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PubMed1995

Opsin genes.

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Amino Acid Sequence↗
PubMed1953

The molar extinction of rhodopsin.

The molar extinction of rhodopsin is 40,600 cm.(2) per mole equivalent of retinene; i.e., this is the extinction of a solution of rhodopsin which is produced by, or yields on bleaching, a molar solution of retinene. The molar extinctions of all-trans retinene and all-trans retinene oxime have also been determined in ethyl alcohol and aqueous digitonin solutions. On the assumption that each chromophoric group of rhodopsin is made from a single molecule of retinene, it is concluded that the primary photochemical conversion of rhodopsin to lumi-rhodopsin has a quantum efficiency of 1; though the over-all bleaching of rhodopsin in solution to retinene and opsin may have a quantum efficiency as low as one-half. On bleaching cattle rhodopsin, about two sulfhydryl groups appear for each molecule of retinene liberated. In frog rhodopsin the -SH:retinene ratio appears to be higher, 5:2 or perhaps even 3:1. Some of this sulfhydryl appears to have been engaged in binding retinene to opsin; some may have been exposed as the result of changes in opsin which accompany bleaching, comparable with protein denaturation.

Animals↗
PubMed2000

A simple method for classifying genes and a bootstrap test for classifications.

A new simple method for classifying genes is proposed based on Klastorin's method. This method classifies genes into monophyletic groups which are made distinct from each other by evolutionary changes. The method is applicable as long as the phylogenetic tree of genes is obtained. There is a fast algorithm for obtaining the classification. A bootstrap test of a classification is also presented. As an example, we classified opsin genes. The classification obtained by this method is the same as the previous classification based on the function of opsins.

Algorithms↗
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↗
PubMed1999

Evolution of color vision.

Color vision is achieved by comparing the inputs from retinal photoreceptor neurons that differ in their wavelength sensitivity. Recent studies have elucidated the distribution and phylogeny of opsins, the family of light-sensitive molecules involved in this process. Interesting new findings suggest that animals have evolved a strategy to achieve specific sensitivity through the mutually exclusive expression of different opsin genes in photoreceptors.

Animals↗
PubMed1958

The rhodopsin system of the squid.

Squid rhodopsin (lambda(max) 493 mmicro)-like vertebrate rhodopsins-contains a retinene chromophore linked to a protein, opsin. Light transforms rhodopsin to lumi- and metarhodopsin. However, whereas vertebrate metarhodopsin at physiological temperatures decomposes into retinene and opsin, squid metarhodopsin is stable. Light also converts squid metarhodopsin to rhodopsin. Rhodopsin is therefore regenerated from metarhodopsin in the light. Irradiation of rhodopsin or metarhodopsin produces a steady state by promoting the reactions, See PDF for Equation Squid rhodopsin contains neo-b (11-cis) retinene; metarhodopsin all-trans retinene. The interconversion of rhodopsin and metarhodopsin involves only the stereoisomerization of their chromophores. Squid metarhodopsin is a pH indicator, red (lambda(max) 500 mmicro) near neutrality, yellow (lambda(max) 380 mmicro) in alkaline solution. The two forms-acid and alkaline metarhodopsin-are interconverted according to the equation, Alkaline metarhodopsin + H(+) right harpoon over left harpoonacid metarhodopsin, with pK 7.7. In both forms, retinene is attached to opsin at the same site as in rhodopsin. However, metarhodopsin decomposes more readily than rhodopsin into retinene and opsin. The opsins apparently fit the shape of the neo-b chromophore. When light isomerizes the chromophore to the all-trans configuration, squid opsin accepts the all-trans chromophore, while vertebrate opsins do not and hence release all-trans retinene. Light triggers vision by affecting directly the shape of the retinene chromophore. This changes its relationship with opsin, so initiating a train of chemical reactions.

Animals↗
PubMed2000

Sequence, genomic structure and tissue expression of carp (Cyprinus carpio L.) vertebrate ancient (VA) opsin.

We report the isolation and characterisation of a novel opsin cDNA from the retina and pineal of the common carp (Cyprinus carpio L.). When a comparison of the amino acid sequences of salmon vertebrate ancient opsin (sVA) and the novel carp opsin are made, and the carboxyl terminus is omitted, the level of identity between these two opsins is 81% and represents the second example of the VA opsin family. We have therefore termed this C. carpio opsin as carp VA opsin (cVA opsin). We show that members of the VA opsin family may exist in two variants or isoforms based upon the length of the carboxyl terminus and propose that the mechanism of production of the short VA opsin isoform is alternative splicing of intron 4 of the VA opsin gene. The VA opsin gene consists of five exons, with intron 2 significantly shifted in a 3' direction relative to the corresponding intron in rod and cone opsins. The position (or lack) of intron 2 appears to be a diagnostic feature which separates the image forming rod and cone opsin families from the more recently discovered non-visual opsin families (pin-opsins (P), vertebrate ancient (VA), parapinopsin (PP)). Finally, we suggest that lamprey P opsin should be reassigned to the VA opsin family based upon its level of amino acid identity, genomic structure with respect to the position of intron 2 and nucleotide phylogeny.

Amino Acid Sequence↗
PubMed2006

A frameshift mutation in RPGR exon ORF15 causes photoreceptor degeneration and inner retina remodeling in a model of X-linked retinitis pigmentosa.

