto unrecognised opsin family that diverged early in the evolution of vertebrate photopigments. We have tentatively called this opsin family the vertebrate ancient (VA) opsins. The identification of VA opsin may ultimately help to resolve some of the uncharacterised photoreceptor functions of the eye, which include the regulation of circadian rhythms, pupil size and corneal pigmentation.

Amino Acid Sequence↗
PubMed1986

Visual pigment homologies revealed by DNA hybridization.

A bovine rhodopsin complementary DNA probe was used to detect homologous visual pigment genes in a variety of species. Under stringent DNA hybridization conditions, genomic DNA from most vertebrate species carried a single homologous fragment. Additional homologies were detected in some vertebrates by reducing the hybridization stringency. Homologous fragments were also detected in DNA isolated from invertebrate species, a unicellular alga, and an archaebacterium; many of these fragments were homologous to a Drosophila opsin probe. These results suggest that photosensory pigments in a wide variety of species arose from a common precursor.

Animals↗
PubMed1994

Multiple origins of the green-sensitive opsin genes in fish.

Vertebrate opsins are divided into four major groups: RH1 (rhodopsins), RH2 (rhodopsinlike with various absorption sensitivities), SWS (short-wavelength sensitive), and LWS/MWS (long and middle-wavelength sensitive) groups. The green opsin genes (g101Af and g103Af) in a Mexican characin Astyanax fasciatus belong to the LWS/MWS group, whereas those in goldfish belong to the RH2 group (Yokoyama 1994, Mol Biol Evol 11:32-39). A newly isolated opsin gene (rh11Af) from A. fasciatus contains five exons and four introns, spanning 4.2 kilobases from start to stop codons. This gene is most closely related to the two green opsin genes of goldfish and belongs to the RH2 group. In the LWS/MWS group, gene duplication of the ancestral red and green opsin genes predates the speciation between A. fasciatus and goldfish, suggesting that goldfish also has an additional gene which is orthologous to g101Af and g103Af.

Amino Acid Sequence↗
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↗
PubMed2005

Characterization of the long-wavelength opsin from Mecoptera and Siphonaptera: does a flea see?

Mecoptera and Siphonaptera represent two insect orders that have largely been overlooked in the study of insect vision. Recent phylogenetic evidence demonstrates that Mecoptera (scorpionflies) is paraphyletic, with the order Siphonaptera (fleas) nesting as sister to the family Boreidae (snow fleas), showing an evolutionary trend towards reduction in gross eye morphology within fleas. We provide the first molecular characterization of long-wavelength opsins from these three lineages (opsin gene from fleas [FL-Opsin], the Boreidae [B-Opsin], and a mecopteran family [M-Opsin]) and assess the effects of loss of visual acuity on the structure and function of the opsin gene. Phylogenetic analysis implies a physiological sensitivity in the red-green spectrum for these opsins. Analysis of intron splice sites reveals a high degree of similarity between FL-Opsin and B-Opsin as well as conserved splice sites across insect blue-green and long-wavelength opsins. Calculated rates of evolution and tests for destabilizing selection indicate that FL-Opsin, B-Opsin, and M-Opsin are evolving at similar rates with no radical selective pressures, implying conservative evolution and functional constraint across all three lineages.

Animals↗
PubMed2006

Beauty in the eye of the beholder: the two blue opsins of lycaenid butterflies and the opsin gene-driven evolution of sexually dimorphic eyes.

