对视网膜色素上皮顶端一种拟议的类视黄醇加工蛋白复合物的支持。

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

作者信息

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

出版信息

Exp Eye Res. 2004 Sep;79(3):419-22. doi: 10.1016/j.exer.2004.04.001.

DOI:10.1016/j.exer.2004.04.001

PMID:15336505

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.

摘要

细胞视黄醛结合蛋白（CRALBP）与视网膜色素上皮（RPE）微粒体中的ERM（埃兹蛋白、根蛋白、膜突蛋白）结合磷蛋白50（EBP50）之间的相互作用，引发了一种假说，即类视黄醇加工蛋白复合物存在于RPE顶端。在包被有麦胚凝集素的琼脂糖珠上分离出小鼠RPE顶端突起。对分离出的RPE顶端进行蛋白质组学分析，结果显示存在CRALBP、EBP50、11-顺式视黄醇脱氢酶、细胞视黄醇结合蛋白1和光感受器间类视黄醇结合蛋白。这些结果支持了一种假说，即视觉循环蛋白复合物可能在RPE顶端11-顺式类视黄醇的定位和释放中发挥作用。