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Am. J. Respir. Cell Mol. Biol., Volume 18, Number 4, April, 1998 562-569

Hydrogen Peroxide Activates Extracellular Signal-regulated Kinase via Protein Kinase C, Raf-1, and MEK1

Mark K. Abe, Sreedharan Kartha, Alla Y. Karpova, Jing Li, Pai T. Liu, Wen-Liang Kuo, and Marc B. Hershenson

Department of Pediatrics, Department of Pharmacological and Physiological Sciences, University of Chicago, Chicago, Illinois

We have previously demonstrated that hydrogen peroxide (H2O2) treatment of bovine tracheal myocytes increases the activity of extracellular signal-regulated kinases (ERK), serine/threonine kinases of the mitogen-activated protein (MAP) kinase superfamily thought to play a key role in the transduction of mitogenic signals to the cell nucleus. Moreover, H2O2-induced ERK activation was partially reduced by pretreatment with phorbol 12,13-dibutyrate, which depletes protein kinase C (PKC). In this study, we further examined the signaling intermediates responsible for ERK activation by H2O2 in airway smooth muscle, focusing on MAP kinase/ERK kinase (MEK), a dual-function kinase which is required and sufficient for ERK activation in bovine tracheal myocytes; Raf-1, a serine/threonine kinase known to activate MEK; and PKC. Pretreatment of cells with inhibitors of MEK (PD98059), Raf-1 (forskolin), and PKC (chelerythrine) each reduced H2O2-induced ERK activity. In addition, H2O2 treatment significantly increased both MEK1 and Raf-1 activity. No activation of MEK2 was detected. Together these data suggest that H2O2 may stimulate ERK via successive activation of PKC, Raf-1, and MEK1.




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