Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “Retinaldehyde”

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 775 records · Page 43Linked to original sources
PubMed1983

Seasonal variation of the vitamin A2-based visual pigment in the retina of adult bullfrog, Rana catesbeiana.

Visual pigment composition was determined by HPLC analysis over a one-year period in the adult bullfrog (Rana catesbeiana). In Japan, the vitamin A2-based pigment was only 5% of the total visual pigment from the middle of July to October. The vitamin A2-based pigment increased in November and reached a maximum of 32-36% between January and June. This seasonal variation may relate to the average of outdoor temperature rather than the daylight hours. The amount of vitamin A2-based pigment began to increase when the average temperature became lower than 20 degrees C and it decreased rapidly as the average temperature was higher than 20 degrees C.

Animals↗
PubMed1984

Use of high-performance liquid chromatography in the analysis of retinyl and 3,4-didehydroretinyl compounds in tissue extracts of bullfrog tadpoles and goldfish.

HPLC (high-performance liquid chromatography) was used to analyse retinyl and 3,4-didehydroretinyl compounds in tissue extracts from goldfish and bullfrog tadpoles. Using silica columns (packed with 10-micron mu Porasil or 5-micron Ultrasphere particles) eluted with n-hexane (containing a small amount of dioxane or diethyl ether), the authentic all-trans retinyl and 3,4-didehydroretinyl palmitates, retinal and 3,4-didehydroretinal, retinol and 3,4-didehydroretinol were completely separated. Liver and eye extracts of the goldfish and bullfrog tadpoles had mainly esterified all-trans retinol and all-trans 3,4-didehydroretinol. In the liver, these vitamin A were conjugated to a number of fatty acids whereas in the eye, principally one fatty acid was used. Moreover, the relative proportions of all-trans retinol and all-trans 3,4-didehydroretinol (obtained by analysing the saponified esters) were significantly different between some of these body compartments.

Animals↗
PubMed1984

Pathways in the hydrolysis of vertebrate rhodopsin.

A direct method for measuring the amount of retinal 387 was used along with spectral techniques to measure each of the intermediates in the photolysis of rhodopsin and to unequivocally determine the pathways in solution extracts of bovine rhodopsin and excised toad and skate retinas. Metarhodopsin II 380 was the earliest intermediate which hydrolyzed to retinal 387 plus opsin. In excised toad retinas three approaches were used to show that Meta III 465 decayed directly to retinal 387 plus opsin. The only pathway consistent with the data was: (Formula: See text). In solution extracts the formation and hydrolysis of N-Retinylidene-Opsin was also observed.

Animals↗
PubMed1984

3-Dehydroretinal (vitamin A2 aldehyde) in crayfish eye.

11-Cis-3-dehydroretinal was found in the eye of crayfish, Procambarus clarkii. The 11-cis-3-dehydroretinal was isomerized to all-trans isomer by light-illumination, as was also 11-cis-retinal. Irradiation with deep-red light (lambda greater than 680 nm) selectively isomerized the 11-cis-3-dehydroretinal. The 3-dehydroretinal was not extracted with petroleum ether from the tissue after freeze-drying. These facts suggest that the 11-cis-3-dehydroretinal is the chromophore of crayfish visual pigment. The 3-dehydroretinal content varied with season, high level in winter and low in summer. The crayfish may have a vitamin A1-A2 visual pigment system similar to those of freshwater fishes and amphibians.

Animals↗
PubMed1984

Visual cycle in the mammalian eye. Retinoid-binding proteins and the distribution of 11-cis retinoids.

