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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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

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.[1]

References

  1. Support for a proposed retinoid-processing protein complex in apical retinal pigment epithelium. 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. Exp. Eye Res. (2004) [Pubmed]
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