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PubMedDate not supplied

9-cis Retinal increased in retina of RPE65 knockout mice with decrease in coat pigmentation.

The protein RPE65 is essential for the generation of the native chromophore, 11-cis retinal, of visual pigments. However, the Rpe65 knockout (Rpe65-/-) mouse shows a minimal visual response due to the presence of a pigment, isorhodopsin, formed with 9-cis retinal. Isorhodopsin accumulates linearly with prolonged dark-rearing of the animals. The majority of Rpe65-/- mice have an agouti coat color. A tan coat color subset of Rpe65-/- mice was found to have an enhanced visual response as measured by electroretinograms. The enhanced response was found to be due to increased levels of 9-cis retinal and isorhodopsin pigment levels. Animals of both coat colors reared in cyclic light have minimal levels of regenerated pigment and show photoreceptor degeneration. On dark-rearing, pigment accumulates and photoreceptor degeneration is decreased. In the tan Rpe65-/- mice, the level of photoreceptor degeneration is less than in the agouti animals, which have an increased pigment and decreased free opsin level. Therefore, photoreceptor damage correlates with the amount of the apoprotein present, supporting findings that the activity from unregenerated opsin can lead to photoreceptor degeneration.

Animals↗
PubMedDate not supplied

Photoisomerization in proteorhodopsin mutant D97N.

The first steps of the photocycle of the D97N mutant of proteorhodopsin (PR) have been investigated by means of ultrafast transient absorption spectroscopy. A comparison with the primary dynamics of native PR and D85N mutant of bacteriorhodopsin is given. Upon photoexcitation of the covalently bound all-trans retinal the excited state decays biexponentially with time constants of 1.4 and 20 ps via a conical intersection, resulting in a 13-cis isomerized retinal. Neither of the two-deactivation channels is significantly preferred. The dynamics is slowed down in comparison with native PR at pH 9 and reaction rates are even lower than for native PR at pH 6, where the primary proton acceptor (Asp97) is protonated. Therefore, the ultrafast isomerization is not only controlled by the charge distribution within the retinal binding pocket. This study shows that in addition to direct electrostatics other effects have to be taken into account to explain the catalytic function of Asp97 in PR on the ultrafast isomerization reaction. This may include sterical interactions and/or bound water molecules within the retinal binding pocket.

Bacterial Proteins↗
PubMedDate not supplied

Tryptophan 171 in Pharaonis phoborhodopsin (sensory rhodopsin II) interacts with the chromophore retinal and its substitution with alanine or threonine slowed down the decay of M- and O-intermediate.

Pharaonis phoborhodopsin (ppR), also called pharaonis sensory rhodopsin II, NpSRII, is a photoreceptor for the photophobic response of Natronomonas pharaonis. Tryptophan 182 (W182) of bacteriorhodopsin (bR) is near the chromophore retinal and has been suggested to interact with retinal during the photoreaction and also to be involved in the hydrogen-bonding network around the retinal. W182 of bR is conserved in ppR as tryptophan 171 (W171). To elucidate whether W171 of ppR interacts with retinal during the photoreaction and/or is involved in the hydrogen-bonding network as in bR, we formed W171-substituted mutants of ppR, W171A and W171T. Our low-temperature spectroscopic study has revealed that the substitution of W171 to Ala or Thr resulted in the stabilization of M- and O-intermediates. The stability of M and absorption spectral changes during the M-decay were different depending on the substituted residue. These findings suggest that W171 in ppR interacts with retinal and the degree of the interaction depends on the substituted residues, which might be rate determining in the M-decay. In addition, the involvement of W171 in the hydrogen-bonding network is suggested by the O-decay. We also found that glycerol slowed the decay of M and not of O.

Amino Acid Substitution↗
PubMedDate not supplied

Pressure-induced isomerization of retinal on bacteriorhodopsin as disclosed by fast magic angle spinning NMR.

Bacteriorhodopsin (bR) is a retinal protein in purple membrane of Halobacterium salinarum, which functions as a light-driven proton pump. We have detected pressure-induced isomerization of retinal in bR by analyzing 15N cross polarization-magic angle spinning (CP-MAS) NMR spectra of [zeta-15N]Lys-labeled bR. In the 15N-NMR spectra, both all-trans and 13-cis retinal configurations have been observed in the Lys N(zeta) in protonated Schiff base at 148.0 and 155.0 ppm, respectively, at the MAS frequency of 4 kHz in the dark. When the MAS frequency was increased up to 12 kHz corresponding to the sample pressure of 63 bar, the 15N-NMR signals of [zeta-15N]Lys in Schiff base of retinal were broadened. On the other hand, other [zeta-15N]Lys did not show broadening. Subsequently, the increased signal intensity of [zeta-15N]Lys in Schiff base of 13-cis retinal at 155.0 ppm was observed when the MAS frequency was decreased from 12 to 4 kHz. These results showed that the equilibrium constant of [all-trans-bR]/[13-cis-bR] in retinal decreased by the pressure of 63 bar. It was also revealed that the structural changes induced by the pressure occurred in the vicinity of retinal. Therefore, microscopically, hydrogen-bond network around retinal would be disrupted or distorted by a constantly applied pressure. It is, therefore, clearly demonstrated that increased pressure induced by fast MAS frequencies generated isomerization of retinal from all-trans to 13-cis state in the membrane protein bR.

