The phagocytosis-associated stimulation of glucose-1-14C oxidation by rat polymorphonuclear leukocytes is markedly inhibited by 0.1 mm N-ethylmaleimide, which does not appreciably affect resting cell glucose-1-14C oxidation, glucose uptake, or lactic acid production. One millimolar KCN, 1 mm sodium azide, and 50 mm 3-amino-1H-1,2,4-triazole increase the particle-stimulated activity of the hexose monophosphate shunt. Hydrogen peroxide, either generated enzymatically by d-amino acid oxidase plus d-alanine or added directly, stimulates leukocyte direct oxidation of glucose, and this stimulation is enhanced by KCN and sodium azide and inhibited by N-ethylmaleimide. Hydrogen peroxide-dependent irreversible inhibition of catalase by 3-amino-1H-1,2,4-triazole is increased in rat leukocytes following polystyrene ingestion. Rat polymorphonuclear leukocytes contain a KCN-insensitive glutathione peroxidase and a NADPH-specific glutathione reductase. Fortified 105,000 x g supernatants of rat leukocytes rapidly reduce oxidized glutathione or glutathione which has been oxidized by the addition of hydrogen peroxide and exhibit a concomitant increase of glucose-1-14C oxidation. The data indicate that both phagocytosis and hydrogen peroxide stimulate rat leukocyte hexose monophosphate shunt activity, and similar effects of inhibitors on these two processes suggests that endogenously generated hydrogen peroxide may stimulate the direct oxidation of glucose in phagocytizing cells.
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Peter Reed (1969) studied this question.