PURPOSE: To characterize the course of retinal disease in X-linked progressive retinal atrophy 2 (XLPRA2), a canine model of early onset X-linked retinitis pigmentosa (XLRP) caused by a two-nucleotide microdeletion in RPGR ORF15. METHODS: The retinas of 25 XLPRA2-affected dogs (age range, 2-40.6 weeks) and age-matched control subjects were collected, fixed, and embedded in epoxy resin for morphologic evaluation or in optimal cutting temperature (OCT) medium for TUNEL assay and immunohistochemistry. Cell-specific antibodies were used to examine changes in rods and cones and to evaluate the effects of the primary photoreceptor degeneration on inner retinal cells. RESULTS: Abnormal development of photoreceptors was recognizable as early as 3.9 weeks of age. Outer segment (OS) misalignment was followed by their disorganization and fragmentation. Reduction in length and broadening of rod and cone inner segments (IS) was next observed, followed by the focal loss of rod and cone IS at later time points. The proportion of dying photoreceptors peaked at approximately 6 to 7 weeks of age and was significantly reduced after 12 weeks. In addition to rod and cone opsin mislocalization, there was early rod neurite sprouting, retraction of rod bipolar cell dendrites, and increased Müller cell reactivity. Later in the course of the disease, changes were also noted in horizontal cells and amacrine cells. CONCLUSIONS: XLPRA2 is an early-onset model of XLRP that is morphologically characterized by abnormal photoreceptor maturation followed by progressive rod-cone degeneration and early inner retina remodeling. The results suggest that therapeutic strategies for this retinal degeneration should target not solely photoreceptor cells but also inner retinal neurons.

Animals↗
PubMedDate not supplied

Co-expression of murine opsins facilitates identifying the site of cone adaptation.

Murine cones contain two opsins in the same cone, one ultraviolet (UV) and the other middle-wavelength sensitive (M). A long-wavelength flash only affecting M-opsin suppresses the cone electroretinogram (ERG) produced by light absorption of UV-cone opsin raising the hypothesis that activation of M-cone opsin suppresses UV-cone opsin responses in the same cone. Here we show that pharmacologic blockade of synaptic transmission in the superfused murine retina, which eliminates interaction from second-order neurons, fails to prevent suppression of the UV-opsin driven pathway by long-wavelength stimuli. This proves that the antagonism must be occurring in the same cone, co-expressing both opsins. Our results show that UV-opsin suppression successively ceases in presence of the M-opsin activating background light, which implies that cone light adaptation is controlled at the opsin stage, before activation of transducin. It also reveals the time course of a transient desensitization of cones due to post-opsin factors in the transduction cascade.

Adaptation, Ocular↗
PubMed1986

A concentration of fucosylated glycoconjugates at the base of cone outer segments: quantitative electron microscope autoradiography.

Rod photoreceptors show a discrete band of labeled molecules at the outer segment base shortly after the administration of radioactive protein precursors (Young, 1967). The band signifies the insertion of radiolabeled protein, primarily opsin, into rod disc membrane (Basinger, Bok and Hall, 1976). In contrast, the autoradiographic labeling pattern in cones is characteristically diffuse (Young, 1971), although cones as well as rods are now thought to replace their disc membranes continually (Anderson, Fisher, and Steinberg, 1978). Using grain count analysis in conjunction with electron microscope autoradiography, we demonstrate for the first time that the initial cone outer segment (COS) labeling pattern in the retinas of cone-dominant rodents is not random or diffuse after intraocular injection of [3H]-fucose--a specific glycoprotein precursor. Thirty minutes after [3H]-fucose injection, the Golgi complex is heavily labeled in both rods and cones. At 1.5 hr, labeling first appears in the periciliary region and in the basal portion of the COS. We detected a basal concentration of fucosylated molecules up to 12 hr after injection; thereafter, we found no differential distribution of labeled product molecules in COS. In rods, we observed no band of labeled protein at any of the time points sampled. The low level of labeling in rods is uniformly distributed between the basal and apical portion of the outer segments. Although the identity of the fucosylated material remains unknown, the early labeling of the Golgi complex--followed by labeling over the periciliary region and the basal portion of the outer segment--suggests that newly synthesized membrane protein is transported from sites of synthesis in the inner segment and inserted into disc membrane at the COS base. However, in contrast to rods, the protein is apparently capable of diffusing longitudinally throughout the interconnected membrane network.

Animals↗
PubMedDate not supplied

Cone receptor variations and their functional consequences in two species of hamster.

Results from earlier experiments indicate that different species of rodent vary both in the number of cone types found in their retinas and in the spectral sensitivities of the cone pigments. These features have now been examined in two types of hamster commonly used for research purposes: Syrian golden hamsters (Mesocricetus auratus) and Siberian dwarf hamsters (Phodopus sungorus). Electroretinogram (ERG) flicker photometry, behavioral discrimination tasks, and opsin antibody labeling were used to investigate hamster photoreceptors and their visual consequences. Results from the three approaches support the following conclusions: (1) The retinas of both species have an abundant population of rods containing a photopigment with peak sensitivity of about 498-500 nm; (2) Siberian dwarf hamsters have two classes of cone: one with maximum sensitivity in the ultraviolet (c. 360 nm), the other with peak sensitivity closely similar to that of its rod; and (3) Syrian golden hamsters have a class of cone with peak sensitivity at about 506 nm, but they lack a second cone type. Implications of these alternative arrangements are discussed.

Animals↗