Bacteriorhodopsins↗
PubMedDate not supplied

Sub-5-fs real-time spectroscopy of transition states in bacteriorhodopsin during retinal isomerization.

By using a sub-5-fs visible laser pulse, we have made the first observation of the vibrational spectra of the transition state during trans-cis isomerization in the retinal chromophore of bacteriorhodopsin (bR(S68). No instant isomerization of the retinal occurs in spite of electron promotion from the bonding pi-orbital to the anti-bonding pi*-orbital. The difference between the in-plane and out-of-plane vibrational frequencies (about 1150-1250 and 900-1000 cm(-1), respectively) is reduced during the first time period. The vibrational spectra after this period became very broad and weak and are ascribed to a "silent state." The silent state lasts for 700-900 fs until the chromophore isomerizes to the cis-C13 = C14 conformation. The frequency of the C = C stretching mode was modulated by the torsion mode of the C13 = C14 double bond with a period of 200 fs. The modulation was clearly observed for four to five periods. Using the empirical equation for the relation between bond length and stretching frequency, we determined the transitional C = C bond length with about 0.01 angstroms accuracy during the torsion motion around the double bond with 1-fs time resolution.

Bacteriorhodopsins↗
PubMed1997

Evidence of alpha-helix slidings during bacteriorhodopsin photocycle-energetics coupling.

The three-dimensional structure of bacteriorhodopsin indicates that the all-trans-cis retinal bending causes alpha-helix slidings during the bacteriorhodopsin photocycle. For the elucidation of alpha-helix slidings taking place during the bacteriorhodopsin photocycle, we calculated ASAs of hydrophobic and hydrophilic atoms translocated by alpha-helix slidings with thermodynamic criteria found previously. Thermodynamic parameters calculated from ASAs (calculated delta Gtransfer and T delta S) were consistent with those (observed delta Gtransfer and T delta S) obtained empirically. These findings indicate that alpha-helix slidings take place during bacteriorhodopsin photocycle-energetics coupling. These mechanisms not only explain various phenomena, including some mutants forming a long-lived intermediate, but also predict various yet-unobserved phenomena, including the generation of heat in early photocycle intermediates.

Amino Acid Sequence↗
PubMed1989

Heterogeneity of responses to LH-releasing hormone and phorbol ester among rat gonadotrophs: a study using a reverse haemolytic plaque assay for LH.

Protein kinase C (PK-C) has been implicated in the action of LHRH because LHRH-induced release of LH is partially mimicked by phorbol esters which activate PK-C, and reduced in magnitude by inhibitors of PK-C. We have used a reverse haemolytic plaque assay for LH to visualize and compare the direct effects on individual rat gonadotrophs of (1) a 2-h exposure to a range of concentrations of LHRH and phorbol 12-myristate 13-acetate (PMA) and (2) a single maximally stimulatory dose (10 nM) of LHRH or PMA, or LHRH in the presence of inhibitors of PK-C (retinal and isoquinolone sulphonamide; H7) over six consecutive 30-min intervals. Quantitative analysis of the size and number of haemolytic plaques indicated that LHRH induced a dose- and time-dependent increase in the amount of LH release by individual gonadotrophs, with no evidence of the priming effect of LHRH. Stimulation by 10nM LHRH induced recruitment of actively secreting gonadotrophs which reached maximum levels by 90 min. There was a delay of 90-120 min before 10 nM PMA caused a significant release of LH, as assessed by both the size and number of plaques. During the first 30 min of exposure, the presence of 10 microM retinal or H7 augmented LHRH-induced secretion of LH, with the absence of any inhibition of the effects of LHRH until 90-120 min, when both the size and number of plaques were reduced compared with those formed in the presence of LHRH alone.(ABSTRACT TRUNCATED AT 250 WORDS)

1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine↗
PubMed1990

Rhodopsin expressed in Chinese hamster ovary cells regulates adenylyl cyclase activity.

