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(Circulation Research. 2009;104:147.)
© 2009 American Heart Association, Inc.

Editorials

NADPH Oxidase in Vascular Injury

A New Insight About Its Regulation and Role in T Cells

Jun-ichi Abe, Chang-Hoon Woo

From the Aab Cardiovascular Research Institute, University of Rochester, Rochester, NY 14642.

Correspondence to Send correspondence to: Jun-ichi Abe, M.D., Ph.D., F.A.H.A., Aab Cardiovascular Research Institute, 601 Elmwood Ave, Box CVRI, University of Rochester School of Medicine and Dentistry, Rochester, NY 14642. Phone: (585) 276-9794, Fax: (585) 276-9830, E-mail Jun-ichi_Abe@urmc.rochester.edu

See related articles, pages 189–200, 219–227

Key Words: NADPH oxidase • T cells • Rac • p47phox phosphorylation • neointimal formation

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

	Introduction

 
Vascular proliferative disorders and their subsequent vascular stenosis resulting from neointimal formation and vascular remodeling have a very relevant clinical effect, especially following percutaneous coronary interventions. In this editorial, we would like to briefly summarize the regulatory mechanism of NADPH oxidase and its role in T cells during the process of neointimal formation.

	Regulation of NADPH Oxidase Activity (Not Expression)

 
Many reports support the critical role of reactive oxygen species (ROS) in vascular injury. The signaling properties of ROS are largely attributable to the reversible oxidation of redox-sensitive target proteins, especially protein tyrosine phosphatases (PTPs). The PTP activity is dependent on the reactive cysteine residues (Cys-SH) that are readily susceptible to oxidation.¹ Oxidative inhibition of PTPs by molecules including PTP1B and SHP2 can increase phosphorylation and activation of many receptor tyrosine kinase.² Therefore, ROS production can be a very important mediator of signal transduction, because activation of receptor tyrosine kinase can initiate many signal transduction pathways. The balance between oxidases and antioxidant enzymes regulates ROS production. One of the prominent sources of vascular reactive oxygen species is NADPH oxidase and its cell-specific expression and localization may have a critical role in regulation of specific and unique ROS-mediated signal transduction pathways by "compartmentalization" of ROS production.² Therefore, the regulatory mechanism of NADPH oxidase "activation" is of great interest. NADPH oxidases consist of membrane-associated cytochrome b558 comprising of the catalytic gp91phox and regulatory p22phox subunits and cytosolic components including p47phox, p67phox, p40phox, and the small GTPase Rac in phagocytic cells. In nonphagocytic cells, several homologs of gp91phox(Nox2) including Nox1 . . . [Full Text of this Article]