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 journalArticle

26 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 languageEnglish (US)
Pages (from-to)419-422
Number of pages4
JournalExperimental Eye Research
Volume79
Issue number3
DOIs
StatePublished - Sep 1 2004
Externally publishedYes

Keywords

  • proteomics
  • retinal pigment epithelium
  • retinoids
  • visual cycle

ASJC Scopus subject areas

  • Ophthalmology
  • Sensory Systems

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    Bonilha, V. L., Bhattacharya, S. K., West, K. A., Crabb, J. S., Sun, J., Rayborn, M. E., Nawrot, M., Saari, J. C., & Crabb, J. W. (2004). Support for a proposed retinoid-processing protein complex in apical retinal pigment epithelium. Experimental Eye Research, 79(3), 419-422. https://doi.org/10.1016/j.exer.2004.04.001