This work was designed to provide an insight into the mammalian visual cycle by investigating the possible function of retinoid-binding proteins in this system, and the distribution and type of 11-cis retinoids present in the interphotoreceptor matrix and the cytosols of the retinal pigment epithelium and retina. The total retinol and retinal in the soluble fractions from these three compartments was 8% (3.31 nmol/eye) of the retinyl palmitate and stearate stored in the pigment epithelium membrane fractions (39 nmol/eye). Only small amounts of retinoids were detected in the rod outer segment cytosol. The insoluble fractions also contained retinol, nearly all of which was found in the retina. The retinoids in the soluble fractions appeared to be bound to cellular retinol-binding protein (CRBP), cellular retinal-binding protein (CRA1BP) and interstitial retinol-binding protein (IRBP, a high-Mr glycoprotein). Using immunospecific precipitation, immunoblot and immunocytochemical techniques it was demonstrated that IRBP was localized in the interphotoreceptor matrix and was synthesized and secreted by the retina, a process that did not require the protein to be glycosylated. The amount of retinol bound to IRBP increased if the eyes were exposed to light, when it was estimated that the protein carried up to 30% of its full capacity for all-trans retinol. In addition to all-trans retinol, IRBP carried smaller amounts of 11-cis retinol. The proportion of 11-cis retinol was frequently higher in eyes that had been protected from illumination, suggesting that IRBP plays a role in rhodopsin regeneration during dark-adaptation. Additionally, endogenous 11-cis retinoids in the retina and RPE cytosols were bound to an Mr 33,000 protein tentatively identified as CRA1BP. The 11-cis retinoid in the retina cytosol was mainly in the form of retinol, while in the RPE cytosol it was mainly in the form of retinal. Substantial amounts of 11-cis retinol were also found in the insoluble (membrane) fraction from the retina. It is suggested that in the mammalian retina 11-cis retinol is generated from all-trans retinol (possibly in the Muller cells). Lack of an 11-cis retinol oxidoreductase in the retina prevents it from being utilized for rhodopsin regeneration until it has been transported to the pigment epithelium, where it is converted to 11-cis retinal and returned to the rod outer segments. It is also suggested that IRBP may be implicated in the transport of retinoids between the rod outer segments, the Muller cells and the pigment epithelium.(ABSTRACT TRUNCATED AT 400 WORDS)

Animals↗
PubMed1984

Properties and immunocytochemical localization of three retinoid-binding proteins from bovine retina.

Cellular retinal-binding protein (CRALBP) complexed with 11-cis-retinal has several properties characteristic of a visual pigment. Interaction of the protein and retinoid results in a bathochromic shift in the absorption spectrum of the chromophore from 380 to 425 nm, accompanied by a decrease in the extinction coefficient (25,000-15,000 M-1 cm-1). Illumination of the complex results in the progressive loss of absorbance at 425 nm and an increase at 375 nm, consistent with the production of a geometrical isomer of retinal that lacks affinity for the binding protein. Analysis by HPLC of the retinoids after illumination reveals that the basis of the spectral transition is a photoisomerization of 11-cis-retinal to all-trans-retinal. Only small amounts (less than 10%) of 13-cis-retinal are produced during the photoisomerization, showing the stereospecificity of the process. Although CRALBP has the spectral characteristics of a blue-sensitive visual pigment, there is no evidence that this is related to its function. This protein may serve as a model for the interactions of 11-cis-retinal and protein. Eleven-cis-retinol bound to CRALBP is a better substrate for esterification by microsomes from retinal pigment epithelium (RPE) than all-trans-retinol bound to cellular retinol-binding protein (CRBP). The product of the reaction, retinyl ester, does not remain bound to either binding protein but becomes associated with the microsomal fraction. Esterification is the first described process, occurring in the dark, by which retinoids can be removed from CRBP and CRALBP. Antibodies to bovine CRBP have been produced in rabbits following injection of the performic acid-oxidized protein.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed1984

Suitability of retinol, retinal and retinyl palmitate for the regeneration of bleached rhodopsin in the isolated frog retina.

The all-trans, 9-cis and 11-cis isomers of retinol, retinal and retinyl palmitate were incorporated into unilamellar dioleoyl-lecithin vesicles (liposomes). Isolated frog retinas were inserted into a perfusion chamber and their absorption spectra were recorded (i) in the dark-adapted state, (ii) after exposure to intense light that bleached greater than 95% of rhodopsin and (iii) after liposomes had been added to the perfusate of the bleached preparations. In each experiment, one of the above isomers of the retinol analogs was tested. Regeneration was promoted by the 9-cis and the 11-cis isomer of retinol and of retinal whereas the trans isomers of all compounds and the cis isomers of retinyl palmitate were inactive.

