Published online before print February 2, 2005
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Department of Medicine, University of Washington, Seattle
@ To whom correspondence should be addressed. E-mail: seym{at}u.washington.edu.
Neutrophilic polymorphonuclear leukocytes (neutrophils) are highly specialized for their primary function, the phagocytosis and destruction of microorganisms, which when coated with opsonins (generally complement and/or antibody), bind to specific receptors on the surface of the phagocyte. Invagination of the cell membrane occurs with the incorporation of the microorganism into an intracellular phagosome. There follows a burst of oxygen consumption, and much, if not all, of the extra oxygen consumed is converted to highly reactive oxygen species. In addition, the cytoplasmic granules discharge their contents into the phagosome, and death of the ingested microorganism soon follows. Among the antimicrobial systems formed in the phagosome is one consisting of myeloperoxidase (MPO), released into the phagosome during the degranulation process, hydrogen peroxide (H2O2), formed by the respiratory burst and a halide, particularly chloride. The initial product of the MPO-H2O2-chloride system is hypochlorous acid, and subsequent formation of chlorine, chloramines, hydroxyl radicals, singlet oxygen, and ozone is proposed. These same toxic agents can be released to the outside of the cell, where they may attack normal tissue and thus contribute to the pathogenesis of disease. This review will consider the potential sources of H2O2 for the MPO-H2O2-halide system; the toxic products of the MPO system; the evidence for MPO involvement in the microbicidal activity of neutrophils; the involvement of MPO-independent antimicrobial systems; and the role of the MPO system in tissue injury. It is concluded that the MPO system plays an important role in the microbicidal activity of phagocytes.
Key Words: neutrophil microbicidal activity • hypochlorous acid • hydrogen peroxide • myeloperoxidase-mediated antimicrobial system • MPO-independent antimicrobial systems • MPO deficiency
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I. C. Cavalcante, M. V. Castro, A. R. F. Barreto, G. W. Sullivan, M. Vale, P. R. C. Almeida, J. Linden, J. M. Rieger, F. Q. Cunha, R. L. Guerrant, et al. Effect of Novel A2A Adenosine Receptor Agonist ATL 313 on Clostridium difficile Toxin A-Induced Murine Ileal Enteritis Infect. Immun., May 1, 2006; 74(5): 2606 - 2612. [Abstract] [Full Text] [PDF]
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S. Baldus, V. Rudolph, M. Roiss, W. D. Ito, T. K. Rudolph, J. P. Eiserich, K. Sydow, D. Lau, K. Szocs, A. Klinke, et al. Heparins Increase Endothelial Nitric Oxide Bioavailability by Liberating Vessel-Immobilized Myeloperoxidase Circulation, April 18, 2006; 113(15): 1871 - 1878. [Abstract] [Full Text] [PDF]
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S. D. Kobayashi, J. M. Voyich, A. R. Whitney, and F. R. DeLeo Spontaneous neutrophil apoptosis and regulation of cell survival by granulocyte macrophage-colony stimulating factor J. Leukoc. Biol., December 1, 2005; 78(6): 1408 - 1418. [Abstract] [Full Text] [PDF]
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D. Morgan, V. V. Cherny, R. Murphy, B. Z. Katz, and T. E. DeCoursey The pH dependence of NADPH oxidase in human eosinophils J. Physiol., December 1, 2005; 569(2): 419 - 431. [Abstract] [Full Text] [PDF]
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V. F. Ximenes, S. d. O. Silva, M. R. Rodrigues, L. H. Catalani, G. J. Maghzal, A. J. Kettle, and A. Campa Superoxide-dependent Oxidation of Melatonin by Myeloperoxidase J. Biol. Chem., November 18, 2005; 280(46): 38160 - 38169. [Abstract] [Full Text] [PDF]
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