Neutrophils exposed to bacterial lipopolysaccharide upregulate NADPH oxidase assembly

The Journal of Clinical Investigation
F R DeLeoW M Nauseef

Abstract

Bacterial LPS is a pluripotent agonist for PMNs. Although it does not activate the NADPH-dependent oxidase directly, LPS renders PMNs more responsive to other stimuli, a phenomenon known as "priming." Since the mechanism of LPS-dependent priming is incompletely understood, we investigated its effects on assembly and activation of the NADPH oxidase. LPS pretreatment increased superoxide (O2-) generation nearly 10-fold in response to N-formyl methionyl leucyl phenylalanine (fMLP). In a broken-cell O2--generating system, activity was increased in plasma membrane-rich fractions and concomitantly decreased in specific granule-rich fractions from LPS-treated cells. Oxidation-reduction spectroscopy and flow cytometry indicated LPS increased plasma membrane association of flavocytochrome b558. Immunoblots of plasma membrane vesicles from LPS-treated PMNs demonstrated translocation of p47-phox but not of p67-phox or Rac2. However, PMNs treated sequentially with LPS and fMLP showed a three- to sixfold increase (compared with either agent alone) in plasma membrane-associated p47-phox, p67-phox, and Rac2, and translocation paralleled augmented O2- generation by intact PMNs. LPS treatment caused limited phosphorylation of p47-phox, and plas...Continue Reading

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Citations

Oct 19, 2012·Inflammation Research : Official Journal of the European Histamine Research Society ... [et Al.]·Georg SingerD Neil Granger
Nov 15, 2011·Seminars in Immunopathology·Kevin M Rigby, Frank R DeLeo
Dec 11, 2008·Immunologic Research·Adam D Kennedy, Frank R DeLeo
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Nov 14, 2003·Microbes and Infection·Scott D KobayashiFrank R DeLeo
Jan 18, 2003·Experimental Cell Research·Johan BylundAnna Karlsson
Mar 10, 2001·Progress in Neurobiology·C Eder, T E DeCoursey
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