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Involvement of Reactive Oxygen Species in the Activation of Tyrosine Kinase and Extracellular Signal-Regulated Kinase by Angiotensin II¹

From the Department of Anatomy and Physiology (G.D.F., E.D.M.), Meharry Medical College, Nashville, Tennessee 37208; Department of Biochemistry (G.D.F., S.E., T.Y., T.I.), Vanderbilt University School of Medicine, Nashville, Tennessee 37232; and Neurobiology of Aging Laboratories (S-i.T.), Mt. Sinai School of Medicine, New York, New York 10029

Address all correspondence and requests for reprints to: Evangeline D. Motley, Department of Anatomy and Physiology, Meharry Medical College, Nashville, Tennessee 37208. E-mail: emotley{at}mmc.edu

Reactive oxygen species (ROS) have been proposed to mediate vascular hypertrophy induced by angiotensin II (Ang II). Recently, we and others have shown that growth-promoting signals by Ang II involve protein tyrosine kinase (PTK) and extracellular signal-regulated kinase (ERK). However, whether ROS contribute to the Ang II-induced PTK and/or ERK activation in vascular smooth muscle cells (VSMCs) remains largely unclear. Here, we have investigated the possible involvement of ROS in Ang II-induced PTK and ERK activation. In the presence of a NADH/NADPH oxidase inhibitor, diphenyleneiodonium (DPI) or an antioxidant, -tocopherol, Ang II-induced protein tyrosine phosphorylation of two major proteins (p120, p70) and ERK activation were markedly reduced, whereas ERK activation by epidermal growth factor was unaffected. DPI also inhibited Ang II-induced H₂O₂ production and PTK activation. In this regard, H₂O₂ and a membrane permeable thiol-oxidizing agent, diamide, stimulated protein tyrosine phosphorylation of p120 and p70, and ERK activation in VSMCs. H₂O₂ also enhanced PTK activity. From these data, we conclude that ROS play a critical role in the Ang II-induced PTK and ERK activation in VSMCs, thereby contributing to vascular growth associated with enhanced Ang II activity.

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