Abstract
The neutrophil is an important component of the innate immune system responsible for host defense. In this regard, it has a dual function: to destroy pathogenic microorganisms and to remove inflammatory debris. This functional role is achieved through a series of rapid and coordinated responses that include chemotaxis, phagocytosis, and intracellular killing of invading microorganisms. The latter is accomplished by release of a variety of microbicidal enzymes and cationic proteins contained in granules (exocytosis) and by production of reactive oxygen intermediates by the NADPH oxidase [1, 2]. In certain situations however, these toxic compounds can injure host tissues as is believed to occur in disorders characterized by inflammatory damage such as rheumatoid arthritis [3], inflammatory bowel disease [4, 5], and acute lung injury [6–8]. Thus to maintain homeostasis and minimize tissue damage, leukocyte microbicidal responses must be precisely regulated by processes including selective triggering and rapid termination of activation cascades once the initial stimulus has been removed. Currently the mechanisms which regulate neutrophil activation are incompletely understood.
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Kruger, J., Fukushima, T., Downey, G.P. (2001). Identification and Characterization of Protein Tyrosine Phosphatases Expressed in Human Neutrophils. In: Baue, A.E., Berlot, G., Gullo, A., Vincent, JL. (eds) Sepsis and Organ Dysfunction. Springer, Milano. https://doi.org/10.1007/978-88-470-2229-4_9
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DOI: https://doi.org/10.1007/978-88-470-2229-4_9
Publisher Name: Springer, Milano
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