Occurrence of a binding protein for 11-cis-retinal in retina.

Futterman, Sidney; Saari, John C.; Blair, Sloane R.

doi:10.1016/s0021-9258(17)40382-6

Cited by 80 publications

(8 citation statements)

References 13 publications

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“…In order to answer this question, we incubated the RPE with apical medium which was devoid of binding proteins or which contained one of a number of apoproteins, other than apo-IRBP. These proteins included apo-CRALBP, apo-RBP, and fatty acid-free BSA, none of which are native to the IPM but can all bind retinoids, including 11-cw-RAL, to varying degrees (Futterman et al, 1977; Horwitz & Heller, 1973). ByHPLC analysis it was determined that if the RPE was incubated with a protein other than apo-IRBP, or if the medium was devoid of binding proteins, the level of [3H]-11-cw-RAL detected apically was reduced by 3-11-fold.…”

Section: Discussionmentioning

confidence: 99%

Promotion of the release of 11-cis-retinal from cultured retinal pigment epithelium by interphotoreceptor retinoid-binding protein

Carlson¹,

Bok²

1992

Biochemistry

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This study investigates whether the interphotoreceptor retinoid-binding protein (IRBP) is necessary for the release of 11-cis-retinaldehyde (RAL) or if the retinoid is constitutively released from the retinal pigment epithelium (RPE) following synthesis. The strategic location of IRBP in the interphotoreceptor matrix (IPM) and its retinoid-binding ability make it a candidate for a role in 11-cis-RAL release. Fetal bovine RPE cells were grown in permeable chambers, and their apical surfaces were incubated with medium containing either apo-IRBP, the apo form of cellular retinaldehyde-binding protein (CRALBP), the apo form of serum retinol-binding protein (RBP), or bovine serum albumin (BSA) or with medium devoid of binding proteins. [3H]-all-trans-Retinol (ROL) was delivered to the basal surface of the cells by RBP. High-performance liquid chromatography demonstrated that [3H]-11-cis-RAL was optimally released into the apical medium when apo-IRBP was present. The most surprising result was the diminished level of [3H]-11-cis-RAL when apo-CRALBP was in the apical medium. Circular dichroism demonstrated that CRALBP had not been denatured by the photobleaching required for endogenous ligand removal. Therefore, apo-CRALBP should have been able to bind [3H]-11-cis-RAL if it was constitutively released into the apical medium. In addition, when proteins other than apo-IRBP were present, or if the cells were incubated with medium alone, the observed decrease in apical [3H]-11-cis-RAL was concomitant with a buildup of intracellular [3H]-all-trans-retinyl palmitate and [3H]-all-trans-ROL in the basal culture medium.(ABSTRACT TRUNCATED AT 250 WORDS)

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Section: Discussionmentioning

confidence: 99%

Promotion of the release of 11-cis-retinal from cultured retinal pigment epithelium by interphotoreceptor retinoid-binding protein

Carlson¹,

Bok²

1992

Biochemistry

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“…Differences in the properties of IRBP and CRALBP must be kept in mind when considering the functional roles of the two proteins. CRALBP displays a high degree of specificity; of the compounds tested so far, only retinoids bind to the protein, and among the retinoids, only retinols and retinals of the 11-cis-configuration are bound (16). Direct binding of other cis-isomers has not yet been investigated.…”

Section: Retinamentioning

confidence: 99%

Immunocytochemical localization of two retinoid-binding proteins in vertebrate retina.

Bunt-Milam¹,

Saari²

1983

The Journal of Cell Biology

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403

208

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The recent discovery and characterization of several proteins that purify with endogenous, bound retinoid have given rise to the suggestion that these proteins, which are abundant in retina, perform a role in transport and function of vitamin A. Immunocytochemical techniques were used to localize two retinoid-binding proteins in the retina of four species. Antisera to cellular retinal-binding protein (CRALBP) and an interphotoreceptor retinoidbinding protein (IRBP) were obtained from rabbits immunized with antigens purified from bovine retina. Antibodies from each antiserum reacted with a single component in retinal homogenates and supernatants which corresponded to the molecular weight and charge of the respective antigen (non-SDS and SDS PAGE, electrophoretic transfer to nitrocellulose, immunochernical staining). Immunocytochemistry controls were antibodies from nonimmune serum and antibodies absorbed with purified antigen. Antigens were localized on frozensectioned bovine, rat, monkey, and human retina using immunofluorescence and the peroxidase-antiperoxidase technique. Specific staining with anti-IRBP was found in the space that surrounds photoreceptor outer segments, with heaviest labeling in a line corresponding to the retinal pigment epithelium (RPE) apical surface. Cone outer segments were positive. Staining with anti-CRALBP was found in two cell types in all species: the RPE and the M011er glial cell. Within the RPE, labeling filled the cytoplasm and was heaviest apically, with negative nuclei. Labeling of M011er cells produced Golgi-like silhouettes with intense staining of all cytoplasmic compartments. Staining of the external limiting membrane was heavy, with labeled microvilli projecting into the interphotoreceptor space. Localization of IRBP to this space bordered by three cell types (RPE, photoreceptor, and Mfiller) is consistent with its proposed role in transport of retinoids among cells. Localization of CRALBP in RPE corroborates previous biochemical studies; its presence in the MOiler cell suggests that this glial cell may play a hitherto unsuspected role in vitamin A metabolism in retina.

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“…CRALBP is found predominantly in the RPE and Muller cells of the retina [317,318]. This protein binds specifically 9-or 11-cis-retinol and RALs with low nanomolar affinities in vitro.…”

Section: Specialized Ocular Retinol-binding Proteinsmentioning

confidence: 99%

The molecular aspects of absorption and metabolism of carotenoids and retinoids in vertebrates

Widjaja‐Adhi

Golczak

2020

Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biolog

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Occurrence of a binding protein for 11-cis-retinal in retina.

Cited by 80 publications

References 13 publications

Promotion of the release of 11-cis-retinal from cultured retinal pigment epithelium by interphotoreceptor retinoid-binding protein

Promotion of the release of 11-cis-retinal from cultured retinal pigment epithelium by interphotoreceptor retinoid-binding protein

Immunocytochemical localization of two retinoid-binding proteins in vertebrate retina.

The molecular aspects of absorption and metabolism of carotenoids and retinoids in vertebrates

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