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@article{1115291,
author = {Kolářová, Hana and Klinke, Anna and Kremserová, Silvie and Adam, Matti and Pekarová, Michaela and Baldus, Stephan and Eiserich, Jason P and Kubala, Lukáš},
article_location = {New York, NY, USA},
article_number = {August},
doi = {http://dx.doi.org/10.1016/j.freeradbiomed.2013.04.014},
keywords = {Platelets; Myeloperoxidase; Inflammation; Cardiovascular diseases; Hemostasis; Adhesion; Nitric oxide; Free radicals},
language = {eng},
issn = {0891-5849},
journal = {FREE RADICAL BIOLOGY AND MEDICINE},
title = {Myeloperoxidase induces the priming of platelets},
volume = {61},
year = {2013}
}
TY - JOUR
ID - 1115291
AU - Kolářová, Hana - Klinke, Anna - Kremserová, Silvie - Adam, Matti - Pekarová, Michaela - Baldus, Stephan - Eiserich, Jason P - Kubala, Lukáš
PY - 2013
TI - Myeloperoxidase induces the priming of platelets
JF - FREE RADICAL BIOLOGY AND MEDICINE
VL - 61
IS - August
SP - 357-369
EP - 357-369
PB - ELSEVIER SCIENCE INC
SN - 08915849
KW - Platelets
KW - Myeloperoxidase
KW - Inflammation
KW - Cardiovascular diseases
KW - Hemostasis
KW - Adhesion
KW - Nitric oxide
KW - Free radicals
N2 - The release of myeloperoxidase (MPO) from polymorphonuclear neutrophils is a hallmark of vascular inflammation and contributes to the pathogenesis of vascular inflammatory processes. However, the effects of MPO on platelets as a contributory mechanism in vascular inflammatory diseases remain unknown. Thus, MPO interaction with platelets and its effects on platelet function were examined. First, dose-dependent binding of MPO (between 1.7 and 13.8 nM) to both human and mouse platelets was observed. This was in direct contrast to the absence of MPO in megakaryocytes. MPO was localized both on the surface of and inside platelets. Cytoskeleton inhibition did not prevent MPO localization inside the three-dimensional platelet structure. MPO peroxidase activity was preserved upon the MPO binding to platelets. MPO sequestered in platelets catabolized NO, documented by the decreased production of NO (on average, an approximately 2-fold decrease). MPO treatment did not affect the viability of platelets during short incubations; however, it decreased platelet viability after long-term storage for 7 days (an approximately 2-fold decrease). The activation of platelets by MPO was documented by an MPO-mediated increase in the expression of surface platelet receptors P-selectin and PECAM-1 (of about 5 to 20%) and the increased formation of reactive oxygen species (of about 15 to 200%). However, the activation was only partial, as MPO did not induce the aggregation of platelets nor potentiate platelet response to classical activators. Nor did MPO induce a significant release of the content of granules. The activation of platelets by MPO was connected with increased MPO-treated platelet interaction with polymorphonuclear leukocytes (an approximately 1.2-fold increase) in vitro. In conclusion, it can be suggested that MPO can interact with and activate platelets, which can induce priming of platelets, rather than the classical robust activation of platelets. This can contribute to the development of chronic inflammatory processes in vessels
ER -
KOLÁŘOVÁ, Hana, Anna KLINKE, Silvie KREMSEROVÁ, Matti ADAM, Michaela PEKAROVÁ, Stephan BALDUS, Jason P EISERICH a Lukáš KUBALA. Myeloperoxidase induces the priming of platelets. \textit{FREE RADICAL BIOLOGY AND MEDICINE}. New York, NY, USA: ELSEVIER SCIENCE INC, 2013, roč.~61, August, s.~357-369. ISSN~0891-5849. doi:10.1016/j.freeradbiomed.2013.04.014.
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