The extent of non-lethal release of lysosomal enzymes from phagocytosing neutrophils is suppressed by an increase in oxygen intermediates generated by stimulated neutrophils. We report that catalytic scavengers quenching these oxygen by-products improve the decreased enzyme release and that the degree of improvement is dependent on the scavenger types and on the dose response. The effects of 5 catalytic scavengers of the oxidative metabolites on the secretion of lysosomal enzymes and phagocytosis were assessed using the dose response by incubating normal human neutrophils with zymosan, ^<14>C-inulin and various ^1O^2 alone raised the release of α-mannosidase, β-glucuronidase and lysozymes in accordance with their concentrations, without enhancing the secretion of LDH, and lowered phagocytosis inversely proportional to their concentrations. Mannitol which quenches OH alone was slightly effective on the increase of these enzymes and decrease of phagocytosis, whereas catalase which scavenges the H_2O_2 was almost ineffective. On the other hand, superoxide dismutase (SOD) which converts O_2-to H_2O_2, at low concentrations (150-300U/ml) rather inhibited, while at higher concentration (above 600U/ml), it potentiated, enzyme release. Superoxide dismutase at low concentrations enhanced, while at higher concentrations it lowered phagocytosis.
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