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PubMed1992

Retinol forms retinoic acid via retinal.

Hepatic cytosol from normal deermice having cytosolic alcohol dehydrogenase (ADH+) also displays retinol dehydrogenase activity and converts retinol to retinoic acid, whereas cytosol from ADH- deermice lacks these enzyme activities and does not produce retinoic acid. Furthermore, microsomes from either strain do not convert retinol to retinoic acid. However, when cytosol from ADH- animals is added to the microsomes, retinoic acid is produced. The obligatory role of retinal as an intermediary step in retinoic acid formation is further shown by isotopic dilution of retinoic acid formed from labeled retinol upon addition of unlabeled retinal. Microsomal retinol dehydrogenase also catalyzes the reduction of retinal to retinol, thereby explaining the decrease in retinoic acid production from retinol in liver cytosol of ADH+ deermice when microsomes are added. Thus, the results of this study indicate that retinal is an obligatory intermediate in the hepatic production of retinoic acid from retinol and that cytosolic and microsomal retinol dehydrogenases play a key role in this process.

Alcohol Dehydrogenase↗
PubMed1994

Effects of the intermediate retinoid metabolite retinal on the pattern of the dental lamina in vitro.

Retinoids have important roles in pattern formation during embryonic development and might act as endogenous morphogens. They are necessary for normal odontogenesis and excess retinol alters the pattern of odontogenesis producing supernumerary buds of the dental lamina in the diastema region of the mouse mandible. Because the metabolism of retinoids in the developing mandible is unknown, the effects of retinal (an intermediate metabolite in the local conversion of retinol to retinoic acid) on the patterning of odontogenesis were examined. Retinal produces supernumerary buds and enhanced epithelial proliferation in day-9 mandibles in vitro. The endogenous levels of retinal in the mandible at the time of initiation of odontogenesis were also measured by high-performance liquid chromatography. Retinal was detected only at day 10 and not at later stages of development. Local metabolism of this intermediate retinoid may be a rate-determining step in the production of active retinoid metabolites that may control the pattern of the dentition, which is established at the time of the appearance of the dental lamina at embryonic day 12.

Animals↗
PubMed1977

Effect of light-adaptation on the photoreaction of bacteriorhodopsin from Halobacterium halobium.

Light-induced formation of the 410 nm intermediate was investigated on dark-and light-adapted bacteriorhodopsin. The amplitude of the light-induced absorption increase at 410 nm of the light-adapted bacteriorhodopsin was twice as large as that of the dark-adapted bacteriorhodopsin. The amount of protons released from bacteriorhodopsin in response to illumination was also enhanced by light-adaptation. The degree of the enhancement was independent of the temperature in the dark-adaptation. The relation between these photochemical events and the isomeric configurations of retinal is discussed.

Adaptation, Physiological↗
PubMed1978

Kinetic study of photoregeneration process of digitonin-solubilized squid rhodopsin.

In the photoregeneration process of squid rhodopsin, an intermediate has been found at neutral pH values (phosphate buffer) with a flash light (lambda greater than 540 nm). An intermediate R430, with the 11-cis retinal as chromophore, is produced from metarhodopsin in light and is converted to rhodopsin through the processes R430 leads to P380 and P380 leads to rhodopsin. The pH dependence of the velocity of the conversions suggests that processes R430 leads to P380 and P380 leads to rhodopsin involve a protolytic reaction and that the ionized group is a histidine residue of opsin. Kinetic parameters show that the largest conformational change in opsin occurs in the conversion of R430 leads to P380.

Animals↗
PubMed1980

Resonance Raman spectroscopy of chemically modified and isotopically labelled purple membranes. I. A critical examination of the carbon-nitrogen vibrational modes.

Resonance Raman spectra of bacteriorhodopsin are compared to the spectra of this protein modified in the following ways: (1) selective deuteration at the C-15 carbon atom of retinal, (2) full deuteration of the retinal, (3) the addition of a conjugated double bond in the beta-ionone ring (3-dehydroretinal), (4) full deuteration of the protein and lipid components, (5) 15N enrichment of the entire membrane and (6) deuteration of the entire membrane (including the retinal). A detailed comparison of the 15N-enriched membrane and naturally occurring purple membrane from 800 cm-1 to 1700 cm-1 reveals that 15N enrichment affects the frequency of only two vibrational modes. These occur at 1642 cm-1 and 1620 cm-1 in naturally occurring purple membrane and at 1628 cm-1 and 1615 cm-1 in the 15N-enriched samples. Therefore, this pair of bands reflects the states of protonation of the Schiff base. However, our data also indicate that neither of these modes are simple, localized C=N-H or C=N stretching vibrations. In the case of the 1642 cm-1 band motions of the retinal chain beyond C-15 are not significantly involved. On the other hand, in the 1620 cm-1 band atomic motions in the isoprenoid chain beyond C-15 are involved.

