Mechanisms of human neutrophil oxidant production after severe injury.

Autor: Quaid G; Department of Surgery, University of Cincinnati, College of Medicine, Cincinnati, Ohio 45267-0558, USA., Cave C, Williams MA, Hennigan RF, Bokoch G, Solomkin JS
Jazyk: angličtina
Zdroj: Surgery [Surgery] 2001 Oct; Vol. 130 (4), pp. 669-75; discussion 675-6.
DOI: 10.1067/msy.2001.116923
Abstrakt: Background: The purpose of this study was to determine the mechanisms of enhanced oxidant production after severe injury.
Methods: Neutrophils were harvested from patients within 24 hours of admission who had an injury severity score greater than 16. Nonadherent and adherent neutrophil oxidant production was measured after N-formyl-methionyl-leucyl-phenylalanine (fMLP) stimulation. Translocation of cytochrome b558 and cytosolic components p47phox and p67phox were determined by oxidation-reduction spectroscopy and immunoblotting, respectively. Flow cytometry measured integrin expression. Integrin and p47phox colocalization was examined by confocal microscopy.
Results: Eighteen patients were studied within 15 +/- 1.4 hours. Four women and 14 men suffered a blunt injury and had a mean injury severity score of 22 (range, 16 to 34). Nonadherent patient neutrophils showed a decrease in fMLP-stimulated oxidant production, whereas adherent neutrophil oxidant production was increased in both the vehicle control and fMLP-stimulated groups. Nicotinamide adenine dinucleotide phosphate (NADPH) oxidase components p47phox and cytochrome b558 were mobilized to the plasma membrane, whereas p67phox showed minimal change. Integrin CD11b a chain showed a significant increase in expression. Confocal microscopy showed colocalization of p47phox and a chain CD11b on the plasma membrane of patient neutrophils.
Conclusions: Colocalization of NADPH oxidase components and integrins may regulate the enhanced oxidant production in human neutrophils after severe injury.
Databáze: MEDLINE
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