The role of myeloperoxidase and superoxide anion in the luminol- and lucigenin-dependent chemiluminescence of human neutrophils |
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Authors: | Paul Stevens Dickson Hong |
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Institution: | Department of Medicine, Division of Infectious Diseases, University of California at Los Angeles, Center for the Health Sciences, Los Angeles, California 90024 U.S.A. |
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Abstract: | The amount of chemiluminescence (CL) or light that is emitted from human polymorphonuclear leukocytes (PMN) during phagocytosis or activation by soluble stimuli is dependent on the emission of photons from the oxidation of particulate or bystander molecules. Because the compounds luminol and lucigenin yield photons with high quantum efficiency these agents have been introduced to sensitively assess PMN-CL. Since there is limited information about the pathways involved in the chemiluminescence of these compounds, we investigated the role of both myeloperoxidase (MPO) and superoxide anion (· O2?) in luminol-and lucigenin-PMN-CL. We compared the CL between normal and MPO- deficient PMN using zymosan for phagocytosis and N-formylmethionyleucylphenylalanine (FMLP) as a soluble stimulus. Our data demonstrated that luminol-CL was dependent on the presence of MPO and independent of · O2? generation during phagocytosis but independent of MPO during FMLP activation. In contrast lucigenin-CL was independent of MPO during both phagocytosis and FMLP activation and appeared to reflect · O2? production. Consequently, dependent on the type of activation, it appears that luminol- and lucigenin-CL are generated via different oxidative pathways and may serve as potentially useful tools to differentiate the redox activity of phagocytic cells. |
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