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PubMed1996

Light perception in the vertebrate brain: an ultrastructural analysis of opsin- and vasoactive intestinal polypeptide-immunoreactive neurons in iguanid lizards.

Recent biochemical and immunocytochemical evidence indicates that a population of circadian and reproductive rhythm-entraining photoreceptors lies in the basal diencephalon of iguanid lizards. Here, we report the results of correlated light and electron microscopy of opsin-immunoreactive cells in the basal brain, and we discuss their ultrastructural relationship to known photoreceptors. Cerebrospinal fluid (CSF)-contacting bipolar neurons in the lizards Anolis carolinensis and Iguana iguana were immunolabeled with antisera generated against vertebrate retinal opsins and vasoactive intestinal polypeptide (VIP). Within the brain, opsin-immunoreactive cells were found exclusively in the ependyma of the basal region of the lateral ventricles (adjacent to nucleus paraolfactorius/nucleus ventromedialis and neostriatum/paleostriatum). Cells in the same anatomical location and with the same morphology were labeled with anti-VIP antisera. These cells possessed a dendritic process that extended toward the lateral ventricle, ending in a bulbous terminal that protruded into the ventricle. Axonal processes travelled ventrally and caudally. The entire cell, including the axonal process, exhibited opsin-like and VIP-like immunoreactivity. By light microscopy, opsin-like immunostaining appeared punctate, with immunoreactivity greatest in the bulbous terminal. Opsin- and VIP-immunostained thick sections were resectioned, and individual cells observed by light microscopy were then characterized using electron microscopy. We found that all immunostained cells were morphologically similar and that they were morphologically distinct from neighboring nonimmunoreactive cells. CSF-contacting opsin- and VIP-immunoreactive cells lacked the membranous stacks characteristic of retinal photoreceptors but were ciliated and contained numerous large electron-dense vesicles. Multiple synaptic contacts were made on the soma and putative dendritic processes of opsin- and VIP-immunoreactive CSF-contacting neurons. Our results provide the first ultrastructural characterization of opsin-immunostained encephalic CSF-contacting neurons in a vertebrate animal, and they indicate that these putative photoreceptors share structural features with pineal photoreceptors and with certain invertebrate extraretinal photoreceptors, but they are morphologically and biochemically distinct from visual photoreceptors of the retina.

Animals↗
PubMed1999

Evolution of visual pigments in geckos.

Most geckos are nocturnal forms and possess rod retinas, but some diurnal genera have pure-cone retinas. We isolated cDNAs encoding the diurnal gecko opsins, dg1 and dg2, similar to nocturnal gecko P521 and P467, respectively. Despite the large morphological differences between the diurnal and nocturnal gecko photoreceptor types, they express phylogenetically closely related opsins. These results provide molecular evidence for the reverse transmutation, that is, rods of an ancestral nocturnal gecko have backed into cones of diurnal geckos. The amino acid substitution rates of dgl and dg2 are higher than those of P521 and P467, respectively. Changes of behavior regarding photic environment may have contributed to acceleration of amino acid substitutions in the diurnal gecko opsins.

Amino Acid Sequence↗
PubMed2006

Bone morphogenetic protein 7 increases chick photoreceptor outer segment initiation.

PURPOSE: The purpose of this study was to investigate the regulation of photoreceptor differentiation and outer segment elongation by the growth factor BMP7. METHODS: Dissociated low-density embryonic day 6 (E6) chick retinal cultures were grown for 6 days in the presence of BMP7, other members of the TGF-beta family of growth factors, or control vehicle. Cultured cells were characterized using microscopy, immunocytochemistry, and RT-PCR. Antibodies against visinin and GABA were used to distinguish photoreceptors from nonphotoreceptor cells, and monoclonal antibodies rhodopsin (rho) 4D2, OS-2, and COS-1 were used to distinguish subpopulations of cones and rods. RT-PCR was used to investigate mRNAs encoding visual pigments. RESULTS: Photoreceptors treated with BMP7 initiated outer segment elongation more frequently than photoreceptors in control cultures. The effect on outer segment initiation was confined to rods and to green opsin-expressing cones and appeared not to involve an increase in outer segment length. BMP7 did not appear to affect the survival, proliferation, or differentiation of progenitors or the fate of photoreceptors or amacrine cells in vitro. BMP5 and GDF5 showed weaker stimulatory effects than BMP7 on outer segment formation, whereas activin, BMP2, and BMP4 inhibited visual pigment expression and outer segment formation, and BMP6 had no detectable effects. CONCLUSIONS: BMP7 must be added to the list of candidate molecules capable of stimulating outer segment formation.

