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Isolation and characterization of cDNA clones encoding aldose reductase
1Department of Ophthalmology, Washington University School of Medicine, St Louis, MO 63110.
Current Eye Research
|October 1, 1989
Summary
Researchers isolated and characterized bovine lens aldose reductase (AR) cDNA. This enzyme is crucial in diabetic complications, and understanding its genetic structure provides insight into its function.
Area of Science:
- Biochemistry
- Molecular Biology
- Genetics
Background:
- Aldose reductase (AR) plays a role in diabetic complications, particularly in the visual system.
- The genetic structure and functional organization of aldose reductase genes are not well understood.
Purpose of the Study:
- To isolate and characterize complementary DNA (cDNA) clones encoding bovine lens aldose reductase.
- To determine the nucleotide sequence and deduce the amino acid sequence of bovine lens aldose reductase.
Main Methods:
- Isolation and characterization of complementary DNA (cDNA) clones from bovine lens.
- Nucleotide sequencing of four independently isolated aldose reductase cDNA clones.
- Sequence analysis to determine the composite cDNA sequence and deduce the primary amino acid structure.
Main Results:
- A composite cDNA sequence of 1154 nucleotides was established.
- The cDNA encodes a 296-amino acid primary structure for bovine lens aldose reductase.
- The deduced amino acid sequence exhibits high homology to rat lens aldose reductase and similarities to human liver aldehyde reductase and frog lens rho-crystallin.
Conclusions:
- The study provides the first detailed characterization of bovine lens aldose reductase cDNA.
- The findings offer insights into the structure and potential function of aldose reductase in the context of diabetic complications.
- Comparative sequence analysis highlights evolutionary conservation and potential functional relationships with related enzymes.