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J Biol Chem, Vol. 273, Issue 24, 15022-15029, June 12, 1998
From the Department of Medicine, Division of Cardiology, Emory
University, Atlanta, Georgia 30322
Angiotensin II induces an oxidant
stress-dependent hypertrophy in cultured vascular smooth
muscle cells. To investigate the growth-related molecular targets of
H2O2, we examined the redox sensitivity
of agonist-stimulated activation of the mitogen-activated protein
kinase (MAPK) family. We show here that angiotensin II elicits a rapid
increase in intracellular H2O2 and a rapid and robust phosphorylation of both p42/44MAPK (16-fold) and p38MAPK (15-fold). However, exogenous H2O2 activates
only p38MAPK (14-fold), and diphenylene iodonium, an NADH/NADPH oxidase
inhibitor, attenuates angiotensin II-stimulated phosphorylation of
p38MAPK, but not p42/44MAPK. Furthermore, in cells stably
transfected with human catalase, angiotensin II-induced
intracellular H2O2 generation is almost
completely blocked, resulting in inhibition of phosphorylation of
p38MAPK, but not p42/44MAPK, and a subsequent partial decrease in
angiotensin II-induced hypertrophy. Specific inhibition of either the
p38MAPK pathway with SB203580
(4-(4-fluorophenyl)-2-(4-methylsulfinylphenyl)-5-(4-pyridyl)1H-imidazole) or the p42/44MAPK pathway with PD98059
(2-(2'-amino-3'-methoxyphenyl)oxanaphthalen-4-one) also partially, but
significantly, attenuates angiotensin II-induced hypertrophy; however,
simultaneous blockade of both pathways has an additive inhibitory
effect, indicating that the hypertrophic response to angiotensin II
requires parallel, independent activation of both MAPK pathways. These
results provide the first evidence that p38MAPK is a critical component
of the oxidant stress (H2O2)-sensitive signaling pathways activated by angiotensin II in vascular smooth muscle cells and indicate that it plays a crucial role in vascular hypertrophy.
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