TAILIEUCHUNG - Báo cáo khoa học: An alternative isomerohydrolase in the retinal Muller cells of a cone-dominant species

Cone photoreceptors have faster light responses than rods and a higher demand for 11-cisretinal (11cRAL), the chromophore of visual pigments. RPE65 is the isomerohydrolase in the retinal pigment epithelium (RPE) that converts all-transretinyl ester to 11-cisretinol, a key step in the visual cycle for regenerating 11cRAL. | IFEBS Journal An alternative isomerohydrolase in the retinal Muller cells of a cone-dominant species Yusuke Takahashi1 Gennadiy Moiseyev2 Ying Chen2 Olga Nikolaeva2 and Jian-Xing Ma2 1 Department of Medicine Endocrinology Harold Hamm Oklahoma Diabetes Center University of Oklahoma Health Sciences Center Oklahoma City OK USA 2 Department of Physiology Harold Hamm Oklahoma Diabetes Center University of Oklahoma Health Sciences Center Oklahoma City OK USA Keywords cone-dominant retina isomerohydrolase Muller cell retinoids visual cycle Correspondence . Ma 941 Stanton L. Young Boulevard BSEB 328B Oklahoma City OK 73104 USA Fax 1 405 271 3973 Tel 1 405 271 4372 E-mail jian-xing-ma@ Received 26 January 2011 revised 20 May 2011 accepted 13 June 2011 doi Cone photoreceptors have faster light responses than rods and a higher demand for 11-cis retinal 11cRAL the chromophore of visual pigments. RPE65 is the isomerohydrolase in the retinal pigment epithelium RPE that converts all-trans retinyl ester to 11-cis retinol a key step in the visual cycle for regenerating 11cRAL. Accumulating evidence suggests that cone-dominant species express an alternative isomerase likely in retinal Muller cells to meet the high demand for the chromophore by cones. In the present study we describe the identification and characterization of a novel isomerohydro-lase RPE65c from the cone-dominant zebrafish retina. RPE65c shares 78 amino acid sequence identity with RPE-specific zebrafish RPE65a orthologue of human RPE65 and retains all of the known key residues for the enzymatic activity of RPE65. Similar to the other RPE-specific RPE65 RPE65c was present in both the membrane and cytosolic fractions used all-trans retinyl ester as its substrate and required iron for its enzymatic activity. However immunohistochemistry detected RPE65c in the inner retina including Muller cells but not in the RPE. Furthermore double-immunostaining of dissociated retinal .

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