PortalPublikationenMyeloperoxidase attracts neutrophils by physical forces.

Myeloperoxidase attracts neutrophils by physical forces.

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Myeloperoxidase attracts neutrophils by physical forces. / Klinke, Anna; Nussbaum, Claudia; Kubala, Lukas; Friedrichs, Kai; Rudolph, Tanja Katharina; Rudolph, Volker; Paust, Hans-Joachim; Schröder, Christine; Benten, Daniel; Lau, Denise; Szöcs, Katalin; Furtmüller, Paul G; Heeringa, Peter; Sydow, Karsten; Duchstein, Hans-Jürgen; Ehmke, Heimo; Schumacher, Udo; Meinertz, Thomas; Sperandio, Markus; Baldus, Stephan.

in: BLOOD, Jahrgang 117, Nr. 4, 4, 2011, S. 1350-1358.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Klinke, A, Nussbaum, C, Kubala, L, Friedrichs, K, Rudolph, TK, Rudolph, V, Paust, H-J, Schröder, C, Benten, D, Lau, D, Szöcs, K, Furtmüller, PG, Heeringa, P, Sydow, K, Duchstein, H-J, Ehmke, H, Schumacher, U, Meinertz, T, Sperandio, M & Baldus, S 2011, 'Myeloperoxidase attracts neutrophils by physical forces.', BLOOD, Jg. 117, Nr. 4, 4, S. 1350-1358. https://doi.org/10.1182/blood-2010-05-284513

APA

Klinke, A., Nussbaum, C., Kubala, L., Friedrichs, K., Rudolph, T. K., Rudolph, V., Paust, H-J., Schröder, C., Benten, D., Lau, D., Szöcs, K., Furtmüller, P. G., Heeringa, P., Sydow, K., Duchstein, H-J., Ehmke, H., Schumacher, U., Meinertz, T., Sperandio, M., & Baldus, S. (2011). Myeloperoxidase attracts neutrophils by physical forces. BLOOD, 117(4), 1350-1358. [4]. https://doi.org/10.1182/blood-2010-05-284513

Vancouver

Klinke A, Nussbaum C, Kubala L, Friedrichs K, Rudolph TK, Rudolph V et al. Myeloperoxidase attracts neutrophils by physical forces. BLOOD. 2011;117(4):1350-1358. 4. https://doi.org/10.1182/blood-2010-05-284513

Bibtex

@article{befbb9788537416d9135ca5f2023724f,
title = "Myeloperoxidase attracts neutrophils by physical forces.",
abstract = "Recruitment of polymorphonuclear neutrophils (PMNs) remains a paramount prerequisite in innate immune defense and a critical cofounder in inflammatory vascular disease. Neutrophil recruitment comprises a cascade of concerted events allowing for capture, adhesion and extravasation of the leukocyte. Whereas PMN rolling, binding, and diapedesis are well characterized, receptor-mediated processes, mechanisms attenuating the electrostatic repulsion between the negatively charged glycocalyx of leukocyte and endothelium remain poorly understood. We provide evidence for myeloperoxidase (MPO), an abundant PMN-derived heme protein, facilitating PMN recruitment by its positive surface charge. In vitro, MPO evoked highly directed PMN motility, which was solely dependent on electrostatic interactions with the leukocyte's surface. In vivo, PMN recruitment was shown to be MPO-dependent in a model of hepatic ischemia and reperfusion, upon intraportal delivery of MPO and in the cremaster muscle exposed to local inflammation or to intraarterial MPO application. Given MPO's affinity to both the endothelial and the leukocyte's surface, MPO evolves as a mediator of PMN recruitment because of its positive surface charge. This electrostatic MPO effect not only displays a so far unrecognized, catalysis-independent function of the enzyme, but also highlights a principal mechanism of PMN attraction driven by physical forces.",
author = "Anna Klinke and Claudia Nussbaum and Lukas Kubala and Kai Friedrichs and Rudolph, {Tanja Katharina} and Volker Rudolph and Hans-Joachim Paust and Christine Schr{\"o}der and Daniel Benten and Denise Lau and Katalin Sz{\"o}cs and Furtm{\"u}ller, {Paul G} and Peter Heeringa and Karsten Sydow and Hans-J{\"u}rgen Duchstein and Heimo Ehmke and Udo Schumacher and Thomas Meinertz and Markus Sperandio and Stephan Baldus",
year = "2011",
doi = "10.1182/blood-2010-05-284513",
language = "English",
volume = "117",
pages = "1350--1358",
journal = "BLOOD",
issn = "0006-4971",
publisher = "American Society of Hematology",
number = "4",

}

RIS

TY - JOUR

T1 - Myeloperoxidase attracts neutrophils by physical forces.

