3H]Ouabain binding to human erythrocytes in protein-énergy malnutrition.

Abstract

[3H]Ouabain binding to erythrocytes was determined in normal children and in children suffering from kwashiorkor or marasmus. Scatchard plot analysis of [3H]ouabain binding displayed straight lines with linear slopes in all subjects indicating the presence of a single species of ouabain binding sites on erythrocytes. The number of ouabain binding sites per cell was 385 +/- 26 (mean +/- SEM, n = 3) in normal, 891 +/- 102 (n = 8) (p less than 0.001) in kwashiorkor and 316 +/- 45 (n = 3) in marasmic children. The equilibrium dissociation constant (Kd) for ouabain binding in kwashiorkor (16 nmol/1) was similar to that in control (12 nmol/1). The specific activity of Na+, K+ -ATPase of erythrocyte membrane has been shown to be higher in kwashiorkor children as compared to normal children [3]. This increase in enzyme activity may be considered as a consequence of increase in the enzyme content as indicated by the increased number of ouabain binding sites on red cells. Elevation in the level and activity of erythrocyte Na+, K+ -ATPase in kwashiorkor might represent a compensatory mechanism in response to a primary membrane abnormality, to effect prevention of Na+ accumulation and K+ depletion inside the cell.