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Myeloperoxidase enhances nitric oxide catabolism during myocardial ischemia and reperfusion

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Myeloperoxidase enhances nitric oxide catabolism during myocardial ischemia and reperfusion. / Baldus, Stephan; Heitzer, Thomas; Eiserich, Jason P; Lau, Denise; Mollnau, Hanke; Ortak, Michelle; Petri, Susan; Goldmann, Britta; Duchstein, Hans-Jürgen; Berger, Jürgen; Helmchen, Udo; Freeman, Bruce A; Meinertz, Thomas; Münzel, Thomas.

In: FREE RADICAL BIO MED, Vol. 37, No. 6, 15.09.2004, p. 902-911.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Baldus, S, Heitzer, T, Eiserich, JP, Lau, D, Mollnau, H, Ortak, M, Petri, S, Goldmann, B, Duchstein, H-J, Berger, J, Helmchen, U, Freeman, BA, Meinertz, T & Münzel, T 2004, 'Myeloperoxidase enhances nitric oxide catabolism during myocardial ischemia and reperfusion', FREE RADICAL BIO MED, vol. 37, no. 6, pp. 902-911. https://doi.org/10.1016/j.freeradbiomed.2004.06.003

APA

Baldus, S., Heitzer, T., Eiserich, J. P., Lau, D., Mollnau, H., Ortak, M., Petri, S., Goldmann, B., Duchstein, H-J., Berger, J., Helmchen, U., Freeman, B. A., Meinertz, T., & Münzel, T. (2004). Myeloperoxidase enhances nitric oxide catabolism during myocardial ischemia and reperfusion. FREE RADICAL BIO MED, 37(6), 902-911. https://doi.org/10.1016/j.freeradbiomed.2004.06.003

Vancouver

Baldus S, Heitzer T, Eiserich JP, Lau D, Mollnau H, Ortak M et al. Myeloperoxidase enhances nitric oxide catabolism during myocardial ischemia and reperfusion. FREE RADICAL BIO MED. 2004 Sep 15;37(6):902-911. https://doi.org/10.1016/j.freeradbiomed.2004.06.003

Bibtex

@article{0d85829cfb884956b9cca952444b6245,
title = "Myeloperoxidase enhances nitric oxide catabolism during myocardial ischemia and reperfusion",
abstract = "Impaired microvascular function during myocardial ischemia and reperfusion is associated with recruitment of polymorphonuclear neutrophils (PMN) and has been attributed to decreased bioavailability of nitric oxide (NO). Whereas myeloperoxidase (MPO), a highly abundant, PMN-derived heme protein facilitates oxidative NO consumption and impairs vascular function in animal models of acute inflammation, its capacity to function in this regard during human myocardial ischemia and reperfusion remains unknown. Plasma samples from 30 consecutive patients (61 +/- 14 years, 80% male) presenting with acute myocardial infarction were collected 9 +/- 4 h after vessel recanalization and compared to plasma from healthy control subjects (n = 12). Plasma levels of MPO were higher in patients than in control subjects (1.4 +/- 0.9 vs 0.3 +/- 0.2 ng/mg protein, respectively, p < 0.0001). The addition of hydrogen peroxide to patient plasma resulted in accelerated rates of NO consumption compared to control subjects (0.53 +/- 0.25 vs 0.068 +/- 0.039 nM/s/mg protein, respectively, p < 0.0001). Myocardial tissue from patients with the same pathology revealed intense recruitment of MPO-positive PMN localized along infarct-related vessels as well as diffuse endothelial distribution of non-PMN-associated MPO immunoreactivity. Endothelium-dependent microvascular function, as assessed by an acetylcholine-dependent increase in forearm blood flow in 75 patients with symptomatic coronary artery disease, inversely correlated with MPO plasma levels (r = -0.75, p < 0.005). Plasma from patients undergoing myocardial reperfusion contained increased levels of MPO, which catalytically consumed NO in the presence of H(2)O(2). Given the correlation between intravascular MPO levels and forearm vasomotor function in patients with coronary artery disease, MPO appears to be an important modulator of vasomotor function in inflammatory vascular disease and a potential therapeutic target for treatment.",
keywords = "Aged, Animals, Case-Control Studies, Enzyme-Linked Immunosorbent Assay, Female, Heme/chemistry, Humans, Hydrogen Peroxide/pharmacology, Immunohistochemistry, Male, Middle Aged, Models, Biological, Myocardial Infarction/blood, Myocardial Ischemia/pathology, Myocardium/pathology, Neutrophils/metabolism, Nitric Oxide/metabolism, Peroxidase/chemistry, Platelet Endothelial Cell Adhesion Molecule-1/chemistry, Rabbits, Regional Blood Flow, Reperfusion, Reperfusion Injury, Time Factors",
author = "Stephan Baldus and Thomas Heitzer and Eiserich, {Jason P} and Denise Lau and Hanke Mollnau and Michelle Ortak and Susan Petri and Britta Goldmann and Hans-J{\"u}rgen Duchstein and J{\"u}rgen Berger and Udo Helmchen and Freeman, {Bruce A} and Thomas Meinertz and Thomas M{\"u}nzel",
year = "2004",
month = sep,
day = "15",
doi = "10.1016/j.freeradbiomed.2004.06.003",
language = "English",
volume = "37",
pages = "902--911",
journal = "FREE RADICAL BIO MED",
issn = "0891-5849",
publisher = "Elsevier Inc.",
number = "6",

