Rhodopsin regeneration in the normal and in the detached/replaced retina of the skate

Sun, Yifan; Ripps, Harris

doi:10.1016/0014-4835(92)90173-p

Cited by 10 publications

(6 citation statements)

References 35 publications

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“…By binding all-trans retinol and 11-cis retinal, IRBP solubilizes these hydrophobic compounds and protects them from isomeric and oxidative degradation (Chen and Noy, 1994 ;Crouch et al, 1992 ;Tschanz and Noy, 1997). Furthermore, IRBP promotes both the delivery of alltrans retinol from rods to the RPE and the transfer of 11-cis retinal from the RPE to the rods (Carlson and Bok, 1992 ;Jones et al, 1989 ;Okajima et al, 1989Okajima et al, , 1990Sun and Ripps, 1992).…”

Section: Introductionmentioning

confidence: 97%

Interphotoreceptor Retinoid-Binding Protein (IRBP) is Rapidly Cleared From theXenopusInterphotoreceptor Matrix

Cunningham

Yang

Gonzalez‐Fernandez

1999

Experimental Eye Research

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Section: Introductionmentioning

confidence: 97%

Interphotoreceptor Retinoid-Binding Protein (IRBP) is Rapidly Cleared From theXenopusInterphotoreceptor Matrix

Cunningham

Yang

Gonzalez‐Fernandez

1999

Experimental Eye Research

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“…12,13 Furthermore, IRBP promotes both the delivery of all-trans retinol from rods to the RPE and the transfer of 11-cis retinal from the RPE to the rods. [14][15][16][17][18] Its modular structure distinguishes IRBP from other retinoidbinding proteins. The IRBP gene is composed of multiple repeats [4 in mammals [19][20][21][22] and amphibians 23 ; 2 in teleosts 24,25 ] which code for homologous regions, or modules.…”

Section: Introductionmentioning

confidence: 99%

Fourth module of Xenopus interphotoreceptor retinoid-binding protein: activity in retinoid transfer between the retinal pigment epithelium and rod photoreceptors

Gonzalez‐Fernandez

Baer

Baker

et al. 1998

Current Eye Research

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“…First, since retinoids are insoluble compounds, IRBP is thought to solubilize retinoids within the IPM (Pepperberg et al 1993). Secondly, IRBP is thought to target the delivery of all-trans retinol to the RPE (Okajima et al 1989), and promote the release of 11-cis retinal from the RPE (Okajima et al 1990, Carlson & Bok 1992, Sun & Ripps 1992.…”

Section: The Interphotoreceptor (Ipm) -More Than Meets the Rpementioning

confidence: 99%

Evolution of the visual cycle: the role of retinoid-binding proteins

Gonzalez‐Fernandez¹

2002

Journal of Endocrinology

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The trafficking of retinoids in the retina represents a model to study soluble hormone-binding proteins in a complex system subject to profound evolutionary adaptations. Although a remarkable illustration of convergent evolution, all visual systems detect light in the same way, that is through the photoisomerization of an 11-cis retinoid to a corresponding trans isomer. What is strikingly different between the systems, is the mechanism by which the 11-cis chromophore is reformed and visual pigment regenerated in a process known as the visual cycle. The variations of the cycle address a problem inherent to retinoids themselves. That is, the properties that make these molecules suited for light detection also account for their susceptibility to oxidative and isomeric degradation, and cellular toxicity. The cycle therefore provides an opportunity to examine the role of soluble hormonebinding proteins within an integrative and evolutionary context. The present review focuses on interphotoreceptor retinoid-binding protein (IRBP), a controversial glycolipoprotein that recruits a protein fold common to Cterminal-processing proteases and the crotonase family. This unorthodox retinoid-binding protein is entrapped in the subretinal compartment of those eyes that translocate visual cycle retinoids between the photoreceptors and the retinal pigment epithelium. Recent studies suggest that we should look beyond a strictly carrier function if we are to appreciate the role of IRBP in the visual cycle. Here we draw lessons from other soluble hormone-binding proteins to anticipate avenues of future research likely to provide insight into the structure and function of IRBP in vision.

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Rhodopsin regeneration in the normal and in the detached/replaced retina of the skate

Cited by 10 publications

References 35 publications

Interphotoreceptor Retinoid-Binding Protein (IRBP) is Rapidly Cleared From theXenopusInterphotoreceptor Matrix

Interphotoreceptor Retinoid-Binding Protein (IRBP) is Rapidly Cleared From theXenopusInterphotoreceptor Matrix

Fourth module of Xenopus interphotoreceptor retinoid-binding protein: activity in retinoid transfer between the retinal pigment epithelium and rod photoreceptors

Evolution of the visual cycle: the role of retinoid-binding proteins

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