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Myeloperoxidase, a Leukocyte-Derived Vascular NO Oxidase
Jason P. Eiserich,123*Stephan Baldus,23*Marie-Luise Brennan,6Wenxin Ma,4Chunxiang Zhang,4Albert Tousson,5Laura Castro,23Aldons J. Lusis,6William M. Nauseef,7C. Roger White,34Bruce A. Freeman23
Myeloperoxidase (MPO) is an abundant mammalian phagocyte
hemoprotein thought to primarily mediate host defense reactions.Although its microbicidal functions are well established in vitro,humans deficient in MPO are not at unusual risk of infection.MPO was
observed herein to modulate the vascular signaling andvasodilatory
functions of nitric oxide (NO) during acute inflammation.After
leukocyte degranulation, MPO localized in and around vascularendothelial cells in a rodent model of acute endotoxemia and impairedendothelium-dependent relaxant responses, to which MPO-deficientmice
were resistant. Altered vascular responsiveness was due tocatalytic
consumption of NO by substrate radicals generated byMPO. Thus MPO can
directly modulate vascular inflammatory responsesby regulating NO
bioavailability.
1 Department of Internal Medicine, Division of
Nephrology, and Department of Human Physiology, University of
California, Davis, CA 95616, USA.
2 Department of
Anesthesiology,
3 Center for Free Radical Biology,
4 Department of Medicine, and
5 Imaging Facility, University of Alabama,
Birmingham, AL 35233, USA.
6 Department of
Microbiology and Molecular Genetics and Department of Medicine,
University of California, Los Angeles, CA 90095, USA.
7 Department of Medicine and the Inflammation
Program, Veterans Administration Medical Center and University of Iowa,
Iowa City, IA 52242, USA.
*
These authors contributed equally to this work.
To whom correspondence should be addressed. E-mail:
jpeiserich{at}ucdavis.edu or bruce.freeman{at}ccc.uab.edu
Present address: Department of Cardiology, University
Hospital Eppendorf, Hamburg, Germany.
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