IOVS
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text (PDF)
Right arrow Submit a response
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Sato, S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Sato, S.

Investigative Ophthalmology & Visual Science, Vol 34, 3172-3178, Copyright © 1993 by Association for Research in Vision and Ophthalmology

ARTICLES AND REPORTS

Aldose reductase the major protein associated with naphthalene dihydrodiol dehydrogenase activity in rat lens

S Sato
Laboratory of Ocular Therapeutics, National Eye Institute, National Institutes of Health, Bethesda, Maryland 20892.

PURPOSE. Recent studies have indicated that certain aldose reductase inhibitors prevent the formation of cataracts in naphthalene-fed rats. The study was designed to investigate whether aldose reductase itself is involved in the metabolism of naphthalene in the lens and the mechanism of this cataract formation. METHODS. Aldose reductase was purified from whole rat lens using a series of chromatographic steps that include gel filtration, affinity chromatography, and chromatofocusing. The dehydrogenase activity of the purified enzyme was evaluated with 1,2-dihydro-1,2-dihydroxynaphthalene (naphthalene dihydrodiol) as substrate. The same dehydrogenase activity was also examined with the recombinant protein obtained from rat lens aldose reductase clone. RESULTS. Throughout the purification steps, dehydrogenase activity with naphthalene dihydrodiol as substrate coeluted with aldose reductase activity assayed with DL-glyceraldehyde as substrate. The purified aldose reductase, which appeared as a single band on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, displayed dehydrogenase activity with naphthalene dihydrodiol as a substrate similar to that observed with the crude extract from whole rat lens. Recombinant protein from rat lens aldose reductase clone also displayed dehydrogenase activity similar to that observed with purified rat lens aldose reductase. Both the reductase and dehydrogenase activities of purified aldose reductase were inhibited by aldose reductase inhibitors. However, inhibition of dehydrogenase activity was less than reductase activity. Aldehyde reductase, an another nicotinamide adenine dinucleotide phosphate-dependent reductase, also displayed dihydrodiol dehydrogenase activity with naphthalene dihydrodiol and this activity was also inhibited by aldose reductase inhibitors. CONCLUSIONS. Aldose reductase displays dehydrogenase activity in addition to reductase activity. In rat lens aldose reductase is a major protein associated with naphthalene dihydrodiol dehydrogenase activity. This suggests that aldose reductase is linked to 1,2-dihydroxynaphthalene formation in rat lens and the subsequent formation of cataracts in naphthalene-fed rats.


This article has been cited by other articles:


Home page
 Drug Metab. Dispos.Home page
K. Sugiyama, T.-C. L. Wang, J. T. Simpson, L. Rodriguez, P. F. Kador, and S. Sato
Aldose Reductase Catalyzes the Oxidation of Naphthalene-1,2-Dihydrodiol for the Formation of Ortho-Naphthoquinone
Drug Metab. Dispos., January 1, 1999; 27(1): 60 - 67.
[Abstract] [Full Text]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1993 by the Association for Research in Vision and Ophthalmology