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J. Biol. Chem., Vol. 276, Issue 24, 21098-21104, June 15, 2001
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From the Vertebrate opsins in both photoreceptors and the
retinal pigment epithelium (RPE) have fundamental roles in the visual
process. The visual pigments in photoreceptors are bound to
11-cis-retinal and are responsible for the initiation of
visual excitation. Retinochrome-like opsins in the RPE are bound to
all-trans-retinal and play an important role in chromophore
metabolism. The retinal G protein-coupled receptor (RGR) of the RPE and
Müller cells is an abundant opsin that generates
11-cis-retinal by stereospecific photoisomerization of its
bound all-trans-retinal chromophore. We have analyzed a 32-kDa protein (p32) that co-purifies with bovine RGR from RPE microsomes. The co-purified p32 was identified by mass spectrometric analysis as 11-cis-retinol dehydrogenase (cRDH), and
enzymatic assays have confirmed the isolation of an active cRDH. The
co-purified cRDH showed marked substrate preference to
11-cis-retinal and preferred NADH rather than NADPH as the
cofactor in reduction reactions. cRDH did not react with endogenous
all-trans-retinal bound to RGR but reacted specifically
with 11-cis-retinal that was generated by
photoisomerization after irradiation of RGR. The reduction of
11-cis-retinal to 11-cis-retinol by cRDH
enhanced the net photoisomerization of all-trans-retinal
bound to RGR. These results indicate that cRDH is involved in the
processing of 11-cis-retinal after irradiation of RGR opsin
and suggest that cRDH has a novel role in the visual cycle.
Interaction of 11-cis-Retinol Dehydrogenase with the
Chromophore of Retinal G Protein-coupled Receptor Opsin*
, Center for Craniofacial Molecular Biology,
University of Southern California School of Dentistry and
¶ Departments of Ophthalmology and Microbiology, University of
Southern California School of Medicine and Doheny Eye Institute, Los
Angeles, California 90033 and § Beckman Research Institute
of the City of Hope, Duarte, California 91010
*
This work was supported in part by grants from the Hoover
Foundation (to H. K. W. F.) and National Institutes of Health Grants EY03040 and EY08364 (to H. K. W. F.) and RR06217 and CA33752 (to T. D. L.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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