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- W2078335037 abstract "Light detection destroys the visual pigment of vertebrate rod photoreceptors, rhodopsin, as its retinyl moiety is photoisomerized from 11-cis to all-trans. Rhodopsin is regenerated through a series of reactions that begin in the rod outer segment with the release of the all-trans retinal and its reduction to all-trans retinol. All-trans retinol is then transported to the neighboring retinal pigment epithelial cells where it is used to remake 11-cis retinal. The reduction of all-trans retinal to all-trans retinol is catalyzed by retinol dehydrogenase and requires metabolic input in the form of NADPH. We have used the fluorescence of all-trans retinol to monitor its concentration in isolated mouse rod photoreceptors. After the bleaching of rhodopsin, all-trans retinol formation proceeds with a rate of ∼0.06 min−1, which is faster than the rate of rhodopsin regeneration in whole animals; this would allow recycled chromophore to contribute to the 11-cis retinal used for regeneration. Inner segment metabolic pathways appear to make a significant contribution to the pool of NADPH needed for the reduction of all-trans retinal, as formation of all-trans retinol is suppressed in rod outer segments separated from the cell body. Finally, generation of all-trans retinol is suppressed in the absence of glucose, indicating a critical dependence of all-trans retinol formation on the level of metabolic activity." @default.
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- W2078335037 date "2009-02-01" @default.
- W2078335037 modified "2023-09-26" @default.
- W2078335037 title "Formation Of All-Trans Retinol In Mouse Rod Photoreceptors" @default.
- W2078335037 doi "https://doi.org/10.1016/j.bpj.2008.12.2724" @default.
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