Bacteriorhodopsins↗
PubMed1981

Specific photoisomerization of retinal in squid rhodopsin and metarhodopsin.

The composition of retinal isomers in the photosteady-state mixtures formed from squid rhodopsin and metarhodopsin was determined by high-pressure liquid chromatography. A large amount of 9-cis-retinal was obtained at liquid N2 temperature when rhodopsin was irradiated with orange light, but only small quantities of 9-cis-retinal were obtained at 15 degrees C. Scarcely any 9-cis-retinal was produced from metarhodopsin by irradiation at liquid N2 temperature. A large quantity of 7-cis-retinal was found in the photoproduct of rhodopsin irradiated at solid carbon dioxide temperature, but not at 15 degrees C and liquid N2 temperature. 7-cis-Retinal was not produced from metarhodopsin at any temperatures. These results indicate that the photoisomerization of retinal is regulated by the structure of the retinal-binding site of this protein. The formation of 9-cis- and 7-cis-retinals is forbidden in the metarhodopsin protein.

Animals↗
PubMed1976

Oxidative damage of retinal rod outer segment membranes and the role of vitamin E.

Highly purified bovine rod outer segment membranes show loss of structural integrity under an air atmosphere. Obvious ultrastructural changes are preceded by increases in absorbance below 400 nm. These changes are inhibited by Ar or N2 atmospheres and appear to be due primarily to oxidative damage to the polyunsaturated fatty acids of the membrane lipids. Loss of polyunsaturated fatty acids, formation of malonaldehyde and fluorescent products characteristic of lipid oxidation accompany the spectral alterations. The elevated ultraviolet absorbance can largely be removed from the membranes by gentle extraction of the lipids using phospholipase C and hexane without changing the visible absorbance of rhodopsin. We have found a large seasonal variation in the endogenous level of alpha-tocopherol (vitamin E) in the bovine rod outer segment preparations. For much of the year we find that the rod outer segment membranes contain higher levels of alpha-tocopherol than have been previously reported in biological membranes. Rod outer segments which are low in endogenous tocopherol can be protected from oxygen damage by adding exogenous tocopherol. The rod outer segments are extremely susceptible to oxygen damage due to the unusually high content of polyunsaturated fatty acids in the membrane lipids. The presence of tocopherol inhibits oxygen damage but does not eliminate it. The tocopherol in the rod outer segments is consumed in air, thus complete protection from peroxidation in vitro requires an inert atmosphere as well as high levels of tocopherol. This work suggests that extensive precautions against oxidative degradation should also be employed in studies of other membrane systems where important deleterious effects of oxygen may be less obvious.

Animals↗
PubMed1979

Biochemical aspects of the visual process. XL. Spectral and chemical analysis of metarhodopsin III in photoreceptor membrane suspensions.

The late photointermediates of rhodopsin photolysis have been analyzed spectrally and chemically in bovine rod outer segment membrane suspension at 25 degrees C and pH 6.5. The decay of metarhodopsin II follows two spectrally distinct routes, resulting 40 min after illumination in a stable mixture of photo-products with absorbance maxima around 380 and 452 nm, free retinal and metarhodopsin III, respectively. Chemical analysis shows that three different products are involved: free retinal (approx. 34%), protein-bound retinal (approx. 51%) and lipid-bound retinal (approx. 15%). The latter fraction consists of retinylidene-phosphatidylethanolamine exclusively. Photolysis of membranes reconstituted with various phospholipids gives a qualitatively normal spectral picture, but the production of metarhodopsin III may vary with the phospholipid composition, i.e. with the percent of phosphatidylethanolamine present. Chemical analysis shows that with increasing phosphaatidylethanolamine content of the membrane, the retinylidene phosphatidylethanolamine fraction increases proportionally at the expense of free retinal, while the fraction of protein-bound retinal remains unaffected. The results indicate that under these conditions metarhodopsin III (defined as a long wavelength product of metarhodopsin II decay) is composed of two chemically distinct components: opsin-bound retinal and retinylidene phosphatidylethanolamine.

Animals↗
PubMed1979

A possible role of rhodopsin in maintaining bilayer structure in the photoreceptor membrane.

31P-NMR measurements demonstrate that at 37 degrees C, independent of the photolytic state of the photopigment rhodopsin, the lipids in the photo-receptormembrane are almost exclusively organised in a bilayer. In strong contrast, the 31P-NMR spectra of the extracted lipids are characteristic for the hexagonal HII phase and an isotropic phase. The isotropic phase is characterised by freeze-fracture electron microscopy as particles and pits on smooth surfaces, possibly indicating inverted micelles. These results suggest a structural role for rhodopsin in maintaining the photoreceptor membrane lipids in a bilayer configuration.

