Medizinische Universität Graz Austria/Österreich - Forschungsportal - Medical University of Graz

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"Köpfe" der aktuellen Meldungen:

Nina Höller

Nariae Baik-Schneditz

Bernhard Schwaberger

Lukas Peter Mileder

Niels Hammer

Daniel Scherr

Gerhard Pichler

Roland Malli

Gewählte Publikation:

SHR Neuro Krebs Kardio Lipid Stoffw Microb

Curcic, S; Holzer, M; Pasterk, L; Knuplez, E; Eichmann, TO; Frank, S; Zimmermann, R; Schicho, R; Heinemann, A; Marsche, G.
Secretory phospholipase A₂ modified HDL rapidly and potently suppresses platelet activation.
Sci Rep. 2017; 7(1):8030-8030 Doi: 10.1038/s41598-017-08136-1 [OPEN ACCESS]
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Führende Autor*innen der Med Uni Graz: Curcic Sanja; Marsche Gunther
Co-Autor*innen der Med Uni Graz: Frank Sasa; Gruden Eva; Heinemann Akos; Holzer Michael; Pasterk Lisa; Schicho Rudolf
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Abstract:: Levels of secretory phospholipases A₂ (sPLA₂) highly increase under acute and chronic inflammatory conditions. sPLA₂ is mainly associated with high-density lipoproteins (HDL) and generates bioactive lysophospholipids implicated in acute and chronic inflammatory processes. Unexpectedly, pharmacological inhibition of sPLA₂ in patients with acute coronary syndrome was associated with an increased risk of myocardial infarction and stroke. Given that platelets are key players in thrombosis and inflammation, we hypothesized that sPLA₂-induced hydrolysis of HDL-associated phospholipids (sPLA₂-HDL) generates modified HDL particles that affect platelet function. We observed that sPLA₂-HDL potently and rapidly inhibited platelet aggregation induced by several agonists, P-selectin expression, GPIIb/IIIa activation and superoxide production, whereas native HDL showed little effects. sPLA₂-HDL suppressed the agonist-induced rise of intracellular Ca²⁺ levels and phosphorylation of Akt and ERK1/2, which trigger key steps in promoting platelet activation. Importantly, sPLA₂ in the absence of HDL showed no effects, whereas enrichment of HDL with lysophosphatidylcholines containing saturated fatty acids (the main sPLA₂ products) mimicked sPLA₂-HDL activities. Our findings suggest that sPLA₂ generates lysophosphatidylcholine-enriched HDL particles that modulate platelet function under inflammatory conditions.
Find related publications in this database (using NLM MeSH Indexing): Blood Platelets - cytology; Blood Platelets - metabolism; Cells, Cultured -; Humans -; Lipoproteins, HDL - metabolism; Mitogen-Activated Protein Kinase 1 - metabolism; Mitogen-Activated Protein Kinase 3 - metabolism; Phospholipases A2 - metabolism; Platelet Activation -; Platelet Glycoprotein GPIIb-IIIa Complex - metabolism; Selectins - metabolism