Direct stimulation of Na+-K+-ATPase and its glucosylated derivative by aldose reductase inhibitor
- 1 June 1987
- journal article
- research article
- Published by American Diabetes Association in Diabetes
- Vol. 36 (6) , 716-720
- https://doi.org/10.2337/diabetes.36.6.716
Abstract
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.This publication has 12 references indexed in Scilit:
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