Lactate formation and glyoxalase activity in normal and leukemic human leukocytes in vitro.

In their review of the carbohydrate metabolism of leukocytes, Beck and Valentine (4) stated that normal myeloid leukocytes possess a high rate of aerobic glycolysis. Various reports (8, 9, 11) have indicated that, quantitatively, leukocytes from persons with leukemia do not have this capacity to make lactic acid aerobically. However, leukemic leukocytes seem to possess an anaerobic glycolysis, since incubation of such cells in an atmosphere of nitrogen increases the yield of lactic acid (5, 9, 11). On the other hand, normal, polymorphonuclear granulocytes do not exhibit this Pasteur effect (9). No explanation is available for the different metabolic characteristics of the normal and leukemic leukocyte. The data reported in this paper indicate a difference between normal and leukemic leukocytes in the activity of a specific enzyme, glyoxalase. If methylglyoxal is the precursor of lactic acid in leukocytes, 1 then (since glyoxalase catalyzes the conversion of methylglyoxal to lactic acid [8]) the observed difference in enzyme activity between normal and leukemic leukocytes might account for the variation in their abilities to form lactic acid aerobically.