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Vitamin A aldehyde-taurine adduct and the visual cycle.

ABSTRACT: Visual pigment consists of opsin covalently linked to the vitamin A-derived chromophore, 11-cis-retinaldehyde. Photon absorption causes the chromophore to isomerize from the 11-cis- to all-trans-retinal configuration. Continued light sensitivity necessitates the regeneration of 11-cis-retinal via a series of enzyme-catalyzed steps within the visual cycle. During this process, vitamin A aldehyde is shepherded within photoreceptors and retinal pigment epithelial cells to facilitate retinoid trafficking, to prevent nonspecific reactivity, and to conserve the 11-cis configuration. Here we show that redundancy in this system is provided by a protonated Schiff base adduct of retinaldehyde and taurine (A1-taurine, A1T) that forms reversibly by nonenzymatic reaction. A1T was present as 9-cis, 11-cis, 13-cis, and all-trans isomers, and the total levels were higher in neural retina than in retinal pigment epithelium (RPE). A1T was also more abundant under conditions in which 11-cis-retinaldehyde was higher; this included black versus albino mice, dark-adapted versus light-adapted mice, and mice carrying the Rpe65-Leu450 versus Rpe65-450Met variant. Taurine levels paralleled these differences in A1T. Moreover, A1T was substantially reduced in mice deficient in the Rpe65 isomerase and in mice deficient in cellular retinaldehyde-binding protein; in these models the production of 11-cis-retinal is compromised. A1T is an amphiphilic small molecule that may represent a mechanism for escorting retinaldehyde. The transient Schiff base conjugate that the primary amine of taurine forms with retinaldehyde would readily hydrolyze to release the retinoid and thus may embody a pool of 11-cis-retinal that can be marshalled in photoreceptor cells.

SUBMITTER: Kim HJ

PROVIDER: S-EPMC7547175 | biostudies-literature |

REPOSITORIES: biostudies-literature

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Project description:Recently, the conjugation of metal oxide nanoparticles with organic moieties has attracted the attention of many researchers for various applications. In this research, the green and biodegradable vitamin C was employed in a facile and inexpensive procedure to synthesize the vitamin C adduct (3), which was then blended with green ZnONPs to fabricate a new composite category (ZnONPs@vitamin C adduct). The morphology and structural composition of the prepared ZnONPs and their composites were confirmed by several techniques: Fourier-transform infrared (FT-IR) spectroscopy, field-emission scanning electron microscopy (FE-SEM), UV-vis differential reflectance spectroscopy (DRS), energy dispersive X-ray (EDX) analysis, elemental mapping, X-ray diffraction (XRD) analysis, photoluminescence (PL) spectroscopy, and zeta potential measurements. The structural composition and conjugation strategies between the ZnONPs and vitamin C adduct were revealed by FT-IR spectroscopy. The experimental results for the ZnONPs showed that they possessed a nanocrystalline wurtzite structure with quasi-spherical particles with a polydisperse size ranging from 23 to 50 nm, while the particle size appeared greater in the FE-SEM images (band gap energy of 3.22 eV); after loading with the l-ascorbic acid adduct (3), the band gap energy dropped to 3.06 eV. Later, under solar light irradiation, the photocatalytic activities of both the synthesized ZnONPs@vitamin C adduct (4) and ZnONPs, including the stability, regeneration and reusability, catalyst amount, initial dye concentration, pH effect, and light source studies, were investigated in detail in the degradation of Congo red dye (CR). Furthermore, an extensive comparison between the fabricated ZnONPs, composite (4), and ZnONPs from previous studies was performed to gain insights to commercialize the catalyst (4). Under optimum conditions, the photodegradation of CR after 180 min was 54% for ZnONPs and 95% for the ZnONPs@l-ascorbic acid adduct. Moreover, the PL study confirmed the photocatalytic enhancement of the ZnONPs. The photocatalytic degradation fate was determined by LC-MS spectrometry.

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Vitamin A aldehyde-taurine adduct and the visual cycle.

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