Animals↗
PubMed1983

Interactions in mixed monolayers between distearoyl-L-phosphatidylethanolamine, rod outer segment phosphatidylethanolamine and all-trans retinal. Effect of pH.

The interactions in mixed monolayers between distearoyl-L-phosphatidylethanolamine, natural phosphatidylethanolamine purified from bovine rod outer segments and all-trans retinal have been studied at the nitrogen/water interface at 21.0 +/- 0.5 degrees C. Seven mixtures of each phospholipid with all-trans retinal, covering the whole range of molar fractions, were studied. The monolayers were spread on a 1 X 10(-3) M phosphate buffer subphase at three different pH values, 5.5, 7.1 and 8.2. The results for the two series of mixtures are strikingly different. The surface phase rule shows that all-trans retinal is miscible with the natural phospholipid at the interface. Small, negative deviations with respect to the additivity rule are observed in this case. The excess free energies of mixing were also calculated as a function of concentration for this system at four different surface pressures, 5, 7, 10 and 13 mN X m-1. They are negative for the four surface pressures considered and symmetrical with respect to the mole fraction. On the other hand, when distearoyl-L-phosphatidylethanolamine is mixed with all-trans retinal, the components are no longer miscible at the interface. This marked difference in behaviour between the two lipids reflects the importance of hydrophobic interactions in the mixed monolayers of phospholipids with retinals. Furthermore, for the two series of mixtures, the surface pressure isotherms do not show any significant shift when the subphase pH is changed from 5.5 to 8.2. This behaviour raises questions about the formation of a Schiff base between phosphatidylethanolamine and retinal at the interface. It is suggested that, owing to the nature of the disk membranes, such an effect would also be observed in vivo. The possible implications of this are discussed, particularly with respect to questions pertaining to the stability of the retinal chromophore.

Animals↗
PubMed1985

Volatile anesthetics cause conformational changes of bacteriorhodopsin in purple membrane.

We examined the effects of volatile anesthetics on the structure of the bacteriorhodopsin in the purple membrane by measurements of the absorption spectrum and the visible circular dichroism (CD) spectrum and assay of the retinal composition. As the concentrations of halothane, enflurane and methoxyflurane were increased, the absorption at 560 nm decreased but that at 480 nm increased with an isosbestic point around 510 nm. These anesthetic-induced spectroscopic changes were reversible. The CD spectrum showed the biphasic pattern with a positive and a negative band. As the concentration of halothane was increased from 4 mM to 8mM, the negative band reversibly diminished more drastically than the positive band, and at 8 mM of halothane the positive band shifted to around 480 nm. These results show that halothane disturbed the exciton coupling among bacteriorhodopsin molecules. The retinal isomer composition was analyzed using high performance liquid chromatography. The ratio of 13-cis- to all-trans-retinal was 47:53, 34:66 and 19:81 at control, 7.4 mM and 14.9 mM enflurane, respectively. After elimination of enflurane, the ratio returned to the control value. These findings indicate that volatile anesthetic directly affect a bacteriorhodopsin in the purple membrane and induce conformational changes in it.

Anesthetics↗
PubMed1986

The effect of retinoids on the activity of the membrane form of galactosyltransferase, studied in an enzyme/liposome model system.

In the present study the effect of retinoids on the membrane form of galactosyltransferase was tested. A model system consisting of pure bovine milk galactosyltransferase and phosphatidylserine vesicles was used for this investigation. Retinol, retinal and retinylphosphate were able to overcome the modulating effect of phosphatidylserine, that is, activated the enzyme. Retinoic acid and retinylpalmitate were ineffective in this system.

Animals↗
PubMed1988

Electron spin resonance study of the interactions of retinoids with a phospholipid model membrane.

The effects of up to 20 mol% incorporation of all-trans-retinol (vitamin A), retinal (vitamin A aldehyde) and retinoic acid (vitamin A acid) on acyl chain order and dynamics in liquid crystalline dipalmitoylphosphatidylcholine membranes at pH 7.5 were studied by electron spin resonance (ESR) of 5-, 7-, 10-, 12- and 16-doxyl spin-labelled stearic acids intercalated into the membrane. Order parameters S and correlation times tau c determined from the ESR spectra demonstrate that the influence of retinoic acid differs from retinol or retinal. Whereas the latter two retinoids have negligible effect (less than 1%) on acyl chain order towards the membrane surface (5 position), retinoic acid reduces the order parameter by as much as 8% at 20 mol% incorporation. All three retinoids restrict acyl chain motion to a similar extent approaching the center of membrane (10, 12 and 16 positions), where up to 22% increases in order parameter and correlation time were observed. Complementary osmotic swelling and carboxyfluorescein release measurements show that the enhancement in permeability of egg phosphatidylcholine membranes to erythritol and carboxyfluorescein is greater with all-trans-retinoic acid than all-trans-retinol or retinal.