Animals↗
PubMed1992

Structural comparison of metarhodopsin II, metarhodopsin III, and opsin based on kinetic analysis of Fourier transform infrared difference spectra.

Fourier transform infrared difference spectra were measured at 30-s intervals after a complete bleach of rhodopsin (rho) samples at 20 degrees C and three different pH values. At each pH, all of the spectra could be fit globally to two exponential decay processes. Using a branched unimolecular kinetic model in which metarhodopsin II (meta II) is hydrolyzed to opsin and retinal both directly and through metarhodopsin III (meta III), we calculated rho-->meta II, rho-->meta III, and rho-->opsin difference spectra at each of the pH values and obtained estimates for the microscopic rate constants at each pH. Because of assumptions that had to be made about the branching ratio between the meta II decay pathways, some uncertainties remain in our calculated rho-->meta III difference spectrum at each pH. Nevertheless, our data covering long time ranges, especially those obtained at pH 8, place significant new constraints on the spectrum of meta III and thus on its structure. The rho-->meta II spectrum shows no significant pH dependence over the range examined (pH 5.5-8). However, the rho-->meta III and rho-->opsin spectra each include a limited subset of pH-dependent peaks, which are mostly attributable to titratable amino acid side chains. Our observations can be used to refine an earlier conclusion that the visual pigment refolds to a rhodopsin-like conformation during meta II decay (Rothschild, K.J., J. Gillespie, and W.J. DeGrip. 1987 Biophys. J. 51:345-350). Most of this refolding occurs in the same way at pH values ranging from 5.5 to 8 and whether meta II decays to meta III or opsin. Meta II displays unique spectral perturbations that are mostly attributable to a few residues, probably including three to four aspartic or glutamic acids and an arginine.

Animals↗
PubMed1987

Immunoelectron microscopic localization of photoreceptor-specific markers in the monkey retina.

Antibodies for several molecules that function in the visual process were used to localize these molecules in primate rod and cone cells. These antibodies (monoclonal or polyclonal) were prepared against Interphotoreceptor Retinoid-binding Protein (IRBP), S-antigen (S-Ag), opsin, alpha-transducin and also against cyclic GMP (cGMP). Lowicryl-embedded tissues were labeled with secondary antibodies linked to colloidal gold. Although IRBP is predominantly an extracellular protein, the relatively small amount found intracellularly was localized mainly in rods, with little in cones. Opsin, S-Ag and cGMP were found mainly in rod cell outer segments. A polyclonal antiserum raised against transducin-alpha purified from rod outer segments predominantly labeled rod cells, but an antiserum against the carboxyterminal decapeptide of transducin-alpha labeled both rod and cone cells. Thus, most of these specialized molecules are present predominantly in rod cells, confirming major differences in components of the visual cycle in rods and cones.

Animals↗
PubMed2006

Heterologous expression of bovine rhodopsin in Drosophila photoreceptor cells.

