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J. Biol. Chem., Vol. 278, Issue 14, 12094-12100, April 4, 2003
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From the Department of Cardiology, Guy's, King's, and St.
Thomas's School of Medicine, King's College London, Bessemer
Road, London SE5 9PJ, United Kingdom
Endothelial cells express a constitutively active
phagocyte-type NADPH oxidase whose activity is augmented by agonists
such as angiotensin II. We recently reported (Li, J.-M., and Shah, A. M. (2002) J. Biol. Chem. 277, 19952-19960) that in
contrast to neutrophils a substantial proportion of the NADPH oxidase
in unstimulated endothelial cells exists as preassembled intracellular complexes. Here, we investigate the mechanism of angiotensin II-induced endothelial NADPH oxidase activation. Angiotensin II (100 nmol/liter)-induced reactive oxygen species production (as measured
by dichlorohydrofluorescein fluorescence or lucigenin
chemiluminescence) was completely absent in coronary microvascular
endothelial cells isolated from p47phox
knockout mice. Transfection of p47phox
cDNA into p47phox
Mechanism of Endothelial Cell NADPH Oxidase Activation by
Angiotensin II
ROLE OF THE p47phox SUBUNIT*
/ cells restored the
angiotensin II response, whereas transfection of antisense
p47phox cDNA into wild-type cells depleted
p47phox and inhibited the angiotensin II
response. In unstimulated human microvascular endothelial cells,
there was significant
p47phox-p22phox complex
formation but minimal detectable p47phox
phosphorylation. Angiotensin II induced rapid serine
phosphorylation of p47phox (within 1 min,
peaking at ~15 min), a 1.9 ± 0.1-fold increase in
p47phox-p22phox complex
formation and a 1.6 ± 0.2-fold increase in
NADPH-dependent O
*
This work was supported by British Heart Foundation (BHF)
Program Grant RG/98008.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Holds the BHF Chair of Cardiology in King's College London. To
whom correspondence should be addressed. Tel.: 44-207-346-3865; Fax:
44-207-346-4771; E-mail: ajay.shah@kcl.ac.uk.
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