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Papers In Press, published online ahead of print November 29, 2001
Department of Pharmacology, University of Illinois at Chicago, College of Medicine, Chicago, IL 60612
Corresponding Author: jiefan{at}uic.edu
In this study, we explored a novel function of polymorphonuclear neutrophils (PMN) NAD(P)H oxidase in the mechanism of TNFa-induced NF-kB activation and ICAM-1 expression in endothelial cells. Studies were made in mice lacking p47phox subunit of NAD(P)H oxidase as well as in cultured mouse lung vascular endothelial cells (MLVEC) from these mice. In response to TNFa challenge, NF-kB activation and ICAM-1 expression were significantly attenuated in lungs of p47phox-/- mice as compared to wild-type (WT) mice. The attenuation of NF-kB activation in p47phox-/- mice was secondary to inhibition of NIK activity and subsequent IkBa degradation. Induction of neutropenia using anti-PMN serum prevented the initial TNFa-induced NF-kB activation and ICAM-1 expression in WT mice, indicating the involvement of PMN NAD(P)H oxidase in signaling these responses. Moreover, the responses were restored upon repletion with PMN obtained from WT mice but not with PMN from p47phox-/- mice. These findings were recapitulated in MLVEC co-cultured with PMN, suggesting that NF-kB activation and resultant ICAM-1 expression in endothelial cells occurred secondary to oxidants generated by the PMN NAD(P)H oxidase complex. The functional relevance of the PMN NAD(P)H oxidase in mediating TNFa-induced ICAM-1-dependent endothelial adhesivity was evident by markedly reduced adhesion of p47phox-/- PMN in co-cultured experiments. Thus, oxidant signaling by the PMN NAD(P)H oxidase complex is an important determinant of TNFa-induced NF-kB activation and ICAM-1 expression in endothelial cells.
J. Biol. Chem, 10.1074/jbc.M110054200
Submitted on October 18, 2001
Revised on November 12, 2001
Accepted on November 29, 2001
Role of neutrophil NADPH oxidase in the mechanism of TNFa-induced NF-kB activation and ICAM-1 expression in Endothelial cells
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