An extracellular retinol-binding glycoprotein in the eyes of mutant rats with retinal dystrophy: development, localization, and biosynthesis.

Gonzalez‐Fernandez, Federico; Landers, Robert A.; Glazebrook, Patricia A.; Fong, Shao-Ling; Liou, Gregory I.; Lam, Dominic Man‐Kit; Bridges, C.D.B.

doi:10.1083/jcb.99.6.2092

Cited by 76 publications

(23 citation statements)

References 29 publications

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“…This coin cides with the time during which photore ceptor inner segments form and elongate [17] in the chick retina. This developmental course corresponds well with that found for rat [6,7], mouse [8] and human [9] IRBP by immunoblot studies. On the other hand, the ontogeny of serum albumin cannot be corre- …”

Section: Ontogeny O F Two Proteins In the Chick Ipmsupporting

confidence: 66%

“…IRBP was seen ( fig. 7) to build up sharply as the inner segments form, in agree ment with its ontogeny in other species [6][7][8][9], measured by immunochemical methods. In contrast, serum albumin accumulates gradually; its concentration in the subretinal space remains nearly constant throughout development, as the subretinal space be comes wider.…”

Section: Discussionmentioning

confidence: 75%

“…The pre sent study is the first to examine the totality of proteins present in the IPM of any retinal degeneration; previous emphasis [6][7][8] has been on immunoblots to detect IRBP alone. Figure 4 shows that not only is IRBP (140 kD) nondetectable in the RCS rat IPM [6,7], but also other changes occur in amounts of major IPM protein bands: the 220-, 27-, 24-and possibly 22-kD bands are diminished. The identities of these proteins and the significance of these changes are not yet known.…”

Section: Changes In Ipm Proteins In Rcs Rat Retinal Degenerationmentioning

confidence: 99%

“…Attention was focused on the proteins in the interphotoreceptor matrix (IPM), the thin layer of extracellular material between the neural retina and the retinal pigment epi thelium (RPE), by Adler and Severin in 1981 [1], Since that time, interphotoreceptor reti noid-binding protein (IRBP) was discovered [2,3], and many studies have dealt with its occurrence [4,5], ontogeny [6][7][8][9] and disap pearance during retinal degeneration [6-8, 10, 11 ] in several species.…”

Section: Introductionmentioning

confidence: 99%

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Comparison of Proteins in the Interphotoreceptor Matrix of Vertebrates

Adler

Spencer²,

Heth³

1988

Ophthalmic Res

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Interphotoreceptor matrix (IPM) proteins from a wide range of vertebrate species were examined by gel electrophoresis. Extensive similarities in the banding patterns of the proteins were found. S antigen, serum albumin and interphotoreceptor retinoid-binding protein (IRBP) were identified immunochemically. The latter two proteins dominate the IPM obtained from the apical surface of the retinal pigment epithelium, whereas IPM prepared from the retina washes contains IRBP plus outer-segment components including S antigen. IRBP is present in IPM from the all-cone lizard (Anolis) eye, as well as from rod and cone-dominant animals. The ontogeny of IRBP in chick IPM is different from that of serum albumin in age of onset and rapidity of development. Comparison between Royal College of Surgeons rat IPM and normal rat IPM showed that several proteins are changed in amount. This study is a step toward a functional characterization of components common to the IPM of all vertebrates.

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Section: Ontogeny O F Two Proteins In the Chick Ipmsupporting

confidence: 66%

Section: Discussionmentioning

confidence: 75%

Section: Changes In Ipm Proteins In Rcs Rat Retinal Degenerationmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Comparison of Proteins in the Interphotoreceptor Matrix of Vertebrates

Adler

Spencer²,

Heth³

1988

Ophthalmic Res

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“…This protein is expressed mainly by the cone and rod photoreceptor cells [11][12][13]. It binds to the retinoids in the interphotoreceptor matrix and facilitates their exchange between the IPM and the cells that carry out the visual cycle [14][15][16].…”

Section: Introductionmentioning

confidence: 99%

Interphotoreceptor Retinoid-Binding Protein Implications in Diabetic Retinopathy

Bermea¹

2018

Early Events in Diabetic Retinopathy and Intervention Strategies

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The interphotoreceptor retinoid-binding protein (IRBP) is the most abundant protein in the interphotoreceptor matrix (IPM) and its levels decrease beginning in the early stages of diabetes. IRBP participates in the delivery of retinoids between retinal cells to carry out the visual cycle and also protects those retinoids against degradation in the IPM. IRBP deficiency is related to several conditions such as retinitis pigmentosa, cone-rod dystrophy, increased oxidative stress in the photoreceptors, and myopia. Decreased IRBP levels in diabetes could be due to the secretion of inflammatory cytokines and a direct effect of hyperglycemia on the photoreceptors. It is known that prior to the occurrence of vascular changes in diabetic retina, electrophysiological alterations occur on early potentials. Alterations on the photoreceptor outer segments and increased oxidative stress indicate an important affliction of the photoreceptors from early stages. Due to the importance of IRBP in photoreceptor wellness, its decreased levels may be linked to early photoreceptor affection. More studies are required to describe in detail the whole impact that decreased levels of IRBP in diabetes may have.

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Interphotoreceptor retinoid-binding protein (IRBP): Expression in the adult and developingXenopus retina

et al. 1996

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Apposition of the neural retina and pigment epithelium is critical to photoreceptor development and function. Interphotoreceptor retinoid-binding protein (IRBP) is a major component of the extracellular matrix separating these epithelia in the African clawed frog Xenopus laevis (Gonzalez-Fernandez et al., [1993], J. Cell Sci. 105:7-21). In the adult retina, IRBP appears to mediate the transport of hydrophobic molecules, particularly retinoids and fatty acids, within the hydrophilic extracellular domain. In this paper, we compare the distribution of IRBP and its mRNA in adult and embryonic Xenopus retina. Xenopus IRBP antisense RNA, labeled with tritium or digoxigenin, was used for in situ hybridizaton studies. For immunohistochemistry, we used an antiserum against Xenopus IRBP expressed in Escherichia coli. In the adult, we found that IRBP is synthesized at similar levels by both rods and cones. The protein is restricted to the interphotoreceptor matrix, with lesser amounts in the pigment epithelial cytoplasm. In the embryo, expression of the mRNA for IRBP is restricted to the central retina, where photoreceptor differentiation has taken place. By contrast, the protein is distributed throughout the embryonic subretinal space. Therefore, the presence of IRBP precedes photoreceptor differentiation. In summary, IRBP is synthesized by both rods and cones and may be internalized by the pigment epithelium. In the embryo, IRBP is synthesized by the central retina and diffuses through the matrix, reaching the undifferentiated peripheral retina. In view of its ligand-binding properties, diffusion of IRBP may provide the peripheral neural retina with a vehicle to transport retinoids and docosahexaenoic acid (molecules critical to normal retinal development) from the pigment epithelium.

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An extracellular retinol-binding glycoprotein in the eyes of mutant rats with retinal dystrophy: development, localization, and biosynthesis.

Cited by 76 publications

References 29 publications

Comparison of Proteins in the Interphotoreceptor Matrix of Vertebrates

Comparison of Proteins in the Interphotoreceptor Matrix of Vertebrates

Interphotoreceptor Retinoid-Binding Protein Implications in Diabetic Retinopathy

Interphotoreceptor retinoid-binding protein (IRBP): Expression in the adult and developingXenopus retina

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