In the presence of 10−8 M concentrations of the aldose reductase inhibitor AL 1576, there is a 20-30% increase in the rate of hydrolysis of near-saturating concentrations of ATP by bovine renal Na+-K+-ATPase. When bovine renal Na+-K+-ATPase is reacted with glucose 6-phosphate in the presence of 10−8 M concentrations of AL 1576 or 10−6 M concentrations of a second aldose reductase inhibitor, sorbinil, glucosylation occurs. Whereas sorbinil has no effect on ATP hydrolysis by the glucosylated Na+-K+-ATPase, 10−8 M AL 1576 causes a shift in the kinetics of hydrolysis of ATP from substrate inhibition to normal substrate activation. The aldose reductase inhibitors interact with the enzyme at the low-affinity ATP-binding site.
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Original Contributions| June 01 1987
Direct Stimulation of Na+-K+-ATPase and Its Glucosylated Derivative By Aldose Reductase Inhibitor
Margaret H Garner;
Address correspondence and reprint requests to Dr. Abraham Spector, Dept. of Ophthalmology, Columbia University, 630 West 168th Street, New York, NY 10032.
Margaret H Garner, Abraham Spector; Direct Stimulation of Na+-K+-ATPase and Its Glucosylated Derivative By Aldose Reductase Inhibitor. Diabetes 1 June 1987; 36 (6): 716–720. https://doi.org/10.2337/diab.36.6.716
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