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Science 28 June 2002:
Vol. 296. no. 5577, pp. 2391 - 2394
DOI: 10.1126/science.1106830
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Reports

Myeloperoxidase, a Leukocyte-Derived Vascular NO Oxidase

Jason P. Eiserich,123*dagger Stephan Baldus,23*ddagger Marie-Luise Brennan,6 Wenxin Ma,4 Chunxiang Zhang,4 Albert Tousson,5 Laura Castro,23 Aldons J. Lusis,6 William M. Nauseef,7 C. Roger White,34 Bruce A. Freeman23dagger

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 and vasodilatory functions of nitric oxide (NO) during acute inflammation. After leukocyte degranulation, MPO localized in and around vascular endothelial cells in a rodent model of acute endotoxemia and impaired endothelium-dependent relaxant responses, to which MPO-deficient mice were resistant. Altered vascular responsiveness was due to catalytic consumption of NO by substrate radicals generated by MPO. Thus MPO can directly modulate vascular inflammatory responses by 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.

dagger    To whom correspondence should be addressed. E-mail: jpeiserich{at}ucdavis.edu or bruce.freeman{at}ccc.uab.edu

ddagger    Present address: Department of Cardiology, University Hospital Eppendorf, Hamburg, Germany.

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Nitric Oxide-dependent Generation of Reactive Species in Sickle Cell Disease. ACTIN TYROSINE NITRATION INDUCES DEFECTIVE CYTOSKELETAL POLYMERIZATION.
M. Aslan, T. M. Ryan, T. M. Townes, L. Coward, M. C. Kirk, S. Barnes, C. B. Alexander, S. S. Rosenfeld, and B. A. Freeman (2003)
J. Biol. Chem. 278, 4194-4204
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Nitrolinoleate, a nitric oxide-derived mediator of cell function: Synthesis, characterization, and vasomotor activity.
D. G. Lim, S. Sweeney, A. Bloodsworth, C. R. White, P. H. Chumley, N. R. Krishna, F. Schopfer, V. B. O'Donnell, J. P. Eiserich, and B. A. Freeman (2002)
PNAS 99, 15941-15946
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Myeloperoxidase Functions as a Major Enzymatic Catalyst for Initiation of Lipid Peroxidation at Sites of Inflammation.
R. Zhang, M.-L. Brennan, Z. Shen, J. C. MacPherson, D. Schmitt, C. E. Molenda, and S. L. Hazen (2002)
J. Biol. Chem. 277, 46116-46122
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Characterization of Nitric Oxide Consumption Pathways by Normal, Chronic Granulomatous Disease and Myeloperoxidase-Deficient Human Neutrophils.
S. R. Clark, M. J. Coffey, R. M. Maclean, P. W. Collins, M. J. Lewis, A. R. Cross, and V. B. O'Donnell (2002)
J. Immunol. 169, 5889-5896
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