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(Arteriosclerosis, Thrombosis, and Vascular Biology. 2004;24:625.)
© 2004 American Heart Association, Inc.

Editorials

Subcellular Localization of Nox-Containing Oxidases Provides Unique Insight Into Their Role in Vascular Oxidant Signaling

Michael S. Wolin

From the Department of Physiology, New York Medical College, Valhalla, NY.

Correspondence to Michael S. Wolin, PhD, Department of Physiology, New York Medical College, Valhalla, NY 10595. E-mail mike wolin@nymc.edu

An extract of the first 250 words of the full text is provided, because this article has no abstract.

Originally, reactive oxygen species (ROS) were thought to be key participants in cellular injury. However, it is rapidly becoming realized that many of the individual species, such as hydrogen peroxide, are important mediators in a diverse array of cellular signaling processes. These processes include physiological regulation associated with the cellular sensing of oxygen tension, forces derived from stretch and shear, the control of cellular growth, and death.^1–4 One of the most active areas under investigation in cellular regulation is the subcellular localization and organization of signaling mechanisms. In the article in this issue of Atherosclerosis, Thrombosis, and Vascular Biology,⁵ Hilenski and colleagues provide the first report on the subcellular localization of the Nox-1 and Nox-4 subunit–containing NAD(P)H oxidases in vascular smooth muscle cells on caveolae and focal adhesions, respectively. These observations have important implications for the organization of oxidant signaling mechanisms thought to be involved in the control of fundamental physiological processes, including the role of Nox-1 expression in promoting cell growth^3–5 and roles for Nox oxidase activation by p47phox subunit binding in the sensing of cellular stretch forces.⁶

See page 677

Redox Control by Each Nox Is Likely to Be Localized

Localization of ROS-producing oxidases influences the function of both the signaling mechanisms, which activate the specific oxidases, and the regulatory pathways they control. Because there appear to be specific mechanisms of activation for the individual oxidases that may depend on processes such as the binding of subunits including p47phox and rac,^3–5 there need to be ways to control the activation mechanisms for these systems in the subcellular . . . [Full Text of this Article]

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