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Vol. 63, Issue 2, 325-331, February 2003
Division of Cardiology, Emory University School of Medicine,
Atlanta, Georgia (H.C., M.E.D., D.G.H., S.C.D.); and Atlanta Veterans
Administration Medical Center, Atlanta, Georgia (Z.L., W.K., D.G.H.,
S.C.D.)
Hydrogen peroxide mediates vasodilation, but the mechanisms responsible
for this process remain undefined. We examined the effect of
H2O2 on nitric oxide (NO·)
production and the signaling events involved. NO· release from
bovine aortic endothelial cells was detected with an
NO·-specific microelectrode. The addition of
H2O2 caused a potent dose-dependent increase in
NO· production. This was partially Ca2+-dependent
because BAPTA/AM reduced NO· production at low (<50 µM) but
not high (>100 µM) concentrations of H2O2.
Phosphatidylinositol (PI) 3-kinase inhibition [with wortmannin or
2-(4-morpholinyl)-8-phenyl-1(4H)-benzopyran-4-one hydrochloride], infection with a dominant-negative mutant of Akt, or mitogen-activated protein kinase kinase/extracellular signal-regulated kinase 1/2 (MEK/ERK1/2) inhibition (with PD98059 or U0126) partially attenuated, whereas inhibition of both PI 3-kinase and MEK1/2 abolished
H2O2-dependent NO· production. ERK1/2
seemed necessary for NO· production early (<5 min) after
H2O2 addition, whereas PI 3-kinase/Akt was more
important at later time points. Phosphorylation of endothelial nitric-oxide synthase (eNOS) at serine 1179 was observed >10 min after
the addition of H2O2, and this was prevented by
wortmannin but not by PD98059. c-Src family tyrosine kinase(s) was
found to be upstream of H2O2-dependent Akt and
eNOS serine 1179 phosphorylation and subsequent NO· production.
In summary, H2O2 causes endothelial NO·
release mediated by cooperative effects between PI
3-kinase/Akt-dependent eNOS serine 1179 phosphorylation and activation
of MEK/ERK1/2. This may represent an acute cellular adaptation to an
increase in oxidant stress.
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