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

被引：32

作者：

Bonilha, VL

Bhattacharya, SK

West, KA

Crabb, JS

Sun, J

Rayborn, ME

Nawrot, M

Saari, JC

Crabb, JW

机构：

[1] Cleveland Clin Fdn, Cole Eye Inst I3L, Cleveland, OH 44195 USA

[2] Univ Washington, Dept Ophthalmol, Seattle, WA 98195 USA

[3] Univ Washington, Dept Biochem, Seattle, WA 98195 USA

来源：

EXPERIMENTAL EYE RESEARCH | 2004年 / 79卷 / 03期

关键词：

retinoids; proteomics; retinal pigment epithelium; visual cycle;

D O I：

10.1016/j.exer.2004.04.001

中图分类号：

R77 [眼科学];

学科分类号：

100212 ;

摘要：

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. (C) 2004 Elsevier Ltd. All rights reserved.

引用

页码：419 / 422

页数：4

共 17 条

[1]

BHATTACHARYA SK, 2002, FED AM SOC EXP BIOL, V14, P2

[2]

BHATTACHARYA SK, 2002, ANN M ASS RES VIS OP

[3] Ezrin promotes morphogenesis of apical microvilli and basal infoldings in retinal pigment epithelium [J].