The cDNA encoding bovine opsin was transfected into Chinese hamster ovary (CHO) cells to generate stable clones expressing the rod cell photoreceptor protein. Cells expressing opsin, when incubated in 11-cis retinal and exposed to light, inhibited forskolin-stimulated adenylyl cyclase activity. Rhodopsin-mediated inhibition of adenylyl cyclase was prevented by treatment of cells with pertussis toxin. In the same cells, thrombin stimulated phosphatidylinositol hydrolysis through G protein-mediated pathways, but rhodopsin neither significantly influenced the action of thrombin nor stimulated phosphatidylinositol hydrolysis. Our findings indicate that rhodopsin selectively regulates a Gi protein in intact CHO cells that is coupled to adenylyl cyclase but not to phospholipase C.

Adenylate Cyclase Toxin↗
PubMed2004

A purified agonist-activated G-protein coupled receptor: truncated octopus Acid Metarhodopsin.

G-protein coupled receptors (GPCRs) mediate responses to many types of extracellular signals. So far, bovine rhodopsin, the inactive form of a GPCR, is the only member of the family whose three dimensional structure has been determined. It would be desirable to determine the structure of the active form of a GPCR. In this paper, we report the large scale preparation of a stable, homogenous species, truncated octopus rhodopsin (t-rhodopsin) in which proteolysis has removed the proline-rich C-terminal; this species retains the spectral properties and the ability for light-induced G-protein activation of unproteolyzed octopus rhodopsin. Moreover, starting from this species we can prepare a pure, active form of pigment, octopus t-Acid Metarhodopsin which has an all-trans-retinal as its agonist. Photoisomerization of t-Acid Metarhodopsin leads back to the inactive form, t-rhodopsin with the inverse agonist 11-cis-retinal. Octopus t-Acid Metarhodopsin can activate an endogenous octopus G-protein in the dark and this activity is reduced by irradiation with orange light which photoregenerates t-Acid Metarhodopsin back to the initial species, t-rhodopsin.

Animals↗
PubMed1996

High-level inducible expression of visual pigments in transfected cells.

A method for high-level expression of a functionally active, recombinant human red cone opsin was developed by adding the coding sequence for the C-terminal epitope of bovine rhodopsin onto the C terminus of the cone opsin and cloning the resulting construct into the vector pMEP4 beta. The recombinant pMEP4 beta vector was transfected stably into 293-EBNA cells, and expression of the cone opsin was induced by the addition of CdCl2 into the medium. The recombinant cone opsin was reconstituted with 11-cis retinal and purified by immunoaffinity chromatography. Spectral analysis prior to and following photobleaching confirmed its identity as a red cone opsin. The protein was targeted to the cell membrane and activated bovine transducin.

Animals↗
PubMed2001

Nucleotide and deduced amino acid sequence of equine retinal and pineal gland phosducin.

OBJECTIVES: To determine the full-length complementary DNA (cDNA) sequence of equine retinal and pineal gland phosducin (PHD) and to clone these sequences. SAMPLE POPULATION: Samples of equine retinal RNA. PROCEDURE: A primer set was designed for use in identifying a fragment of the equine PHD nucleotide sequence, derived from retinal RNA samples, and subsequently for use to deduce specific primers for additional examination. The full-length cDNA was determined by the method of rapid amplification of cDNA ends (RACE). For full-length cDNA, newly designed primers were used. Nucleotide sequences were analyzed by use of computer software. The deduced amino acid sequence was compared with sequences of PHD reported for other species. In addition, the sequence of equine pineal PHD was cloned. RESULTS: The cDNA nucleotide sequence for equine PHD was 1,209 base pairs (bp) in length with an open-reading frame encoding a protein of 245 amino acids and a calculated molecular mass of 28.214 kd. Similarity with amino acid sequences of PHD from other species was 89 to 93%. Sequences of equine PHD from retina and pineal gland were identical. Equine PHD contained a peptide sequence with 100% homology to an uveitopathogenic peptide reported for rat PHD. CONCLUSIONS: Equine PHD is a highly conserved protein that has homology of immunologic interest with rat PHD. These results establish a basis for studying the role of PHD in ocular inflammation of horses.

Amino Acid Sequence↗
PubMedDate not supplied

Influence of membrane components on the stability and drug release properties of reverse phase evaporation vesicles (REVs): light sensitive all-trans retinal, negatively charged phospholipid dicetylphosphate and cholesterol.

Incorporation of a negatively charged phospholipid, dicetylphosphate, initially increased encapsulation efficiency (from 12 to 24%) but beyond 5% (molar) a detrimental effect was observed. Rate of drug release from REVs was, for most cases, found to be bi-phasic implying partitioning between the lipid bilayer and the aqueous compartment. It was not possible to prepare liposomes with more than 1% (molar) all-trans retinal (ATR) as a membrane component. When ATR was reduced to 0.5% (molar), encapsulation efficiency increased to 7.76%. Upon exposure to long wave UV (365 nm), release from ATR containing REVs was increased and this was attributed to the formation of 13-cis isomer as indicated by HPLC and UV spectroscopy data.