Animals↗
PubMed1984

Rod outer segment membranes: good acceptors for retinoids?

The exchange of all-trans retinoids (retinal, retinol, retinylpalmitate) between PC-vesicles, PC-vesicles and liver microsomes or PC-vesicles and rod outer segment membranes is investigated using 11,12(3)H labeled compounds. In the first two systems, retinal and retinol exchange rapidly, retinyl acetate slowly and retinyl palmitate not at all. Rod outer segment membranes however take up relatively small amounts of retinoids (retinylpalmitate less than retinol less than retinal) and rapidly lose 60-90% of their label in the presence of PC-vesicles. E.G. retinoids clearly favour the PC-vesicle membrane. Apparently, rod outer segment membranes have a much lower affinity for retinoids than other artificial or natural membranes investigated so far.

Animals↗
PubMed1984

Squid m-retinochrome. Two forms of metaretinochrome.

When retinochrome absorbs light, it bleaches to m-retinochrome, which may act as a direct supplier of 11-cis-retinal to protein opsin to form rhodopsin. The present experiments were aimed at further elucidating the molecular state of m-retinochrome. Retinochrome and m-retinochome were mixed each with sodium borohydride, subjected to sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and the resultant fluorescence bands were examined. The reduced retinochrome showed only one band due to N-retinyl protein, whereas the reduced m-retinochrome had two bands. When extracted with successive volumes of n-hexane, m-retinochrome released the 11-cis-retinal chromophore in a time-course consisting of fast and slow phases. These findings indicated that m-retinochrome exists in two forms, with loose and tight coupling of the chromophore to the protein moiety. Those forms were usually balanced in a molar ratio of about 1:2, and the proportion of the tight form of m-retinochrome was increased in the presence of excess 11-cis-retinal. Based upon these findings, the role of m-retinochrome in the visual cells is discussed.

Animals↗
PubMed1985

Properties of the visual pigments of the moth Manduca sexta and the effects of two detergents, digitonin and chaps.

The three known visual pigments (P520, P450, P357) of the moth, Manduca sexta (Lepidoptera, Sphingidae), were extracted in two different detergents (2% digitonin, 6 or 12 mM CHAPS). As is the case in unextracted membranes, the metarhodopsins are quite stable in CHAPS extracts, while in digitonin the metarhodopsins of P520 and P450 decay rapidly at 15 degrees C to opsin and free retinal. The relative absorbance ratios are: 1.0:1.6 (P520:M485), 1.0:1.1 (P450:M485), and 1.0:0.8 (P357:M470). The relative amounts of the visual pigments found in digitonin extracts is 100:25:8 (P520:P450:P357); about 60 picomoles of P520 can be extracted from one Manduca retina.

Animals↗
PubMed1985

Competition between retinal and 3-dehydroretinal for opsin in the regeneration of visual pigment.

Rhodopsin regenerated faster than porphyropsin in all preparations of bullfrog opsin, bullfrog rod outer segment membrane and cattle opsin. When opsin was incubated with excess amount of an equimolar mixture of 11-cis-retinal and 11-cis-3-dehydroretinal, the composition of the regenerated pigment was simply dependent on the ratio of regeneration rates of rhodopsin and porphyropsin. This result can provide a mechanism to account for the discrepancy in vitamin A1/A2 composition between the retina and the pigment epithelium. The property of opsin preferring retinal to 3-dehydroretinal may be one of the basic factors affecting vitamin A1/A2 visual pigment systems.

Animals↗
PubMed1985

Larval and adult visual pigments of the zebrafish, Brachydanio rerio.

Photoreceptors of adult and larval zebrafish were assayed by microspectrophotometry to characterize their visual pigments, and to determine when the visual pigments first appear during development. Short single cone outer segments contained a pigment with a lambdamax near 417 nm. Long single cones and long members of double cone outer segments contained a pigment with a lambdamax near 480 nm. Short members of double cone outer segments contained a pigment with a lambdamax near 556 nm. Rod outer segments contained a rhodopsin with a lambdamax near 501 nm. All four visual pigment types found in adult photoreceptors were present in the earliest measurable larval photoreceptors.

