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) |
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Pages (from-to) | 419-422 |
Number of pages | 4 |
Journal | Experimental Eye Research |
Volume | 79 |
Issue number | 3 |
DOIs | |
State | Published - Sep 1 2004 |
Externally published | Yes |
Keywords
- proteomics
- retinal pigment epithelium
- retinoids
- visual cycle
ASJC Scopus subject areas
- Ophthalmology
- Sensory Systems