Chemistry, Pharmaceutical↗
PubMed1990

Survival of structure and function in postmortem rat and human retinas: rhodopsin regeneration, cGMP and the ERG.

Procedures for regenerating visual pigment and restoring phototransduction have been established with freshly isolated, bleached rat retinas. Phosphatidyl choline liposomes containing a 500 microM mixture of retinal isomers, including the 9-cis and 11-cis forms, were employed and the results compared with dark-adapted retinas, incubated similarly but without retinal. The following were recovered in a 60 min incubation, rhodopsin (plus isorhodopsin) to 91% of the original rhodopsin concentration, 87% of cGMP and 89% of PIII amplitude at saturation. PIII amplitude vs. log intensity curves gave values of n between 0.6 and 1/2.0 and sigma between 85 and 439 quanta/micron 2. Human retinas, ranging from 18 to 58 hours postmortem and treated as above, also produced photoresponses. Of the 7 retinas studied so far, rhodopsin has been regenerated to 0.1-0.35 nmol/mg protein, cGMP to 23.5-49.2 pmol/mg protein, and PIII to 20-50 microV: in some cases a b-wave was also seen. Values of n varied between 0.6 and 1.0, and sigma between 132 and 3700 quanta/micron 2. PIII responses were also seen after retinas, approximately 30 hours postmortem, were incubated for a further 24 hours in fortified medium. After incubation, retinal vacuolation was reduced.

Adolescent↗
PubMed1993

Characteristics of beta-lactoglobulin binding to the all-trans-retinal moiety covalently immobilized on Celite.

All-trans-retinal was covalently immobilized on Celite and investigated as a bioselective adsorption matrix for beta-lactoglobulin. Two types of Celite supports were compared, indicating the best performance with 100/120 mesh, type R648. The R648 matrix yielded a high concentration (9.2 mumol/ml) of the ligand when the derivative was produced, and the derivatized matrix exhibited the best retention of beta-lactoglobulin. Binding of beta-lactoglobulin to the immobilized trans-retinal matrix is biospecific, but the affinity is dependent on pH and ionic strength. alpha-Lactalbumin is not bound to this bioselective adsorbant, so its elution was not retarded or affected by pH or buffer concentration. Affinity for beta-lactoglobulin was optimal at pH 5.14; a dissociation constant of 2.7 microM was obtained in .1 M buffer solutions. At pH 7.0, the affinity decreased 44-fold, and, below pH 3.5, no binding occurred. The estimated loading capacity based on chromatographic data was approximately 14 g/L (.75 mumol/ml) of support.

Adsorption↗
PubMed1999

Binding of lipophilic nutrients to beta-lactoglobulin prepared by bioselective adsorption.

The binding of the lipophilic nutrients, retinal, vitamin D2, and retinyl palmitate by beta-lactoglobulin was measured by analysis of changes in the fluorescence of the tryptophanyl residue of beta-lactoglobulin or the retinyl moiety. The fluorescence intensity of the tryptophanyl residue was quenched by retinoid or vitamin D binding but was enhanced by palmitate binding. The analysis of competitive binding experiments with palmitate indicated that retinal and palmitate did not compete for the same site; however, vitamin D2, which binds with a stoichiometry of 2, appeared to displace palmitate at higher concentrations. Also, the retinoids and vitamin D2 were bound more tightly than was palmitate. The results are consistent with the model in which the retinoids and vitamin D2 bind in the calyx formed by the beta-barrel; palmitate and a second molecule of vitamin D2 bind in a surface pocket near the dimer contact region. Retinyl palmitate, which has both moieties, appeared to bind at both sites.

Adsorption↗
PubMed1978

Electrocyclization reaction of higher conjugated polyenals: photochemical behaviors of retinal (vitamin A1 aldehyde) homologues.

During the studies on a photoreaction of retinal, involving various kinds of (Z)-(E) isomerization, a heretofore unknown photoproduct of retinal was isolated in a pure state and was characterized unambiguously. Thus, direct irradiation of all-(E)-retinal (I) and of all-(E)-beta-ionylidenecrotonaldehyde (II) in acetonitrile solution gave the corresponding 6e-electrocyclized photoproducts, (III) and (IV), both via the possible 7-(Z)-isomer intermediates of the parent conjugated polyenals. Unlike the lower members in the retinal series, it was also confirmed that sigmatropic rearrangement or photo-Diels-Alder reaction hardly proceeds in these higher members of the series mentioned above.

Acetonitriles↗