Aging↗
PubMed1985

A photoproduct with 13-cis retinal generated by irradiation with violet light in the octopus retina.

The photoconversion between rhodopsin (R) and metarhodopsin (MR) was investigated in the retina of Octopus ocellatus by measurements of the fast photovoltage (FPV) in conjunction with high pressure liquid chromatography (HPLC). Following conversion of most of R to MR by short-term exposure to an intense violet light, a large vitreous negative FPV due to photon absorption by MR was observed with an orange test flash. By continuing the exposure to the same violet light, however, the negative FPV became very small, though long-term irradiation with blue-green light produced a recovery. With the violet light exposure a substance other than R and MR is produced, which hardly contributes to FPV generation. Analysis of retinal isomers with HPLC show that such an exposure produces a substance with 13-cis retinal as its chromophore and that it was significantly reduced after exposure to blue-green light.

Animals↗
PubMed1986

A fly, Drosophila melanogaster, forms 11-cis 3-hydroxyretinal in the dark.

All-trans and 11-cis 3-hydroxyretinals were synthesized and the presence of these substances in the head of Drosophila melanogaster was shown by using high performance liquid chromatography. Even when the head extract was prepared in the dark from the flies reared successively in the dark, both of the 3-hydroxyretinal isomers were detected. In the culture medium, they were not present. D. melanogaster must have an 11-cis 3-hydroxyretinal forming-system that does not need light.

Animals↗
PubMed1986

Separation and identification of geometric isomers of 3-hydroxyretinoids and occurrence in the eyes of insects.

The 9-cis, 11-cis, 13-cis and all-trans isomers of 3-hydroxyretinal oxime, and the 11-cis, 13-cis and all-trans isomers of 3-hydroxyretinol have been resolved by high pressure liquid chromatography (HPLC) and identified by their spectral properties. The antimony chloride reaction product of 3-hydroxyretinol is spectrally indistinguishable from that of retinol. Heads of insects from 8 genera of Diptera and Lepidoptera were found to contain 3-hydroxyretinoids. The most abundant isomers of 3-hydroxyretinal are 11-cis and all-trans.

Animals↗
PubMed1986

A simple procedure for the extraction of the native chromophore of visual pigments: the formaldehyde method.

The chromophore of visual pigments was efficiently extracted in its original isomeric conformation by dichloromethane/hexane in the presence of excess formaldehyde. This new method of extraction (the formaldehyde method) in combination with HPLC is useful for the determination of the chromophore composition of visual pigments. The chromophore isolated by this method is biologically active and can be used for regeneration experiments.

Animals↗
PubMed1987

Isolation and characterization of a retinal-binding protein from the squid retina.

A retinal-binding protein (RALBP) was isolated from the squid retina, and purified by anion-exchange and size-exclusion chromatography. The molecular weight was determined to be 51,000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and by gel filtration. The purified sample showed absorption maxima at about 330 and 400 nm in addition to a protein band, indicating the occurrence of retinol and retinal, respectively. The relative heights of these two peaks varied from preparation to preparation, depending on retinoid ligands. Irradiation of RALBP caused no marked change in absorption, but the amount of 11-cis-retinal decreased to form a photosteady state mixture with all-trans- and 13-cis-retinals. RALBP was fairly stable even in the presence of hydroxylamine (100 mM), but was affected by sodium borohydride (30 mM) or borane dimethylamine (400 mM), with the retinal reduced to retinol. When incubated with metaretinochrome-carrying membranes in the dark, RALBP specifically took up 11-cis-retinal and lost all-trans-retinol. Upon further incubation of this RALBP with opsin-containing membranes, rhodopsin was progressively formed in the dark. Squid RALBP may act as a shuttle in transferring the 11-cis-retinal from metaretinochrome to opsin in the visual cells.

Animals↗