PURPOSE: Vertebrate and invertebrate visual pigments are similar in amino acid sequence, structural organization, spectral properties, and mechanism of action, but possess different chromophores and trigger phototransduction through distinct biochemical pathways. The bovine opsin gene (Rho) was expressed in Drosophila, to examine the properties of a vertebrate opsin within invertebrate photoreceptor cells. METHODS: Transgenic Drosophila expressing the bovine opsin gene (Rho) in photoreceptors were created. Protein expression and cellular location of bovine rhodopsin was assessed by protein blots and immunofluorescence. The glycosylation state was determined by mobility profiles in SDS-PAGE before and after treatment with endoglycosidase. The rhodopsin chromophore was determined by HPLC-mass spectroscopy (MS) and the spectral properties by spectroscopy. The ability of the bovine rhodopsin to couple to Drosophila phototransduction components was assessed by electroretinography and to couple to vertebrate transducin by light-mediated GTPgammaS-binding assays. RESULTS: Rho showed stable expression even in the absence of endogenous Rh1 opsin and chromophore. It was correctly targeted to the rhabdomeric membranes. Rho remained glycosylated during the maturation process and possessed a distinct glycosylation pattern from that of native Rho. The Drosophila-expressed Rho associated with the 3-hydroxyretinal chromophore but failed to evoke an electroretinogram response from fly photoreceptors. However, the Drosophila-expressed Rho activated transducin in a light-dependent manner. CONCLUSIONS: Drosophila photoreceptors express a vertebrate rhodopsin as a functional visual pigment, but the expression does not activate the Drosophila phototransduction pathway. The system allows the characterization and comparison of vertebrate and invertebrate visual pigment properties in a common cell type.

Animals↗
PubMed2006

Overview of retinoid metabolism and function.

Retinoids (vitamin A) are crucial for most forms of life. In chordates, they have important roles in the developing nervous system and notochord and many other embryonic structures, as well as in maintenance of epithelial surfaces, immune competence, and reproduction. The ability of all-trans retinoic acid to regulate expression of several hundred genes through binding to nuclear transcription factors is believed to mediate most of these functions. The role of all-trans retinoic may extend beyond the regulation of gene transcription because a large number of noncoding RNAs also are regulated by retinoic acid. Additionally, extra-nuclear mechanisms of action of retinoids are also being identified. In organisms ranging from prokaryotes to humans, retinal is covalently linked to G protein-coupled transmembrane receptors called opsins. These receptors function as light-driven ion pumps, mediators of phototaxis, or photosensory pigments. In vertebrates phototransduction is initiated by a photochemical reaction where opsin-bound 11-cis-retinal is isomerized to all-trans-retinal. The photosensitive receptor is restored via the retinoid visual cycle. Multiple genes encoding components of this cycle have been identified and linked to many human retinal diseases. Central aspects of vitamin A absorption, enzymatic oxidation of all-trans retinol to all-trans retinal and all-trans retinoic acid, and esterification of all-trans retinol have been clarified. Furthermore, specific binding proteins are involved in several of these enzymatic processes as well as in delivery of all-trans retinoic acid to nuclear receptors. Thus, substantial progress has been made in our understanding of retinoid metabolism and function. This insight has improved our view of retinoids as critical molecules in vision, normal embryonic development, and in control of cellular growth, differentiation, and death throughout life.

Animals↗
PubMed2001

Photoreceptor subtype specification: from flies to humans.

Multiple cell types often differentiate from a pluripotent cell. These cells may then further diversify as distinct subtypes. The visual system provides an ideal model for studying subtype specification as various photoreceptors acquire different functions based on the type of opsin they express. Opsin expression is mostly controlled through transcriptional mechanisms that are evolutionary conserved from Drosophila to humans. In addition, it appears that, from a "default" developmental state, distinct "acquired" photoreceptor states develop upon receiving intrinsic or extrinsic signals. This review discusses factors involved in opsin gene regulation and how their integration may explain how subtype specificity is achieved.

Animals↗
PubMed1997

The molecular evolution of visual pigments of freshwater crayfishes (Decapoda: Cambaridae).

This study examines the diverse maximum wavelength absorption (lambdamax) found in crayfishes (Decapoda: Cambaridae and Parastacidae) and the associated genetic variation in their opsin locus. We measured the wavelength absorption in the photoreceptors of six species that inhabit environments of different light intensities (i.e., burrows, streams, standing waters, and subterranean waters). Our results indicate that there is relatively little variation in lambdamax (522-530 nm) among species from different genera and families. The existing variation did not correlate with the habitat differences of the crayfishes studied. We simultaneously sequenced the rhodopsin gene to identify the amino acid replacements that affect shifts in maximum wavelength absorption. We then related these to changes that correlated with shifts in lambdamax by reconstructing ancestral character states using a maximum-likelihood approach. Using amino acid sequences obtained from five species (all were 301 amino acids in length), we identified a number of candidates for producing shifts of 4 to 8 nm in lambdamax. These amino acid replacements occurred in similar regions to those involved in spectral shifts in vertebrates.

