Sensitization of bleached rod photoreceptors by 11-cis-locked analogues of retinal.

Corson, D. Wesley; Cornwall, M. Carter; MacNichol, Edward F.; Jin, Junda; Johnson, Randy L.; Derguini, Fadila; Crouch, Rosalie K.; Nakanishi, Koji

doi:10.1073/pnas.87.17.6823

Cited by 77 publications

(29 citation statements)

References 40 publications

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“…Unpolarized monochromatic light stimuli were provided by an optical bench containing a tungsten/halogen lamp, Oriel (Stamford, CT) interference filters (10-nm bandpass), neutral density wedges, and fast electromagnetic shutters (Uniblitz, Rochester, NY) and were calibrated with a PIN photodiode radiometer (United Detector Technology, Santa Monica, CA) as described (15). §To whom reprint requests should be addressed.…”

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

“…Bleaching reduces the sensitivity of a cell by depleting the supply of native pigment and by reducing the amplitude of the quantal response from the residual pigment (14)(15)(16)(17). In the absence of li-cis-retinal, this desensitization persists indefinitely (15,18) and is unresponsive to the addition of all-trans-retinal (15,19) or its removal from opsin by hydroxylamine (20,21). We refer to the persistent component of desensitization that results from response attenuation and does not require the presence of a retinal-containing photoproduct as opsin desensitization.…”

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confidence: 99%

“…Light-evoked currents were recorded from the inner segment of rods of the tiger salamander Ambystoma tigrinum by means of a suction electrode connected to a current-tovoltage converter (List Electronics, Darmstadt, F.R.G., L/M-EPC7 patch clamp amplifier) (14,15 (33) and a dichroic ratio of3.78 for porphyropsin and 4.55 for the analogue pigment (see ref. 13).…”

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confidence: 99%

“…The 11-cis isomer of 9-desmethylretinal was separated from the trans isomer by HPLC (QA-porasil; hexane/ethyl acetate solvents) and characterized by absorption and NMR spectroscopy. The analogue was delivered to isolated rods in phosphatidylcholine vesicles in physiological saline as described (14,15).Unpolarized monochromatic light stimuli were provided by an optical bench containing a tungsten/halogen lamp, Oriel (Stamford, CT) interference filters (10-nm bandpass), neutral density wedges, and fast electromagnetic shutters (Uniblitz, Rochester, NY) and were calibrated with a PIN photodiode radiometer (United Detector Technology, Santa Monica, CA) as described (15). §To whom reprint requests should be addressed.…”

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confidence: 99%

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Relief of opsin desensitization and prolonged excitation of rod photoreceptors by 9-desmethylretinal.

Corson

Cornwall

MacNichol

et al. 1994

Proc. Natl. Acad. Sci. U.S.A.

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The 9-methyl group of 11-s-retinal plays a crucial role in photoexcitation of the visual pigment rhodopsin. A hydrogen-substituted analogue, 11-cis-9-desmethylretlnal, combines with opsin to form a pigment that produces abnormal photoproducts and diinished activation of the GTP-binding protein transducin in vitro. We have measured the formation of this analogue pigment in bleached salamander rods and determined the size and shape of its quantal response. In addition, we have characterized the influence of opsin and newly formed analogue pigment on the quantal response to native porphyropsin. We find that, as 11-cis-9-desmethylretinal combines with opsin in bleached rods, the amplitude of the quantal response from residual native pigment is elevated by 74.5-fold to 0.15 ± 0.09 pA, a value close to the amplitude of the quantal response before bleach (0.31 ± 0.10 pA). When activated by light, the new analogue pigment produces a quantal response that is ==30-fold smaller and decays ""5 times more slowly than that ofnative pigment in unbleached cells. We conclude that the 9-methyl group of retinal is not critical for conversion of opsin to its nondesensitizing state but that it is critical for the normal processes of activation and deactivation of metarhodopsin that give rise to the quantal response.Photoisomerization of li-cis-retinal (Fig. 1, structure 1) initiates an intramolecular rearrangement of rhodopsin that results in a catalytically active state of rhodopsin, R * (1-5). Deactivation of R* requires phosphorylation by rhodopsin kinase (6, 7) and the subsequent binding of arrestin (3,(7)(8)(9). In isolated photoreceptors, pigment activation and deactivation produce a discrete electrical response with a characteristic amplitude and time course (10,11). In an examination of the steric interactions between the apoprotein opsin and its chromophore, Ganter et al. (12) reported that 11-cis-9-desmethylretinal ( Fig. 1, structure 3) produced abnormal photoproducts and transducin activation that was 8% of the rhodopsin control. Here we examine the influence of the 9-methyl group of retinal on the amplitude and shape of the quantal response in isolated rods.To provide access to the ligand binding pocket ofopsin, the native chromophore (13) 11-cis-3,4-dehydroretinal (Fig. 1, structure 2) was removed by bleaching. Bleaching reduces the sensitivity of a cell by depleting the supply of native pigment and by reducing the amplitude of the quantal response from the residual pigment (14)(15)(16)(17). In the absence of li-cis-retinal, this desensitization persists indefinitely (15,18) and is unresponsive to the addition of all-trans-retinal (15,19) or its removal from opsin by hydroxylamine (20,21). We refer to the persistent component of desensitization that results from response attenuation and does not require the presence of a retinal-containing photoproduct as opsin desensitization. Taken together with the loss of sensitivity resulting from pigment depletion, the total loss of sensitivity is commonly referred to as ...

