Abstract
It was shown for the first time that myeloperoxidase, a homodimer that consists of two disulfidebonded identical protomers and catalyzes the formation of hypochlorous acid (HOCl), is decomposed by HOCl into monomers (MPO-Cl). Dimeric myeloperoxidase can also be converted into monomers (hemimyeloperoxidase) by reduction of the disulfide bond. In this study, the effects of two monomeric forms of myeloperoxidase, MPO-Cl and hemi-myeloperoxidase, and native dimeric myeloperoxidase on the production of reactive oxygen (•O 2 − and H2O2) and halogen (HOCl) species by neutrophils were compared. Neutrophil production of these species was monitored after addition of hemi-myeloperoxidase, MPO-Cl, or dimeric myeloperoxidase and also after the subsequent addition of activators, phorbol-12-myristate-13-acetate or N-formyl-Met-Leu-Phe. HOCl production was assessed by chemiluminescence in the presence of luminol; •O 2 − production was assessed by chemiluminescence in the presence of lucigenin and by cytochrome c reduction determined spectrophotometrically, and H2O2 production was measured using fluorimetry with scopoletin. The results indicate that MPO-Cl and hemi-myeloperoxidase, which can occur in blood under halogenative stress, do not prime neutrophil NADPH oxidase, and do not enhance the production of reactive oxygen (•O 2 − and H2O2) and halogen (HOCl) species.
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