Oxygen Independent Microbicidal Mechanisms of Human Polymorphonuclear Leukocytes

  • John K. Spitznagel
  • Noburu Okamura
Conference paper
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 162)


Human polymorphonuclear leukocytes (PMN) have several antimicrobial systems that can be viewed as belonging to two groups. One group depends upon oxidative processes. These include the superoxide anion (O2-), the myeloperoxidase-chloride-hydrogen peroxide system (MPHCl), and free hydroxyl radicals (•OH) (1). The other group (Table 1) functions independently of oxidative processes and includes increased hydrogen ion concentrations, various cationic proteins, cathepsin G, lysozyme, and apolactoferrin (2). The oxidative bactericidal processes are complex and depend upon soluble enzymes or cofactors present in the cytosol and upon enzymes located on or in membranes. The nonoxidative processes appear to depend solely upon proteins found within the PMN granules (3). Although there is indirect evidence that favors the dominance under various conditions of one or the other of these antimicrobial systems, it is unclear, at present, which
Table 1

Oxygen Independent Antibacterial Components

Cationic Proteins


Cathepsin G

Other Azuorphil Granule Proteins



mechanisms are mainly responsible for, or crucial in, the bactericidal activity of PMN in the various environments found in the body. For example, accumulating evidence suggests that oxygen-independent antimicrobial systems operate in vivo in human PMN as well as in those of chickens and rabbits (2).Table mechanisms are mainly responsible for, or crucial in, the bactericidal activity of PMN in the various environments found in the body. Fo example, accumulating evidence suggests that oxygenindependent antimicrobial systems operate in vivo in human PMN as well as in those of chickens and rabbits (2).


Chronic Granulomatous Disease Anaerobic Chamber Granule Protein Human Polymorphonuclear Leukocyte Opsonized Zymosan 
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Copyright information

© Plenum Press, New York 1983

Authors and Affiliations

  • John K. Spitznagel
    • 1
    • 2
  • Noburu Okamura
    • 1
    • 2
  1. 1.Emory University School of MedicineAtlantaUSA
  2. 2.Tokyo Medical and Dental University School of MedicineTokyoJapan

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