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Relief of opsin desensitization and prolonged excitation of rod photoreceptors by 9-desmethylretinal.

Corson

Cornwall

MacNichol

et al. 1994

Proc. Natl. Acad. Sci. U.S.A.

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The enduring legacy of Koji Nakanishi's research on bioorganic chemistry and natural products. Part 1: Isolation, structure determination and mode of action

2020

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In this brief review on Koji Nakanishi's remarkable career in natural products chemistry, we have highlighted a number of his accomplishments that illustrate the broad diversity of his interests. These include the isolation, structure determination, and biological mechanism of action of many natural products including the triterpenoid pristimerin; the diterpenoid ginkgolides; insect and crustacean molting hormones; phytoalexins; the toxic red tide principle brevetoxin; the vanadium tunicate pigments; philanthotoxin from killer wasps; antisickling agents; mitomycin DNA adducts; insect antifeedants; a mitotic hormone, the small molecule fish attractants from the sea anemone; new isolation and purification technologies; molecular chemistry of vision; age‐related macular degeneration; and the development of the exciton circular dichroism (CD) chirality method for microscale determination of absolute configuration of natural products and chirality of other chiral molecules and supramolecular assembly.

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Structure and Function of Activated Rhodopsin

Hofmann

Jäger

Ernst

1995

Israel Journal of Chemistry

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Abstract. After cis/trans isomerization of retinal and early photoproducts, activated rhodopsin (R*) develops signaling states for different proteins in a time-ordered sequence. Rhodopsin kinase binds all Meta forms, including the early Meta I, while interaction with transducin (G,) or arrestin requires the deprotonated Schiff base form, Meta II (MIl). G, recognizes a specific conformation, termed MIl b , which arises from an additional, spectrally silent conversion, linked to proton uptake. Collisional coupling with the GDP-bound G, holoprotein induces the release of GDP and formation of a stable R*-G, complex, in which the nucleotide binding site of G, is empty. The empty site complex, once formed, remains stable, even if the retinal is re-isomerized to the cis configuration. The cytoplasmic surface of rhodopsin appears to provide the majority of interaction sites for other proteins. Physical analyses and mutagenesis have emphasized the loops connecting helices CID and ElF of the seven-helix structure. Any interaction between R* and G, depends on a conserved charge pair at the interface between the helix C and the adjacent loop CD. Replacements or deletions in loops CD and EF were found to cause more specific functional defects, including slow release of GDP or failure of GTP-induced complex dissociation. In the dark, signaling states with low activity can be generated by reversible binding of all-trans-retinal to opsin. These lightindependent signaling states are different from the Meta forms.

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Sensitization of bleached rod photoreceptors by 11-cis-locked analogues of retinal.

Cited by 77 publications

References 40 publications

Relief of opsin desensitization and prolonged excitation of rod photoreceptors by 9-desmethylretinal.

Relief of opsin desensitization and prolonged excitation of rod photoreceptors by 9-desmethylretinal.

The enduring legacy of Koji Nakanishi's research on bioorganic chemistry and natural products. Part 1: Isolation, structure determination and mode of action

Structure and Function of Activated Rhodopsin

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