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Am J Physiol Heart Circ Physiol 281: H1637-H1647, 2001;
0363-6135/01 $5.00
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Vol. 281, Issue 4, H1637-H1647, October 2001

Important role of energy-dependent mitochondrial pathways in cultured rat cardiac myocyte apoptosis

Jun Shiraishi1, Tetsuya Tatsumi1, Natsuya Keira1, Kazuko Akashi1, Akiko Mano1, Satoshi Yamanaka1, Satoaki Matoba1, Jun Asayama3, Takeshi Yaoi2, Shinji Fushiki2, Henry Fliss4, and Masao Nakagawa1

1 Second Department of Medicine and 2 Department of Dynamic Pathology, Kyoto Prefectural University of Medicine, Kyoto 602-8566; 3 Department of Clinical Pharmacology, Kyoto Pharmaceutical University, Kyoto 607-8414, Japan; and 4 Department of Cellular and Molecular Medicine, University of Ottawa, Ottawa, Ontario K1H 8M5, Canada

Recent studies have suggested that apoptosis and necrosis share common features in their signaling pathway and that apoptosis requires intracellular ATP for its mitochondrial/apoptotic protease-activating factor-1 suicide cascade. The present study was, therefore, designed to examine the role of intracellular energy levels in determining the form of cell death in cardiac myocytes. Neonatal rat cardiac myocytes were first incubated for 1 h in glucose-free medium containing oligomycin to achieve metabolic inhibition. The cells were then incubated for another 4 h in similar medium containing staurosporine and graded concentrations of glucose to manipulate intracellular ATP levels. Under ATP-depleting conditions, the cell death caused by staurosporine was primarily necrotic, as determined by creatine kinase release and nuclear staining with ethidium homodimer-1. However, under ATP-replenishing conditions, staurosporine increased the percentage of apoptotic cells, as determined by nuclear morphology and DNA fragmentation. Caspase-3 activation by staurosporine was also ATP dependent. However, loss of mitochondrial transmembrane potential (Delta Psi m), Bax translocation, and cytochrome c release were observed in both apoptotic and necrotic cells. Moreover, cyclosporin A, an inhibitor of mitochondrial permeability transition, attenuated staurosporine-induced apoptosis and necrosis through the inhibition of Delta Psi m reduction, cytochrome c release, and caspase-3 activation. Our data therefore suggest that staurosporine induces cell demise through a mitochondrial death signaling pathway and that the presence of intracellular ATP favors a shift from necrosis to apoptosis through caspase activation.

cytochrome c; mitochondria; necrosis; staurosporine


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