Although previous investigations have shown that wing coloration is an important component of social signaling in butterflies, the contribution of opsin evolution to sexual wing color dichromatism and interspecific divergence remains largely unexplored. Here we report that the butterfly Lycaena rubidus has evolved sexually dimorphic eyes due to changes in the regulation of opsin expression patterns to match the contrasting life histories of males and females. The L. rubidus eye contains four visual pigments with peak sensitivities in the ultraviolet (UV; lambdamax=360 nm), blue (B; lambdamax=437 nm and 500 nm, respectively) and long (LW; lambdamax=568 nm) wavelength range. By combining in situ hybridization of cloned opsin-encoding cDNAs with epi-microspectrophotometry, we found that all four opsin mRNAs and visual pigments are expressed in the eyes in a sex-specific manner. The male dorsal eye, which contains only UV and B (lambdamax=437 nm) visual pigments, indeed expresses two short wavelength opsin mRNAs, UVRh and BRh1. The female dorsal eye, which also has the UV and B (lambdamax=437 nm) visual pigments, also contains the LW visual pigment, and likewise expresses UVRh, BRh1 and LWRh mRNAs. Unexpectedly, in the female dorsal eye, we also found BRh1 co-expressed with LWRh in the R3-8 photoreceptor cells. The ventral eye of both sexes, on the other hand, contains all four visual pigments and expresses all four opsin mRNAs in a non-overlapping fashion. Surprisingly, we found that the 500 nm visual pigment is encoded by a duplicate blue opsin gene, BRh2. Further, using molecular phylogenetic methods we trace this novel blue opsin gene to a duplication event at the base of the Polyommatine+Thecline+Lycaenine radiation. The blue opsin gene duplication may help explain the blueness of blue lycaenid butterflies.

Animal Communication↗
PubMed1984

Immunoreactivity of rhodopsin and opsin.

An examination by a radioimmunoassay of the relative affinity of opsin and rhodopsin for rabbit antibody raised against bovine rhodopsin revealed that opsin was the preferred antigen. About 10-fold greater amounts of rhodopsin than opsin were required to achieve 50% inhibition of binding of 125I-labeled ligand in the RIA. Opsin was more reactive when examined in the light or dark, compared to rhodopsin incubated in the dark. Mixtures of opsin and rhodopsin (prepared by partial bleaching of rhodopsin or synthetic mixtures) exhibited increased reactivity with increasing mole fraction of opsin. This response was nonlinear, with small increases in opsin producing relatively large increases in reactivity. A partial fractionation of the antibody into two groups showing differential reactivities toward opsin and rhodopsin was achieved by affinity chromatography on opsin-Sepharose. However, with both groups, opsin was still the preferred antigen. Scatchard analysis of 125I-labeled rhodopsin and opsin produced nonlinear plots, indicating the presence of multiple species of antibody. The affinities and binding capacities were similar for both labeled antigens. In competitive binding studies, the antibody showed a strong preference for either labeled ligand (rhodopsin or opsin) as compared to the unlabeled material. These latter observations indicate that altering rhodopsin either by bleaching or iodination produced changes in the relative immunoreactivity of the molecule.

Animals↗
PubMed1996

Cyclophilin-related protein RanBP2 acts as chaperone for red/green opsin.

Cyclophilins are ubiquitous and abundant proteins that exhibit peptidyl prolyl cis-trans isomerization (PPlase) activity in vitro. Their functions in vivo, however, are not well understood. Two new retinal cyclophilin isoforms, types I and II, are highly expressed in cone photoreceptors of the vertebrate retina. Type-II cyclophilin is identical to RanBP2, a large protein that binds the GTPase Ran. Here we report that two contiguous domains in RanBP2, Ran-binding domain 4 (RBD4) and cyclophilin, act in concert as a chaperone for the opsin molecule of the red/green-sensitive visual pigment of a dichromatic vertebrate. In Drosophila, the cyclophilin NinaA is expressed in all photoreceptors and is required for the expression of only a subset of opsins. The molecular basis of these photoreceptor class-specific effects and the functions of NinaA and other cyclophilins in vivo remain unclear. Unlike NinaA, which forms a stable complex with opsin from retinular cells R1-6, we find that the cyclophilin domain of RanBP2 does not bind opsin directly; rather, it augments and stabilizes the interaction between red/green (R/G) opsin and the RBD4 domain. This involves a cyclophilin-mediated modification of R/G opsin, possibly involving proline isomerization. The RBD4-cyclophilin supradomain of RanBP2, therefore, is a form of vertebrate chaperone of defined substrate specificity, which may be involved in the processing and/or transport of long-wavelength opsin in cone photoreceptor cells.

Amino Acid Isomerases↗