AU - Klinke, Anna

AU - Nussbaum, Claudia

AU - Kubala, Lukas

AU - Friedrichs, Kai

AU - Rudolph, Tanja Katharina

AU - Rudolph, Volker

AU - Paust, Hans-Joachim

AU - Schröder, Christine

AU - Benten, Daniel

AU - Lau, Denise

AU - Szöcs, Katalin

AU - Furtmüller, Paul G

AU - Heeringa, Peter

AU - Sydow, Karsten

AU - Duchstein, Hans-Jürgen

AU - Ehmke, Heimo

AU - Schumacher, Udo

AU - Meinertz, Thomas

AU - Sperandio, Markus

AU - Baldus, Stephan

PY - 2011

Y1 - 2011

N2 - Recruitment of polymorphonuclear neutrophils (PMNs) remains a paramount prerequisite in innate immune defense and a critical cofounder in inflammatory vascular disease. Neutrophil recruitment comprises a cascade of concerted events allowing for capture, adhesion and extravasation of the leukocyte. Whereas PMN rolling, binding, and diapedesis are well characterized, receptor-mediated processes, mechanisms attenuating the electrostatic repulsion between the negatively charged glycocalyx of leukocyte and endothelium remain poorly understood. We provide evidence for myeloperoxidase (MPO), an abundant PMN-derived heme protein, facilitating PMN recruitment by its positive surface charge. In vitro, MPO evoked highly directed PMN motility, which was solely dependent on electrostatic interactions with the leukocyte's surface. In vivo, PMN recruitment was shown to be MPO-dependent in a model of hepatic ischemia and reperfusion, upon intraportal delivery of MPO and in the cremaster muscle exposed to local inflammation or to intraarterial MPO application. Given MPO's affinity to both the endothelial and the leukocyte's surface, MPO evolves as a mediator of PMN recruitment because of its positive surface charge. This electrostatic MPO effect not only displays a so far unrecognized, catalysis-independent function of the enzyme, but also highlights a principal mechanism of PMN attraction driven by physical forces.

AB - Recruitment of polymorphonuclear neutrophils (PMNs) remains a paramount prerequisite in innate immune defense and a critical cofounder in inflammatory vascular disease. Neutrophil recruitment comprises a cascade of concerted events allowing for capture, adhesion and extravasation of the leukocyte. Whereas PMN rolling, binding, and diapedesis are well characterized, receptor-mediated processes, mechanisms attenuating the electrostatic repulsion between the negatively charged glycocalyx of leukocyte and endothelium remain poorly understood. We provide evidence for myeloperoxidase (MPO), an abundant PMN-derived heme protein, facilitating PMN recruitment by its positive surface charge. In vitro, MPO evoked highly directed PMN motility, which was solely dependent on electrostatic interactions with the leukocyte's surface. In vivo, PMN recruitment was shown to be MPO-dependent in a model of hepatic ischemia and reperfusion, upon intraportal delivery of MPO and in the cremaster muscle exposed to local inflammation or to intraarterial MPO application. Given MPO's affinity to both the endothelial and the leukocyte's surface, MPO evolves as a mediator of PMN recruitment because of its positive surface charge. This electrostatic MPO effect not only displays a so far unrecognized, catalysis-independent function of the enzyme, but also highlights a principal mechanism of PMN attraction driven by physical forces.

U2 - 10.1182/blood-2010-05-284513

DO - 10.1182/blood-2010-05-284513

M3 - SCORING: Journal article

VL - 117

SP - 1350

EP - 1358

JO - BLOOD

JF - BLOOD

SN - 0006-4971

IS - 4

M1 - 4

ER -