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• W2060275872 abstract "We examined the relative roles of the mitogen-activated protein kinases (MAPK) in mediating theα1 -adrenergic receptor (α1-AR) stimulated hypertrophic phenotype in adult rat ventricular myocytes (ARVM). Norepinephrine (NE; 1 μ) in the presence of the β -AR antagonist propranolol (Pro; 2 μ) caused activation of Ras (>six-fold), MAPK/ERK kinase 1 and 2 (MEK1/2, >10-fold) and extracellular signal-regulated kinases 1 and 2 (ERK1/2, ∼30-fold) within 5 min, as determined by kinase activity assays and Western blots using phospho-specific antibodies. Conversely, p38 and c-Jun amino-terminal kinases (JNK) were not activated by NE/Pro. Activated MEK1/2 signals remained detectable at 2 h, and activated ERK1/2 remained detectable at 48 h. The α1-AR selective inhibitor prazosin (100 n ) completely inhibited the NE/Pro-stimulated activation of Ras, MEK1/2 and ERK1/2. The MEK inhibitor PD98059 caused a concentration-dependent inhibition of NE/Pro-stimulated protein synthesis (as assessed by [3H]leucine incorporation and cellular protein accumulation) and ERK1/2 activation, with ∼50% inhibition at a concentration between 10 and 50μ , which is consistent with the known IC50values of PD98059 for MEK1 (4 μ) and MEK2 (50 μ). Thus, these data show that α1-AR stimulated hypertrophy in ARVM is dependent on the MEK1/2–ERK1/2 signaling pathway." @default.
• W2060275872 created "2016-06-24" @default.
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• W2060275872 date "2001-04-01" @default.
• W2060275872 modified "2023-10-15" @default.
• W2060275872 title "MEK1/2–ERK1/2 Mediates α1-Adrenergic Receptor-stimulated Hypertrophy in Adult Rat Ventricular Myocytes" @default.
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• W2060275872 doi "https://doi.org/10.1006/jmcc.2001.1348" @default.
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