Studies of the spontaneous transfer of retinol from the retinol: retinol-binding protein complex to unilamellar liposomes

Fex, Göran; Johannesson, Gunvor

doi:10.1016/0005-2736(87)90122-2

Cited by 48 publications

(19 citation statements)

References 40 publications

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“…A time constant of <30 s has been reported for transfer between bilayers, indicating that despite its hydrophobic nature, retinol is able to dissociate from lipids and travel through the aqueous phase without the assistance of shuttle proteins. 33 − 35 …”

Section: Results and Discussionmentioning

confidence: 99%

Characterization of Retinol Stabilized in Phosphatidylcholine Vesicles with and without Antioxidants

Chmykh

Nadeau

2020

ACS Omega

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Retinol stability has been reported to be improved by encapsulation in liposomes, both with and without cholesterol. However, this improvement is limited because of lipid peroxidation. In this study, we compare the stability of retinol in phosphatidylcholine liposomes under ultraviolet (UV) light or standard room air, with and without the addition of antioxidants. Both butylated hydroxytoluene (BHT) and a proprietary mix (StoppOx) improved the shelf stability from <10 to over 30 d. The addition of cholesterol had no effect. Fluorescence imaging showed a heterogeneous distribution of retinol within the vesicles, including within the aqueous layer. Fluorescence lifetimes were equally heterogeneous. Under UV irradiation, StoppOx protected retinol for significantly longer than BHT and via different mechanisms. This suggests that natural antioxidants work well to improve the retinol stability, but that further work to determine the optimal vesicle structure remains to be performed.

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Section: Results and Discussionmentioning

confidence: 99%

Characterization of Retinol Stabilized in Phosphatidylcholine Vesicles with and without Antioxidants

Chmykh

Nadeau

2020

ACS Omega

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“…Whether this takes place entirely via aqueous transfer through the IPM (Rando and Bangerter, 1982;Fex and Johannesson, 1987;Ho et al, 1989) or whether another retinoid-binding protein not normally expressed in the IPM is derived from other cellular The ERG traces were in response to a high-intensity (0.3 log cd sec /m 2 ) flash stimulus delivered to the dark-adapted retina; two successive traces obtained for each mouse are superimposed. compartments that border the I PM (e.g., RPE and Müller cells) has yet to be determined.…”

Section: Discussionmentioning

confidence: 99%

Early Onset Photoreceptor Abnormalities Induced by Targeted Disruption of the Interphotoreceptor Retinoid-Binding Protein Gene

et al. 1998

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Vision in all vertebrates is dependent on an exchange of retinoids between the retinal pigment epithelium and the visual photoreceptors. It has been proposed that the interphotoreceptor retinoid-binding protein (IRBP) is essential for this intercellular exchange, and that it serves to prevent the potentially cytotoxic effects of retinoids. Although its precise function in vivo has yet to be defined, the early expression of IRBP suggests that it may also be required for normal photoreceptor development. To further assess the biological role of IRBP, we generated transgenic mice with targeted disruption of the IRBP gene (IRBP-/- mice). Specifically, homologous recombination was used to replace the first exon and promoter region of the IRBP gene with a phosphoglycerate kinase-promoted neomycin-resistant gene. Immunocytochemical and Western blot analyses demonstrated the absence of IRBP expression in the IRBP-/- mice. As early as postnatal day 11, histological examination of the retinas of IRBP-/- mice revealed a loss of photoreceptor nuclei and changes in the structural integrity of the receptor outer segments. At 30 d of age, the photoreceptor abnormalities in IRBP-/- mice were more severe, and electroretinographic recordings revealed a marked loss in photic sensitivity. In contrast, no morphological or electrophysiological changes were detected in age-matched heterozygotes. These observations indicate that normal photoreceptor development and function are highly dependent on the early expression of IRBP, and that in the absence of IRBP there is a slowly progressive degeneration of retinal photoreceptors.

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“…For example, Rando and Bangerter (72) demonstrated that the intermembranous rates of retinoid (all-trans-retinol(al) and 11-cis-retinol) transfer from vesicle to vesicle and vesicle to erythrocyte were exceedingly rapid, whereas all-trans-retinyl palmitate did not undergo transfer at an appreciable rate. Fex and Johannesson (73,74) showed that retinol, similar to unesterified cholesterol and long-chain fatty acids but unlike phospholipids, can transfer rapidly and spontaneously between liposomal membranes. Noy et al (75) suggested that retinoid transfer between different cell types in vivo may depend on the geometry of cellular surfaces, which are highly elaborated in the RPE apical membrane.…”

Section: Photic Generation Of 11-cis-retinal In the Rpementioning

confidence: 99%

Photic generation of 11-cis-retinal in bovine retinal pigment epithelium

Zhang

Choi

Tworak

et al. 2019

Journal of Biological Chemistry

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Studies of the spontaneous transfer of retinol from the retinol: retinol-binding protein complex to unilamellar liposomes

Cited by 48 publications

References 40 publications

Characterization of Retinol Stabilized in Phosphatidylcholine Vesicles with and without Antioxidants

Characterization of Retinol Stabilized in Phosphatidylcholine Vesicles with and without Antioxidants

Early Onset Photoreceptor Abnormalities Induced by Targeted Disruption of the Interphotoreceptor Retinoid-Binding Protein Gene

Photic generation of 11-cis-retinal in bovine retinal pigment epithelium

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