Journal article
Human neutrophil antimicrobial activity
Reviews of infectious diseases, v 10 Suppl 2(Supplement 2), pp S450-S456
Jul 1988
PMID: 3055215
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
Polymorphonuclear neutrophilic leukocytes (PMNs) take up opsonized microorganisms into phagosomes that fuse with secretory granules in the PMN cytoplasm to form phagolysosomes. Killing and digestion of microorganisms take place within phagolysosomes. Antimicrobial activities in phagolysosomes are divided into two classes. Oxygen (O2)-dependent mechanisms are expressed when PMNs undergo the "respiratory burst." An NADPH oxidase in the phagolysosome membrane is activated and reduces O2 to superoxide (O2-). O2 reduction is the first step in a series of reactions that produce toxic oxidants. For example, .O2- dismutases to hydrogen peroxide (H2O2), and the azurophil granule enzyme myeloperoxidase catalyzes the oxidation of Cl- by H2O2 to yield hypochlorous acid (HOCl). The reaction of HOCl with ammonia and amines modulates the toxicity of this oxidant. O2-independent antimicrobial mechanisms include the activities of lysosomal proteases, other hydrolytic enzymes, and proteins and peptides that bind to microorganisms and disrupt essential processes or structural components. For example, the bactericidal/permeability-increasing protein, cathepsin G, and the defensins are released into phagolysosomes from the azurophil granules. Proposed mechanisms of action of neutrophil antimicrobial agents, their range of microbial targets, and their possible interactions within phagolysosomes are discussed.
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Details
- Title
- Human neutrophil antimicrobial activity
- Creators
- E L Thomas - St. Jude Children's Research HospitalR I Lehrer - St. Jude Children's Research HospitalR F Rest - St. Jude Children's Research Hospital
- Publication Details
- Reviews of infectious diseases, v 10 Suppl 2(Supplement 2), pp S450-S456
- Publisher
- Oxford University Press
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- [Retired Faculty]
- Web of Science ID
- WOS:A1988P836900042
- Scopus ID
- 2-s2.0-0024043988
- Other Identifier
- 991019184096304721
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- Collaboration types
- Domestic collaboration
- Web of Science research areas
- Immunology
- Microbiology