Luminol- and lucigenin-dependent chemiluminescence of neutrophils: role of degranulation.
The role of myeloperoxidase in luminol- and lucigenin-dependent chemiluminescence of stimulated human neutrophils has been investigated using purified myeloperoxidase and anti-(human myeloperoxidase) antiserum. This antiserum has been used as a specific enzyme inhibitor to assess myeloperoxidase-dependent neutrophil functions in single preparations of cells, thus overcoming the limitations inherent in other approaches using non-specific haem-inhibitors or myeloperoxidase-deficient neutrophils. The results show that luminol-dependent chemiluminescence is largely dependent on both oxidase activity and degranulation (of myeloperoxidase), while lucigenin monitors oxidase activity independently of the extent of degranulation. Since oxidase activation can occur in the absence of degranulation, assays utilizing luminol-dependent chemiluminescence to measure oxidant generation by stimulated neutrophils should include saturating levels of exogenous myeloperoxidase to overcome this problem.
D000166:Acridines; D003594:Cytoplasmic Granules / Q000378:metabolism*; D006801:Humans; D006861:Hydrogen Peroxide / Q000097:blood; D066298:In Vitro Techniques; D007840:Latex; D008163:Luminescent Measurements; D008165:Luminol; D008863:Microspheres; D009504:Neutrophils / Q000276:immunology* / Q000378:metabolism; D009195:Peroxidase / Q000037:antagonists & inhibitors / Q000097:blood*; D013481:Superoxides / Q000097:blood
D000166:Acridines; D007840:Latex; D013481:Superoxides; C033472:10,10'-dimethyl-9,9'-biacridinium; D008165:Luminol; D006861:Hydrogen Peroxide; D009195:Peroxidase