| Project/Area Number |
10671629
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Ophthalmology
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| Research Institution | HIROSAKI UNIVERSITY |
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Principal Investigator |
ISHIGURO Sei-ichi Hirosaki Univ., Dept. Agri. Life Sci., Prof., 農学生命科学部, 教授 (20111271)
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| Project Period (FY) |
1998 – 1999
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| Project Status |
Completed (Fiscal Year 1999)
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| Budget Amount *help |
¥100,000 (Direct Cost: ¥100,000)
Fiscal Year 1999: ¥100,000 (Direct Cost: ¥100,000)
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| Keywords | 11-cis-retinol / all-trans-retinol / isomerization / rod outer segment / rhodopsin / phospholipids / visual cycle |
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| Research Abstract |
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 connecting with fluorescence spectrophotometer. Isomerization of 11-cis-retinol to all-trans-retinol was observed in the presence of ROS. This isomerization was heat- stable and did not have the 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 RCS but phospholipids did not. On the contrary, 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 the activity of 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.
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