β-ionone activates and bleaches visual pigment in salamander photoreceptors

Vision begins with photoisomerization of 11-cis retinal to the all-trans conformation within the chromophore-binding pocket of opsin, leading to activation of a biochemical cascade. Release of all-trans retinal from the binding pocket curtails but does not fully quench the ability of opsin to activa...

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Veröffentlicht in:Visual neuroscience 2009-05, Vol.26 (3), p.267-274
Hauptverfasser: ISAYAMA, TOMOKI, McCABE ENGLAND, S.L., CROUCH, R.K., ZIMMERMAN, A.L., MAKINO, C.L.
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container_end_page 274
container_issue 3
container_start_page 267
container_title Visual neuroscience
container_volume 26
creator ISAYAMA, TOMOKI
McCABE ENGLAND, S.L.
CROUCH, R.K.
ZIMMERMAN, A.L.
MAKINO, C.L.
description Vision begins with photoisomerization of 11-cis retinal to the all-trans conformation within the chromophore-binding pocket of opsin, leading to activation of a biochemical cascade. Release of all-trans retinal from the binding pocket curtails but does not fully quench the ability of opsin to activate transducin. All-trans retinal and some other analogs, such as β-ionone, enhance opsin’s activity, presumably on binding the empty chromophore-binding pocket. By recording from isolated salamander photoreceptors and from patches of rod outer segment membrane, we now show that high concentrations of β-ionone suppressed circulating current in dark-adapted green-sensitive rods by inhibiting the cyclic nucleotide-gated channels. There were also decreases in circulating current and flash sensitivity, and accelerated flash response kinetics in dark-adapted blue-sensitive (BS) rods and cones, and in ultraviolet-sensitive cones, at concentrations too low to inhibit the channels. These effects persisted in BS rods even after incubation with 9-cis retinal to ensure complete regeneration of their visual pigment. After long exposures to high concentrations of β-ionone, recovery was incomplete unless 9-cis retinal was given, indicating that visual pigment had been bleached. Therefore, we propose that β-ionone activates and bleaches some types of visual pigments, mimicking the effects of light.
doi_str_mv 10.1017/S0952523809090105
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subjects Animals
Biological and medical sciences
Caudata
Cyclic Nucleotide-Gated Cation Channels - antagonists & inhibitors
Cyclic nucleotide-gated channel
Dark Adaptation - physiology
Dose-Response Relationship, Drug
Electric Conductivity
Eye and associated structures. Visual pathways and centers. Vision
Fundamental and applied biological sciences. Psychology
In Vitro Techniques
Kinetics
Larva
Membranes - drug effects
Membranes - metabolism
Membranes - physiology
Neurophysiology
Norisoprenoids - administration & dosage
Norisoprenoids - pharmacology
Photoreceptor Cells, Vertebrate - drug effects
Photoreceptor Cells, Vertebrate - metabolism
Photoreceptor Cells, Vertebrate - physiology
Phototransduction
Retinal Pigments - metabolism
Retinal Rod Photoreceptor Cells - drug effects
Retinal Rod Photoreceptor Cells - physiology
Retinoids
Rhodopsin
Rod Cell Outer Segment - drug effects
Rod Cell Outer Segment - metabolism
Rod Cell Outer Segment - physiology
Time Factors
Urodela - growth & development
Urodela - metabolism
Vertebrates: nervous system and sense organs
title β-ionone activates and bleaches visual pigment in salamander photoreceptors
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