Support for a proposed retinoid-processing protein complex in apical retinal pigment epithelium

Vera L. Bonilha; Sanjoy K. Bhattacharya; Karen A. West; John S. Crabb; Jian Sun; Mary E. Rayborn; Maria Nawrot; John C. Saari; John W. Crabb

doi:10.1016/j.exer.2004.04.001

Support for a proposed retinoid-processing protein complex in apical retinal pigment epithelium

Vera L. Bonilha, Sanjoy K. Bhattacharya, Karen A. West, John S. Crabb, Jian Sun, Mary E. Rayborn, Maria Nawrot, John C. Saari, John W. Crabb

Research output: Contribution to journal › Article › peer-review

29 Scopus citations

Abstract

The interaction of cellular retinaldehyde-binding protein (CRALBP) with ERM (ezrin, radixin, moesin)-binding phosphoprotein 50 (EBP50) in retinal pigment epithelium (RPE) microsomes has led to the hypothesis that a retinoid-processing protein complex exists in apical RPE. Mouse RPE apical processes were isolated on wheat germ agglutinin-coated agarose beads. Proteomic analyses of the isolated apical RPE demonstrated the presence of CRALBP, EBP50, 11-cis-retinol dehydrogenase, cellular retinol-binding protein 1, and interphotoreceptor retinoid-binding protein. The results support the hypothesis that a visual cycle protein complex may serve in the localization and release of 11-cis-retinoid in the apical RPE.

Original language	English (US)
Pages (from-to)	419-422
Number of pages	4
Journal	Experimental Eye Research
Volume	79
Issue number	3
DOIs	https://doi.org/10.1016/j.exer.2004.04.001
State	Published - Sep 2004
Externally published	Yes

Keywords

proteomics
retinal pigment epithelium
retinoids
visual cycle

ASJC Scopus subject areas

Ophthalmology
Sensory Systems

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10.1016/j.exer.2004.04.001

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Support for a proposed retinoid-processing protein complex in apical retinal pigment epithelium. / Bonilha, Vera L.; Bhattacharya, Sanjoy K.; West, Karen A.; Crabb, John S.; Sun, Jian; Rayborn, Mary E.; Nawrot, Maria; Saari, John C.; Crabb, John W.

In: Experimental Eye Research, Vol. 79, No. 3, 09.2004, p. 419-422.

Research output: Contribution to journal › Article › peer-review

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title = "Support for a proposed retinoid-processing protein complex in apical retinal pigment epithelium",

abstract = "The interaction of cellular retinaldehyde-binding protein (CRALBP) with ERM (ezrin, radixin, moesin)-binding phosphoprotein 50 (EBP50) in retinal pigment epithelium (RPE) microsomes has led to the hypothesis that a retinoid-processing protein complex exists in apical RPE. Mouse RPE apical processes were isolated on wheat germ agglutinin-coated agarose beads. Proteomic analyses of the isolated apical RPE demonstrated the presence of CRALBP, EBP50, 11-cis-retinol dehydrogenase, cellular retinol-binding protein 1, and interphotoreceptor retinoid-binding protein. The results support the hypothesis that a visual cycle protein complex may serve in the localization and release of 11-cis-retinoid in the apical RPE.",

keywords = "proteomics, retinal pigment epithelium, retinoids, visual cycle",

author = "Bonilha, {Vera L.} and Bhattacharya, {Sanjoy K.} and West, {Karen A.} and Crabb, {John S.} and Jian Sun and Rayborn, {Mary E.} and Maria Nawrot and Saari, {John C.} and Crabb, {John W.}",

note = "Funding Information: Supported by NIH grants EY06603, EY14239, EY02317, an unrestricted award from Research to Prevent Blindness, Inc. (University of Washington), a Research Center grant from The Foundation Fighting Blindness, and funds from the Cleveland Clinic Foundation. We thank Mei Yin for assistance with SEM.",

year = "2004",

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doi = "10.1016/j.exer.2004.04.001",

language = "English (US)",

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AU - Bonilha, Vera L.

AU - Bhattacharya, Sanjoy K.

AU - West, Karen A.

AU - Crabb, John S.

AU - Sun, Jian

AU - Rayborn, Mary E.

AU - Nawrot, Maria

AU - Saari, John C.

AU - Crabb, John W.

N1 - Funding Information: Supported by NIH grants EY06603, EY14239, EY02317, an unrestricted award from Research to Prevent Blindness, Inc. (University of Washington), a Research Center grant from The Foundation Fighting Blindness, and funds from the Cleveland Clinic Foundation. We thank Mei Yin for assistance with SEM.

PY - 2004/9

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N2 - The interaction of cellular retinaldehyde-binding protein (CRALBP) with ERM (ezrin, radixin, moesin)-binding phosphoprotein 50 (EBP50) in retinal pigment epithelium (RPE) microsomes has led to the hypothesis that a retinoid-processing protein complex exists in apical RPE. Mouse RPE apical processes were isolated on wheat germ agglutinin-coated agarose beads. Proteomic analyses of the isolated apical RPE demonstrated the presence of CRALBP, EBP50, 11-cis-retinol dehydrogenase, cellular retinol-binding protein 1, and interphotoreceptor retinoid-binding protein. The results support the hypothesis that a visual cycle protein complex may serve in the localization and release of 11-cis-retinoid in the apical RPE.

AB - The interaction of cellular retinaldehyde-binding protein (CRALBP) with ERM (ezrin, radixin, moesin)-binding phosphoprotein 50 (EBP50) in retinal pigment epithelium (RPE) microsomes has led to the hypothesis that a retinoid-processing protein complex exists in apical RPE. Mouse RPE apical processes were isolated on wheat germ agglutinin-coated agarose beads. Proteomic analyses of the isolated apical RPE demonstrated the presence of CRALBP, EBP50, 11-cis-retinol dehydrogenase, cellular retinol-binding protein 1, and interphotoreceptor retinoid-binding protein. The results support the hypothesis that a visual cycle protein complex may serve in the localization and release of 11-cis-retinoid in the apical RPE.

KW - proteomics

KW - retinal pigment epithelium

KW - retinoids

KW - visual cycle

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Support for a proposed retinoid-processing protein complex in apical retinal pigment epithelium

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Keywords

ASJC Scopus subject areas

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