1,2-Dipalmitoylphosphatidylcholine↗
PubMed1991

Protein-chromophore interactions in bacteriorhodopsin: the effects of a change in surface potential.

The chromophore retinal is bound to bacteriorhodopsin via a protonated Schiff base linkage. The retinal binding site is reported to be buried in the transmembrane portion of the protein, distant from the membrane surfaces. When bound to bacteriorhodopsin, the absorption maximum of retinal is red-shifted from 366 nm to 568 nm producing a purple color. This color persists across a wide pH range. However, when the pH is raised above 12.0, the membranes become pink in color, while at pH values of 3.0 or below, a blue color is produced. The blue color can also be obtained by removing the divalent cations bound to the surface of the protein. In this study, bacteriorhodopsin was examined by circular dichroism and absorption spectroscopy to determine if protein conformational changes were associated with the color shifts. It was found that although the retinal chromophore can be completely removed by bleaching with hydroxylamine with no significant influence on the secondary structure of the protein, a change in the surface charge of bacteriorhodopsin results in measurable conformational change in the protein, which apparently affects the nature of the retinal binding site.

Bacteriorhodopsins↗
PubMed1992

Retinal and retinol promote membrane fusion.

Disk membranes from the bovine retinal rod outer segments (ROS) were found to fuse with vesicles made of lipids extracted from unbleached ROS disk membranes, using a lipid mixing assay for membrane fusion (relief of self-quenching of R18, octadecylrhodamine B chloride). If the retinal chromophore of rhodopsin was reductively linked to opsin before lipid extraction, the vesicles made of the extracted lipids were not suitable targets for fusion of the disk membranes. The addition of retinal and retinol to these vesicles restored their ability to fuse. Therefore, the presence of all-trans retinal was implicated in promoting membrane fusion in this system. To test this possibility, the ability of retinal and retinol to influence the phase behavior and the fusion capability of large unilamellar vesicles (LUV) of N-methyl dioleoylphosphatidylethanolamine (N-methyl-DOPE) was examined. Both retinal and retinol stimulated the fusion of vesicles of N-methyl-DOPE (contents mixing with ANTS, 1-aminonaphthalene-3,6,8-trisulfonic acid; DPX, p-xylylene bis(pyridinium bromide)). Both compounds reduced the onset temperature for isotropic resonances in the 31P-NMR spectra of N-methyl-DOPE dispersions and the onset temperature, TH, for formation of hexagonal II phase. These results were consistent with previous studies in which the onset temperature for the 31P-NMR isotropic resonances were correlated with stimulation of membrane fusion. These data suggested that both retinal and retinol may stimulate membrane fusion by destabilizing the bilayers of membranes.

Animals↗
PubMed1976

Studies on the metabolism of beta-carotene and apo-beta-carotenoids in rats and chickens.

(1)The relative abilities of the various fractions of rat and chicken liver to oxidize and reduce retinal and 8'-and 12'-apo-beta-carotenal were investigatjed and it has been shown that, while retinal is exclusely oxidized by the soluble fraction, the apocarotenals are mostly oxidized by the particulate fractions of the homogenate. (2) Addition of NAD+ or NADP+ markedly activated the oxidation of the apocarotenals, but not of retinal by the particulate fractions. (3) Considerable amounts of retinal and 8'-, 10'- and 12'-apo-beta-carotenal were isolated from the intestine of chickens fed beta-carotene and these apocarotenoids were conclusively identified. (4) Significant amounts of 8'-, 10'- and 12'-apo-beta-carotenoic acids were isolated from the intestine of rats given 8'-apo-beta-carotenal and these apocarotenoic acids were also conclusively identified. (5) In the light of these observations it is suggested that during conversion to vitamin A, the beta-carotene molecule is simultaneously attacked by the dioxygenase at several double bonds, the primary attack being at the central double bond and a tentative scheme for the mechanism of conversion is proposed.

Animals↗
PubMed1980

Quantitative determination of retinals with complete retention of their geometric configuration.

A method is described for the quantitative extraction of retinal in its original isomeric configuration from retinal-containing pigments. Using excess of hydroxylamine under denaturing conditions, the chromophore of retinal bearing natural products is converted into the corresponding retinaloxime with complete retention of geometric configuration. The retinaloximes can be quantitatively extracted with dichloromethane and analyzed by high-performance liquid chromatography.

Animals↗