Circulation Research. 2001
Published online before print December 13, 2001, doi: 10.1161/hh0202.103615
Published online before print December 13, 2001, doi: 10.1161/hh0202.103615
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Submitted on July 17, 2001
Revised on December 3, 2001
Accepted on December 3, 2001
Essential Role of the NADPH Oxidase Subunit p47phox in Endothelial Cell Superoxide Production in Response to Phorbol Ester and Tumor Necrosis Factor-
From the Department of Cardiology (J.-M.L., A.M.S., S.Y., A.M.S.), Guy's King's & St Thomas' School of Medicine (Denmark Hill Campus), King's College London, London, UK; the Department of Medicine (F.W.), University College London, UK; and the Molecular Immunology Unit (G.Y.B., A.J.T.), Institute of Child Health, London, UK.
* To whom correspondence should be addressed. E-mail: ajay.shah{at}kcl.ac.uk.
A phagocyte-type NADPH oxidase complex is a major source of endothelial reactive oxygen species (ROS) production, but its biochemical function and regulation remain unclear. In neutrophils, the p47phox subunit is centrally involved in oxidase activation in response to agonists such as phorbol-12-myristate-13-acetate (PMA). We investigated the role of p47phox in endothelial cell ROS production in response to PMA or tumor necrosis factor- (TNF) stimulation. To specifically address the role of p47phox, we studied coronary microvascular endothelial cells (CMECs) isolated from p47phox-/- mice and wild-type controls. p47phox was absent in hearts of knockout mice whereas the essential oxidase subunit, p22phox, was expressed in both groups. In the absence of agonist stimulation, the lack of p47phox did not result in a reduction in NADPH-dependent ROS production in p47phox-/- CMECs compared with wild-type CMECs. Prestimulation with PMA (100 ng/mL) or TNF (100 U/mL) for 10 minutes significantly increased NADPH-dependent O2- production in wild-type CMECs, assessed either by lucigenin (5 µmol/L) chemiluminescence or dichlorohydrofluorescein (DCF) fluorescence. This response was completely lost in p47phox-/- cells. Transfection of the full-length p47phox cDNA into p47phox-/- CMECs caused expression of p47phox protein and restoration of the O2- response to PMA and TNF. In wild-type CMECs, transfection of antisense p47phox cDNA substantially reduced p47phox expression and caused loss of the O2- response to PMA and TNF. These data show that endothelial cell p47phox is critical in the upregulation of NADPH oxidase activity by PMA and TNF.
Key words: knockout mice • p47phox • endothelial cells • NADPH oxidase • reactive oxygen species
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