The NADPH oxidase-dependent hemolysis of sheep erythrocytes with the membrane fraction of guinea pig peritoneal macrophages.
As previously reported, the membrane fraction of liquid paraffin-induced, guinea pig peritoneal macrophages exhibits an NADPH-dependent hemolytic activity toward sheep erythrocytes. This activity was inhibited with N-ethylmaleimide, superoxide dismutase, cytochrome c, catalase, desferrioxamine, mannitol, and benzoate. These inhibition profiles indicate that O2- generation by the NADPH oxidase, peroxidation of the membranous lipids with H2O2 or .OH secondarily formed from O2-, and hemolysis of sheep erythrocytes with the peroxides occur in this order in the hemolytic reaction. In fact, the lipid peroxides were found to be formed in the membrane fraction in the presence of Fe3+, subsequent to the O2- generation, and to act as a final hemolytic agent.
Nakamura
T
T
Department of Hygienic Chemistry, Faculty of Pharmaceutical Sciences, Hokkaido University.
Goto
M
M
Koyama
J
J
D000818:Animals; D002462:Cell Membrane / Q000502:physiology; D005290:Ferric Compounds / Q000494:pharmacology; D006168:Guinea Pigs; D006461:Hemolysis; D008054:Lipid Peroxides / Q000378:metabolism; D008264:Macrophages / Q000502:physiology*; D009247:NADH, NADPH Oxidoreductases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D019255:NADPH Oxidases; D010529:Peritoneal Cavity / Q000166:cytology; D012756:Sheep
D005290:Ferric Compounds; D008054:Lipid Peroxides; D009247:NADH, NADPH Oxidoreductases; D019255:NADPH Oxidases