Changes in Na,K-adenosine triphosphatase (ATPase) concentration and Na,K-ATPase—Dependent adenosine triphosphate turnover in human erythrocytes in diabetes☆

Abstract 

The concentration of Na,K-adenosine triphosphatase (ATPase) and Na,K-ATPase-dependent adenosine triphosphate (ATP) turnover was measured in fasting blood samples of 20 subjects with insulin-dependent diabetes mellitus (IDDM), 22 subjects with non-insulin-dependent diabetes mellitus (NIDDM), and 20 nondiabetic subjects. [³H]ouabain binding was used to determine Na,K-ATPase concentration. There were 471 ± 70 (mean ± SD) ouabain binding sites per erythrocyte, normally distributed in the nondiabetic subjects. The number of ouabain sites per cell was lognormally distributed in the two populations of diabetic subjects. The mean of lognormal distributions of ouabain sites per cell was significantly lower in the IDDM group. The mean of the lognormal distribution for the NIDDM group was not significantly different from that of the nondiabetic subjects. Na,K-ATPase-dependent ATP turnover (molar activity) was 9,580 ± 742 mol/mol minute (mean ± SD) normally distributed in the nondiabetic population. A lognormal distribution was observed in the diabetic population. Means of the lognormal distributions were significantly different: 3.98 ± 0.05 for the nondiabetic population and 3.13 ± 0.48 for both diabetic populations. Changes in the concentration of Na,K-ATPase (ouabain sites per cell) and Na,K-ATPase-dependent ATP turnover did not correlate with hemoglobin A_1c (HbA_1c) or with blood glucose. This would suggest that elevated glucose concentrations do not directly cause decreased Na,K-ATPase function in the diabetic erythrocyte.

No full text is available. To read the body of this article, please view the PDF online.