December 2002
Volume 43, Issue 13
Free
ARVO Annual Meeting Abstract  |   December 2002
11-cis Retinol Dehydrogenase Activity in the Cone-Dominant Retina
NL Mata; JS Lee; RS Clemmons; RA Radu; GH Travis
Author Affiliations & Notes
  • NL Mata
    Jules Stein Eye Institute UCLA School of Medicine Los Angeles CA
  • JS Lee
    Jules Stein Eye Institute UCLA School of Medicine Los Angeles CA
  • RS Clemmons
    Jules Stein Eye Institute UCLA School of Medicine Los Angeles CA
  • RA Radu
    Jules Stein Eye Institute UCLA School of Medicine Los Angeles CA
  • GH Travis
    Jules Stein Eye Institute UCLA School of Medicine Los Angeles CA
  • Footnotes
    Commercial Relationships   N.L. Mata, None; J.S. Lee, None; R.S. Clemmons, None; R.A. Radu, None; G.H. Travis, None. Grant Identification: Support: NIH Grant EY11713
Investigative Ophthalmology & Visual Science December 2002, Vol.43, 3609. doi:
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      NL Mata, JS Lee, RS Clemmons, RA Radu, GH Travis; 11-cis Retinol Dehydrogenase Activity in the Cone-Dominant Retina . Invest. Ophthalmol. Vis. Sci. 2002;43(13):3609.

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Abstract

Abstract: : Purpose: Electrophysiological investigations of visual pigment regeneration have previously documented the unique ability of bleached cone photoreceptors to regain light sensitivity upon addition of 11-cis retinol (11c ROL). These findings provide indirect evidence for the existence of an 11-cis retinol dehydrogenase (11c RDH) activity within cone photoreceptors. To explore this possibility, we have characterized the dinucleotide and retinoid substrate specificities for dehydrogenase activities in rod- and cone-dominant retinal tissues. Methods: Membranes were prepared from retina and retinal pigment epithelium (RPE) of rod-dominant cattle and cone-dominant chicken and ground squirrel. These preparations were used in enzymatic assays with chemically defined dinucleotide and retinoid stereoisomers to study the substrate specificities and catalytic activities. Results: RPE membranes from each species examined demonstrated similar dinucleotide (pro-S-NAD) and retinoid (pro-S-11c ROL) specificities for production of 11-cis retinal (11c RAL). Rates of 11c RAL production from the three RPE preparations were also similar (0.4 - 0.6 nmole/min/mg). No redox activity for all-trans retinol or all-trans retinaldehyde (at RAL) was detectable. In retinal membranes from the three species, reduction of at RAL had pro-S dinucleotide and pro-S retinoid specificity as previously reported. The catalytic rates were also similar (5 - 10 nmole/min/mg). No redox activity for 11c ROL or 11c RAL was detectable in bovine retinal membranes. However, chicken and ground squirrel retinal membranes contained a pronounced pro-S-NADP/pro-R-11c ROL-specific dehydrogenase activity. Conclusion: The presence of 11c RDH activity in two cone-dominant retinas corroborates earlier electrophysiologic data indicating that cone photoreceptors utilize 11c ROL to regenerate visual chromophore. Moreover, the unique dinucleotide and retinoid substrate specificities of this "cone-specific" 11c RDH distinguish it from 11c RDH in the RPE and provide further support for an alternate biochemical route of visual-chromophore biosynthesis in cones.

Keywords: 399 enzymes/enzyme inhibitors • 554 retina • 567 retinal pigment epithelium 
© 2002, The Association for Research in Vision and Ophthalmology, Inc., all rights reserved. Permission to republish any abstract or part of an abstract in any form must be obtained in writing from the ARVO Office prior to publication.
Copyright © 2025 Association for Research in Vision and Ophthalmology.
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