Isomerization of 11-cis-retinol to all-trans-retinol in bovine rod outer segments.
It is known that exogenous 11-cis-retinol inhibits the recovery of photosensitivity of bleached rod outer segments (ROS) and 11-cis-retinol exists in the interphotorecepter matrix. We examined the conversion of 11-cis-retinol with bovine ROS. ROS was incubated with 11-cis-retinol under dim red light. Retinoids were extracted from the reaction mixture with hexane and analyzed by HPLC coupled with a fluorescence spectrophotometer. Isomerization of 11-cis-retinol to all-trans-retinol was observed in the presence of ROS. This isomerization was not suppressed by heat treatment and did not have stereospecificity. In addition, we incubated purified rhodopsin and phospholipids extracted from ROS with 11-cis-retinol. Rhodopsin was found to isomerize 11-cis-retinol to all-trans-retinol as well as ROS, but phospholipids did not. In contrast, the phospholipids inhibited the isomerization of 11-cis-retinol to all-trans-retinol by the purified rhodopsin. Commercially available phospholipids, especially phosphatidylserine, also inhibited the isomerization. Our results suggest that rhodopsin has activity for the isomerization of 11-cis-retinol to all-trans-retinol and may play an important role in the detoxification of 11-cis-retinol in the ROS.
Shimizu
T
T
Department of Ophthalmology, Tohoku University School of Medicine, Aoba-ku, Sendai 980-8574, Japan.
Ishiguro
S
S
Tamai
M
M
D000818:Animals; D002417:Cattle; D002851:Chromatography, High Pressure Liquid; D006358:Hot Temperature; D066298:In Vitro Techniques; D008027:Light; D010743:Phospholipids / Q000737:chemistry; D012243:Rhodopsin / Q000737:chemistry; D012374:Rod Cell Outer Segment / Q000378:metabolism* / Q000528:radiation effects; D013050:Spectrometry, Fluorescence; D013237:Stereoisomerism; D014801:Vitamin A / Q000737:chemistry / Q000378:metabolism* / Q000528:radiation effects
D010743:Phospholipids; D014801:Vitamin A; D012243:Rhodopsin