Abstract
The human aldose reductase gene has been cloned by screening a human placental cDNA library with antibodies against bovine lens aldose reductase. The nucleotide sequence of the entire coding region has been determined. The deduced amino acid sequence indicates that the human enzyme is 84% identical to the bovine lens aldose reductase and 85% identical to the rat lens aldose reductase. It is also very similar to the human aldehyde reductase, the bovine prostaglandin F synthase, and to the European common frog rho-crystallin. The deduced amino acid sequence also indicates that maturation of aldose reductase involves removal of the N-terminal methionine.
Highlights
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Library constructed in Xgtll vector was purchased from Clonetech (Palo Alto, CA).The library was screened with anti-bovine lens aldose reductase antibodies
University of Illinois at Chicago) according to the protocol suggested by Clonetech
Summary
The deduced amino acid sequence indicates that the human enzyme is 84%identical to the bovine lens aldose reductase and 85%identical to the rat lens aldose reductase. Aldose reductase has been implicated to be involved in the regulation of cellular osmotic pressure in these tissues. In diabetic patients where the blood sugar level is high, this enzyme has been implicated to be involved in some of the clinical complications such ascataract formation(Kinoshita, 1974), retinopathy (Buzney et al, 1977),neuropathy (Gabbay, 1973),and possibly kidney failure (Corder et al, 1979).Treatment with inhibitors of aldose reductase alleviates some of these symptoms (Kinoshita, 1974;Tomlinson et al.,1982;Judzewitsch et al, 1983). One hypothesis is that in the hyperglycemic patients,the aldose reductase activity increases cellular osmotic pressure, leading to swelling of the cells, and insome yet undetermined fashion, causes some of these clinical complications. We describe the cloning and sequence determination of this gene and discuss its homology with a family of related proteins
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