}

RIS

TY - JOUR

T1 - Myeloperoxidase enhances nitric oxide catabolism during myocardial ischemia and reperfusion

AU - Baldus, Stephan

AU - Heitzer, Thomas

AU - Eiserich, Jason P

AU - Lau, Denise

AU - Mollnau, Hanke

AU - Ortak, Michelle

AU - Petri, Susan

AU - Goldmann, Britta

AU - Duchstein, Hans-Jürgen

AU - Berger, Jürgen

AU - Helmchen, Udo

AU - Freeman, Bruce A

AU - Meinertz, Thomas

AU - Münzel, Thomas

PY - 2004/9/15

Y1 - 2004/9/15

N2 - Impaired microvascular function during myocardial ischemia and reperfusion is associated with recruitment of polymorphonuclear neutrophils (PMN) and has been attributed to decreased bioavailability of nitric oxide (NO). Whereas myeloperoxidase (MPO), a highly abundant, PMN-derived heme protein facilitates oxidative NO consumption and impairs vascular function in animal models of acute inflammation, its capacity to function in this regard during human myocardial ischemia and reperfusion remains unknown. Plasma samples from 30 consecutive patients (61 +/- 14 years, 80% male) presenting with acute myocardial infarction were collected 9 +/- 4 h after vessel recanalization and compared to plasma from healthy control subjects (n = 12). Plasma levels of MPO were higher in patients than in control subjects (1.4 +/- 0.9 vs 0.3 +/- 0.2 ng/mg protein, respectively, p < 0.0001). The addition of hydrogen peroxide to patient plasma resulted in accelerated rates of NO consumption compared to control subjects (0.53 +/- 0.25 vs 0.068 +/- 0.039 nM/s/mg protein, respectively, p < 0.0001). Myocardial tissue from patients with the same pathology revealed intense recruitment of MPO-positive PMN localized along infarct-related vessels as well as diffuse endothelial distribution of non-PMN-associated MPO immunoreactivity. Endothelium-dependent microvascular function, as assessed by an acetylcholine-dependent increase in forearm blood flow in 75 patients with symptomatic coronary artery disease, inversely correlated with MPO plasma levels (r = -0.75, p < 0.005). Plasma from patients undergoing myocardial reperfusion contained increased levels of MPO, which catalytically consumed NO in the presence of H(2)O(2). Given the correlation between intravascular MPO levels and forearm vasomotor function in patients with coronary artery disease, MPO appears to be an important modulator of vasomotor function in inflammatory vascular disease and a potential therapeutic target for treatment.

AB - Impaired microvascular function during myocardial ischemia and reperfusion is associated with recruitment of polymorphonuclear neutrophils (PMN) and has been attributed to decreased bioavailability of nitric oxide (NO). Whereas myeloperoxidase (MPO), a highly abundant, PMN-derived heme protein facilitates oxidative NO consumption and impairs vascular function in animal models of acute inflammation, its capacity to function in this regard during human myocardial ischemia and reperfusion remains unknown. Plasma samples from 30 consecutive patients (61 +/- 14 years, 80% male) presenting with acute myocardial infarction were collected 9 +/- 4 h after vessel recanalization and compared to plasma from healthy control subjects (n = 12). Plasma levels of MPO were higher in patients than in control subjects (1.4 +/- 0.9 vs 0.3 +/- 0.2 ng/mg protein, respectively, p < 0.0001). The addition of hydrogen peroxide to patient plasma resulted in accelerated rates of NO consumption compared to control subjects (0.53 +/- 0.25 vs 0.068 +/- 0.039 nM/s/mg protein, respectively, p < 0.0001). Myocardial tissue from patients with the same pathology revealed intense recruitment of MPO-positive PMN localized along infarct-related vessels as well as diffuse endothelial distribution of non-PMN-associated MPO immunoreactivity. Endothelium-dependent microvascular function, as assessed by an acetylcholine-dependent increase in forearm blood flow in 75 patients with symptomatic coronary artery disease, inversely correlated with MPO plasma levels (r = -0.75, p < 0.005). Plasma from patients undergoing myocardial reperfusion contained increased levels of MPO, which catalytically consumed NO in the presence of H(2)O(2). Given the correlation between intravascular MPO levels and forearm vasomotor function in patients with coronary artery disease, MPO appears to be an important modulator of vasomotor function in inflammatory vascular disease and a potential therapeutic target for treatment.

KW - Aged

KW - Animals

KW - Case-Control Studies

KW - Enzyme-Linked Immunosorbent Assay

KW - Female

KW - Heme/chemistry

KW - Humans

KW - Hydrogen Peroxide/pharmacology

KW - Immunohistochemistry

KW - Male

KW - Middle Aged

KW - Models, Biological

KW - Myocardial Infarction/blood

KW - Myocardial Ischemia/pathology

KW - Myocardium/pathology

KW - Neutrophils/metabolism

KW - Nitric Oxide/metabolism

KW - Peroxidase/chemistry

KW - Platelet Endothelial Cell Adhesion Molecule-1/chemistry

KW - Rabbits

KW - Regional Blood Flow

KW - Reperfusion

KW - Reperfusion Injury

KW - Time Factors

U2 - 10.1016/j.freeradbiomed.2004.06.003

DO - 10.1016/j.freeradbiomed.2004.06.003

M3 - SCORING: Journal article

C2 - 15304260

VL - 37

SP - 902

EP - 911

JO - FREE RADICAL BIO MED

JF - FREE RADICAL BIO MED

SN - 0891-5849

IS - 6

ER -