Abstract
IT is now known that the phagocytic process in polymorphonuclear leucocytes (PMN) is accompanied by marked increases in the rates of oxygen consumption, glucose oxidation by the hexosemonophosphate shunt (HMPS) and oxidation of formate to carbon dioxide1–3. The energy for the phagocytic process seems to come from glycolysis1. The rate of glucose oxidation by the shunt in leucocytes seems to be regulated by the intracellular concentration of NADP (refs. 3 and 4). A suitable hypothesis for the enzyme basis underlying the metabolic stimulation in PMN during phagocytosis should therefore include a mechanism for the reoxidation of NADPH. Attempts have been made to correlate the stimulated activity of the hexosemonophosphate shunt in phagocytosing leucocytes with increased oxidation of NADPH. The evidence indicates that oxidation of NADPH in phagocytosing leucocytes is not accomplished by the classical route of hydrogen transport by way of cytochrome reductase and cytochrome c (ref. 1). Evans and Karnovsky5 have presented evidence for the existence in PMN cell extracts of an NADP-linked lactate dehydrogenase which is activated at low pH. Results obtained by Iyer, Islam and Quastel2 indicated that PMN possess an enzyme system capable of oxidizing NADPH and NADH by a reaction involving the formation of hydrogen peroxide. The enzyme, however, was found to bo much more active towards NADPH than NADH and its activity was strongly enhanced by manganese ions. Later Roberts and Quastel6 reported that the NADPH oxidase in PMN was probably peroxidase. Based on the available evidence, a mechanism was proposed to account for the metabolic changes observed in PMN during phagocytosis. This is seen as follows.
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References
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ROBERTS, J., CAMACHO, Z. Oxidation of NADPH by Polymorphonuclear Leucocytes during Phagocytosis. Nature 216, 606–607 (1967). https://doi.org/10.1038/216606a0
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DOI: https://doi.org/10.1038/216606a0
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