Abstract
The normal bactericidal response of human neutrophils (PMN) involves cell stimulation, followed by a respiratory burst which results from the activation of NADPH oxidase. This multicomponent electron transport chain transfers electrons from intracellular NADPH to extra-cellular oxygen, reducing molecular oxygen to superoxide. This latter product is rapidly converted to hydrogen peroxide and toxic free radicals (1). Activated PMN also release lysosomal proteases and adhere to the endothelial surface, the cells of which can be severely damaged by the secretion of these toxic products if the local cytotoxic response escalates into a systemic process. Indeed, the microvascular collapse, characterisic of pathologies such as shock, asthma, ischemia and graft rejection, may be partially mediated by dysregulation of PMN functions.
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© 1990 Plenum Press, New York
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Paubert-Braquet, M., Hosford, D., Koltz, P., Guilbaud, J., Braquet, P. (1990). Two Structurally Unrelated PAF Antagonists, BN 52021 and BN 52111, Partially Inhibit TNF-Induced Superoxide Release by Human Neutrophils. In: de Paulet, A.C., Douste-Blazy, L., Paoletti, R. (eds) Free Radicals, Lipoproteins, and Membrane Lipids. NATO ASI Series, vol 189. Springer, New York, NY. https://doi.org/10.1007/978-1-4684-7427-5_4
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DOI: https://doi.org/10.1007/978-1-4684-7427-5_4
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