Amino Acid Sequence↗
PubMedDate not supplied

Independent variation of retinal S and M cone photoreceptor topographies: A survey of four families of mammals.

In mammals, cone photoreceptor subtypes are thought to establish topographies that reflect the species-relevant properties of the visual environment. Middle- to long-wavelength-sensitive (M) cones are the dominant population and in most species they form an area centralis at the visual axis. Short-wavelength-sensitive (S) cone topographies do not always match this pattern. We here correlate the interrelationship of S and M cone topographies in representatives of several mammalian orders with different visual ecology, including man, cheetah, cat, Eurasian lynx, African lion, wild hog, roe deer, and red deer. Retinas were labeled with opsin antisera and S and M cone distributions as well as S/M cone ratios were mapped. We find that species inhabiting open environments show M cone horizontal streaks (cheetah, pig, deer). Species living in structured habitats (tiger, lynx, red deer) have increased S cone densities along the retinal margin. In species with active vision (cheetah, bear, tiger, man), S cone distributions are more likely to follow the centripetal M cone gradients. Small species show a ventral bias of peak S cone density which either matches the peak of M cone density in a temporal area centralis (diurnal sciurid rodents, tree shrews) or not (cat, manul, roe deer). Thus, in addition to habitat structure, physical size and specific lifestyle patterns (e.g. food acquisition) appear to underlie the independent variations of M and S cone topographies.

Animals↗
PubMed2001

Non-visual ocular photoreception.

At least six light-regulated phenomena are preserved in the eyes of retinally degenerate mice, including the entrainment of circadian rhythms, the gating of ocular immune response, and pupillary reactivity. Some of these phenomena have also been observed in blind human patients. These findings have prompted the search for a non-visual ocular phototransduction mechanism. Molecular genetic studies have identified several candidate genes for these effects. These include genes encoding novel ocular opsins, such as melanopsin, as well as potential flavin-based photopigments. Data linking these potential photoreceptors to these phenomena are discussed, and the clinical implications of these findings are explored.

Animals↗
PubMed1956

The nature of the gecko visual pigment.

Retinal extracts of the Australian gecko, Phyllurus milii (White), have revealed the presence of a photosensitive pigment, unusual for terrestrial animals, because of its absorption maximum at 524 mmicro. This pigment has an absorption spectrum which is identical in form with that of other visual chromoproteins. It is not a porphyropsin, for bleaching revealed the presence, not of retinene(2), but of retinene(1) as a chromophore. Photolabile pigments with characteristics similar to those of the Phyllurus visual pigment were also detected in retinal extracts of six other species of nocturnal geckos. The presence of this retinal chromoprotein adequately accounts for the unusual visual sensitivity curve described by Denton for the nocturnal gecko. This pigment may have special biological significance in terms of the unique phylogenetic position of geckos as living representatives of nocturnal animals which retain some of the characteristics of their diurnal ancestors. The occurrence of this retinene(1) pigment, intermediate in spectral position between rhodopsin and iodopsin, is interpreted in support of the transmutation theory of Walls. The results and interpretation of this investigation point up the fact that, from a phylogenetic point of view, too great an emphasis on the duplicity theory may serve to detract attention from the evolutionary history of the retina and the essential unitarianism of the visual cells.

Animals↗
PubMed1952

The role of sulfhydryl groups in the bleaching and synthesis of rhodopsin.

