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(Circulation Research. 2002;90:123.)
© 2002 American Heart Association, Inc.

Editorials

Out Phoxing the Endothelium

What’s Left Without p47?

Bernard Lassègue, Kathy K. Griendling

From the Department of Medicine, Cardiology Division, Emory University, Atlanta, Ga.

Correspondence to Bernard Lassègue, Emory University, Division of Cardiology, 1639 Pierce Dr, 319 WMB, Atlanta, GA 30322. E-mail MEDBPL@emory.edu

Key Words: knockout mice • p47^phox • endothelial cells • NADPH oxidase • reactive oxygen species

The importance of the contribution from Li et al¹ presented in this issue lies as much in the questions it raises as in those it answers. In setting out to prove that p47^phox, a regulatory subunit of the phagocyte NADPH oxidase, is equally vital to the superoxide-generating enzyme of vascular endothelial cells, which they successfully did, they also turned up a number of unexpected observations. The latter results, whose interpretation will necessarily remain speculative for the time being, may become fertile ground for future investigations, not only of the endothelium, but also of other tissues that express variants of this enzyme complex first characterized in phagocytes.

In the neutrophil, the bactericidal oxidative burst results from massive superoxide anion production by an NADPH oxidase, a complex of 5 major subunits, the membrane bound gp91^phox and p22^phox, and the regulatory cytosolic components p47^phox, p67^phox, and Rac.² The importance of p47^phox is well documented because its phosphorylation appears to be the limiting step required for assembly of the active enzyme complex.² Furthermore, mutations in p47^phox are a cause of chronic granulomatous disease, an immune deficiency resulting from impaired phagocyte activity.

It is now clear that many other tissues, including all layers of the vascular wall, also produce superoxide and its derivatives.³ These reactive oxygen species are no longer regarded simply as undesirable by-products of aerobic metabolism but also as essential second messengers because they control the function of redox-sensitive signaling proteins. They also appear to be key factors in . . . [Full Text of this Article]

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