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Department of Physiological Sciences, Eastern Virginia Medical School, Norfolk, Virginia 23501
Extracellular signal-regulated kinases (ERK) and
mitogen-activated protein (MAP) kinases participate in cell signaling,
regulating cell growth. In differentiated cells, the role ERK plays is
less well known. This study quantified the degree of basal and
stimulated ERK phosphorylation and contraction in freshly isolated
arteries. The level of basal ERK phosphorylation was identical in
preloaded and slack arteries, was greater in media than in the whole
artery, and was reduced by the MAP or ERK kinase (MEK) inhibitor
PD-98059. Chemical denudation using
1H-[1,2,4]oxadiazolo[4,3-a]quinoxalin-1-one did not elevate basal ERK phosphorylation. PD-98059 reduced maximum phenylephrine (PE)-stimulated ERK phosphorylation but not force. Pervanadate elevated ERK phosphorylation without causing contraction. Contractions produced by PE and relaxations produced by PE washout preceded the ERK phosphorylation. K+ depolarization, muscle
stretch, and angiotensin II elevated ERK phosphorylation transiently,
whereas PE maintained ERK phosphorylation for 30 min. The
1A-adrenergic receptor antagonist WB-4101 reduced PE-stimulated force by 70% and abolished PE-induced ERK
phosphorylation. Afterloaded and zero-load contractions produced by
K+ depolarization displayed identical increases in ERK
phosphorylation. These data indicate that ERK was active basally in the
differentiated artery but regulated by the endothelium and that ERK
phosphorylation was not load dependent. A strong correlation between
PE-induced force and ERK phosphorylation supports the hypothesis that
ERK activation may reflect a signal "notifying" the cell of the
degree of 1-adrenergic receptor-induced contraction.
extracellular signal-regulated kinase; mitogen-activated protein kinase; femoral artery; isometric force; vascular smooth muscle; ODQ; VASP
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