The condensation of retinene(1) with opsin to form rhodopsin is optimal at pH about 6, a pH which favors the condensation of retinene(1) with sulfhydryl rather than with amino groups. The synthesis of rhodopsin, though unaffected by the less powerful sulfhydryl reagents, monoiodoacetic acid and its amide, is inhibited completely by p-chloromercuribenzoate (PCMB). This inhibition is reversed in part by the addition of glutathione. PCMB does not attack rhodopsin itself, nor does it react with retinene(1). Its action in this system is confined to the -SH groups of opsin. Under some conditions the synthesis of rhodopsin is aided by the presence of such a sulfhydryl compound as glutathione, which helps to keep the -SH groups of opsin free and reduced. By means of the amperometric silver titration of Kolthoff and Harris, it is shown that sulfhydryl groups are liberated in the bleaching of rhodopsin, two such groups for each retinene(1) molecule that appears. This is true equally of rhodopsin from the retinas of cattle, frogs) and squid. The exposure of new sulfhydryl groups adds an important element to the growing evidence that relates the bleaching of rhodopsin to protein denaturation. The place of sulfhydryl groups in the structure of rhodopsin is still uncertain. They may be concerned directly in binding the chromophore to opsin; or alternatively they may furnish hydrogen atoms for some reductive change by which the chromophore is formed from retinene(1). In the amperometric silver titration, the bleaching of rhodopsin yields directly an electrical variation. This phenomenon may have some fundamental connection with the role of rhodopsin in visual excitation, and may provide a model of the excitation process in general.

Animals↗
PubMed2002

Activation of mislocalized opsin kills rod cells: a novel mechanism for rod cell death in retinal disease.

Rod photoreceptors are highly compartmentalized sensory neurons that maintain strict ultrastructural and molecular polarity. Structural subdivisions include the outer segment, inner segment, cell body, and synaptic terminal. The visual pigment rhodopsin is found predominantly in membranes of the rod cell outer segment but becomes mislocalized, appearing throughout the plasma membrane of the cell in many retinal diseases and injuries. Currently, there is no known link between rhodopsin redistribution and rod cell death. We propose that activation of mislocalized rhodopsin kills rod cells by stimulating normally inaccessible signaling pathways. This hypothesis was tested in primary retinal cell cultures, which contain photoreceptors. In rod photoreceptors, opsin immunofluorescence occurred throughout the rod cell plasma membrane. Activation of this mislocalized opsin by photostimulation after formation of isorhodopsin or by incubation with beta-ionone (opsin agonist) killed 19-30% of rod cells. Rod cell death was apoptotic, as indicated by marked chromatin condensation and the requirement for caspase-3 activation. Rod cell death could be induced by forskolin (adenylate cyclase agonist), and conversely, beta-ionone-induced cell death could be blocked by cotreatment with SQ22536 (an adenylate cyclase inhibitor). Pertussis toxin (a G protein inhibitor) also blocked beta-ionone-induced cell death. The data support a mechanism by which activation of mislocalized opsin initiates apoptotic rod cell death through G protein stimulation of adenylate cyclase.

Adenine↗
PubMedDate not supplied

Cone visual pigments of the Australian marsupials, the stripe-faced and fat-tailed dunnarts: sequence and inferred spectral properties.

Studies of color vision in marsupial mammals have been very limited. Two photoreceptor genes have been characterized from the tammar wallaby, but a third cone pigment was suggested by microspectrophotometric measurements on cone photoreceptors in two other species, including the fat-tailed dunnart, Sminthopsis crassicaudata. To determine the sequence and infer absorption maxima of the cone photoreceptor pigments of S. crassicaudata and the related stripe-faced dunnart (Sminthopsis macroura), we have used evolutionarily conserved sequences of the cone pigments of other species, including the tammar wallaby, to design primers to amplify the S. macroura and S. crassicaudata pigment sequences by the polymerase chain reaction (PCR) using genomic DNA or retinal cDNA as a template. These primers will be useful for amplifying cone opsin coding sequences from a variety of vertebrates. Amplified products were directly sequenced to determine gene structure and coding sequences. The inferred amino acid sequences of the cone visual pigments indicated that both species have middle-wave-sensitive (MWS) pigments with a predicted absorption maximum (lambda(max)) at 530 nm, and ultraviolet-sensitive (UVS) pigments with a predicted lambda(max) at 360 nm. The MWS pigments of the two species differ by two, and UVS by three amino acid positions. No evidence was obtained for a third cone pigment in either species.

