Myeloperoxidase induces the priming of platelets

0394796 - BFÚ 2014 RIV US eng J - Článek v odborném periodiku
Kolářová, Hana - Klinke, A. - Kremserová, Silvie - Adam, M. - Pekarová, Michaela - Baldus, S. - Eiserich, J.P. - Kubala, Lukáš
Myeloperoxidase induces the priming of platelets.
Free Radical Biology and Medicine. Roč. 61, AUG 2013 (2013), s. 357-369. ISSN 0891-5849. E-ISSN 1873-4596
Grant CEP: GA ČR(CZ) GCP305/12/J038
Institucionální podpora: RVO:68081707
Klíčová slova: ACUTE CORONARY SYNDROMES * NITRIC-OXIDE * REACTIVE OXYGEN
Kód oboru RIV: BO - Biofyzika
Impakt faktor: 5.710, rok: 2013

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).
Trvalý link: http://hdl.handle.net/11104/0222966