Myeloperoxidase, heme enzyme of azurophilic granules in neutrophils, is released into the extracellular space in the inflammation foci. In neutrophils, it stimulates a dose-dependent release of lactoferrin (a protein of specific granules), lysozyme (a protein of specific and azurophilic granules), and elastase (a protein of azurophilic granules). 4-Aminobenzoic acid hydrazide, a potent inhibitor of peroxidase activity of myeloperoxidase, produced no effect on neutrophil degranulation. Using signal transduction inhibitors (genistein, methoxyverapamil, wortmannin, and NiCl2), we demonstrated that myeloperoxidase-induced degranulation of neutrophils resulted from enzyme interaction with the plasma membrane and depends on activation of tyrosine kinases, phosphatidylinositol 3-kinases (PI3K), and calcium signaling. Myeloperoxidase modified by oxidative/halogenation stress (chlorinated and monomeric forms of the enzyme) lost the potency to activate neutrophil degranulation.
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Translated from Byulleten’ Eksperimental’noi Biologii i Meditsiny, Vol. 161, No. 4, pp. 483-488, April, 2016
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Grigorieva, D.V., Gorudko, I.V., Sokolov, A.V. et al. Myeloperoxidase Stimulates Neutrophil Degranulation. Bull Exp Biol Med 161, 495–500 (2016). https://doi.org/10.1007/s10517-016-3446-7
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DOI: https://doi.org/10.1007/s10517-016-3446-7