Amino Acid Sequence↗
PubMed2006

Glycine receptors in a population of adult mammalian cones.

Glycinergic interplexiform cells provide a feedback signal from the inner retina to the outer retina. To determine if cones receive such a signal, glycine was applied on cultured porcine cone photoreceptors recorded with the patch clamp technique. A minor population of cone photoreceptors was found to generate large currents in response to puff application of glycine. These currents reversed close to the calculated equilibrium potential for chloride ions. These glycine-elicited currents were sensitive to strychnine but not to picrotoxin consistent with the expression of alpha-beta-heteromeric glycine receptors. Glycine receptors were also activated by taurine and beta-alanine. The glycine receptor antibody mAb4a labelled a minority of the cone photoreceptors identified by an antibody specific for cone arrestin. Finally, expression of the beta subunit of the glycine receptor was demonstrated by single cell RT-PCR in a similar proportion (approximately 13%) of cone photoreceptors freshly isolated by lectin-panning. The identity of cone photoreceptors was assessed by their specific expression of the cone arrestin mRNA. The population of cone photoreceptors expressing the glycine receptor was not correlated to a specific colour-sensitive subtype as demonstrated by single cell RT-PCR experiments using primers for S opsin, cone arrestin and glycine receptor beta subunit. This glycine receptor expression in a minority of cones defines a new cone population suggesting an unexpected role for glycine in the visual information processing in the outer retina.

Animals↗
PubMed1981

Photochemical reactions of 13-demethyl visual pigment analogues at low temperatures.

The photobleaching reaction of 13-demethylisorhodopsin (hereafter designated as 9-cis- 13-dm-rhodopsin), which was synthesized from 9-cis- 13-demethylretinal and cattle opsin, was investigated by low-temperature spectrophotometry in order to elucidate the role of the 13-methyl group of retinal in photobleaching. When 9-cis- 13-dm-rhodopsin was irradiated at-190 degrees C, batho-13-dm-rhodopsin was produced. Its absorption maximum lay at 532 nm, 11 nm shorter than that of cattle bathorhodopsin (gamma max 543 nm), and batho-13-dm-rhodopsin had an extinction coefficient about 0.6 times that of bathorhodopsin. Batho-13-dm-rhodopsin was thermally unstable. Above-180 degrees C, it converted to a new intermediate, BL-13-dm-rhodopsin, which in turn changed to lumi-13-dm-rhodopsin- above -140 degrees C. BL-13-dm-rhodopsin was "photosensitive" at temperatures around -188 degrees C, though batho-13-dm-rhodopsin and lumi-13-dm-rhodopsin was "photosensitive" at the same temperature. In the photobleaching process, lumi-13-dm-rhodopsin and meta-I-13-dm-rhodopsin were observed. Their thermostabilities were very similar to those of lumirhodopsin and metarhodopsin I, but each dm intermediate differed from its methylated counterpart in its value of gamma max and extinction coefficient.

Animals↗
PubMed1994

An analysis of two spectral properties of vertebrate visual pigments.

Spectral data are scrutinized on two properties: (1) the chromophore-induced wavelength shift, i.e. the variation in absorbance maximum (lambda max) upon exchanging the vitamin A1-based chromophore with one based on vitamin A2 in the same opsin; (2) the half-band width (HBW) variation as a function of the reciprocal of the peak absorbance (lambda max)-1. It is shown that in an extended spectral range that includes the UV and when data are plotted in wavenumbers, the chromophore-induced shifts can be approximated with a parabola, whose minimum occurs near 23,000 cm-1 (approximately 430 nm). Similarly, HBW variations can also be fitted with parabolas, however, these show maxima near 430 nm. The theoretical implications of the two phenomena concerning lambda max tuning in vertebrate visual pigments are discussed.

Amphibians↗