Accelerated decay of glucose 6-phosphate dehydrogenase activity in chronic granulomatous disease.

Abstract

Extract: Glucose 6-phosphate dehydrogenase (EG. 1.1.1.49) (Glc-6-PD) activity was measured in the lcukocytes and red cells of three patients with the classic form of chronic granulomatous discase (CGD) and in controls. Leukocyte homogenates from all three children revealed a decreased Glc-6-PD activity. The activities in both white cells and red cells, measured at timed intervals under conditions of storage at 0° or heating at 38° revealed a more rapid rate of decay in cells of patients than that seen in cells of control subjects. Studies measuring the activities of Glc-6-PD in the presence of 10 μM NADP, or 14 mM 2-mercaptoethanol, or both, disclosed a stabilizing effect with these reagents. Measurement of activity of another NADP-dependent enzyme, 6-phosphogluconic dehydrogenase (EC. 1.1.1.43) (6-PGD), in leukocytes were within normal limits. A correlation coefficient of 0.86 (P < 0.01) was found between Glc-6-Pd activity and the quantitative nitrobluc tetrazolium (NBT) test used to diagnose CGD. Speculation: An increased rate of decay in activity of glucose 6-phosphate dehydrogenase was detected in the leukocytes and red cells of patients with one form of chronic granulomatous disease. The finding of a functional abnormality in an X-linked enzyme is consonant with the known X-linked recessive mode of transmission of this form of the entity. The metabolic derangement involving leukocyte Glc-6-PD activity may provide a basis for the study of other abnormalities of the leukocyte, the socalled neutrophil dysfunction syndrome [7].