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1 Departments of Pathology, VU Medical Center, Amsterdam, The Netherlands; ICaR-VU, VU Medical Center, Amsterdam, The Netherlands; Department of Molecular and Experimental Medicine, The Scripps Research Institute, Ja Lolla, USA
2 Department of Physiology, VU medical Center, Amsterdam, The Netherlands; ICaR-VU, VU Medical Center, Amsterdam, The Netherlands
3 Departments of Pathology, VU Medical Center, Amsterdam, The Netherlands
4 Department of Cardiology, VU Medical Center, Amsterdam, The Netherlands; ICaR-VU, VU Medical Center, Amsterdam, The Netherlands
5 Department of Gynaecology, VU Medical Center, Amsterdam, The Neterlands
6 Department of Molecular and Experimental Medicine, The Scripps Research Institute, Ja Lolla, USA
7 Department of Clinical Chemistry, VU Medical Center, Amsterdam, The Netherlands; ICaR-VU, VU Medical Center, Amsterdam, The Netherlands; Department of Immunopathology, Sanquin Research at CLB, Amsterdam, The Netherlands
8 Departments of Pathology, VU Medical Center, Amsterdam, The Netherlands; ICaR-VU, VU Medical Center, Amsterdam, The Netherlands
* To whom correspondence should be addressed. E-mail: jwm.niessen{at}vumc.nl.
Type II secretory phospholipase A2 (sPLA2) is a cardiovascular risk factor. We recently found depositions of sPLA2 in the necrotic center of infarcted human myocardium as well as to normally appearing cardiomyocytes adjacent to the borderzone. The consequences of binding of sPLA2 to ischemic cardiomyocytes are not known. To explore a potential effect of sPLA2 on ischemic cardiomyocytes at a cellular level we used an in vitro model. The cardiomyocyte cell-line H9c2 or adult cardiomyocytes isolated from rabbits were incubated with sPLA2 in the presence of metabolic inhibitors to mimick ischemia/reperfusion conditions. Cell viability was established using annexin V and propidium iodide or 7AAD. Metabolic inhibition induced an increase of the number of flip-flopped cells, including a population that did not stain with propidium iodide and that was caspase-3 negative. sPLA2 bound to the flip-flopped cells, including those negative for caspase-3. Binding of sPLA2 induced cell death in these latter cells. In addition, sPLA2 potentiated the binding of C-reactive protein (CRP) to these cells. We conclude that by binding to flip-flopped cardiomyocytes, including those that are caspase-3-negative and presumably reversibly injured, sPLA2 may induce cell death and tag these cells with CRP.
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