Caspase inhibition and N6-benzyladenosine-induced apoptosis in HL-60 cells. |
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Authors: | P Mlejnek |
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Institution: | Institute of Botany and Plant Physiology, Mendel University of Agriculture and Forestry Brno, Zemìdìlská 1, 613 00 Brno, Czech Republic. mlejnek@mendelu.cz |
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Abstract: | As an extension of our recently published work (Mlejnek and Kuglík 2000] J. Cell. Biochem. 77:6-17), the role of caspases in N(6)-benzylaminopurine riboside (BAPR)-induced apotosis in HL-60 cells was evaluated in this study. Here, BAPR-induced apoptosis was accompanied by activation of caspase-3 and caspase-9. However, when these caspases were selectively inhibited, the progression of BAPR-induced apoptosis was not markedly affected. Besides that, activation of caspase-3 and caspase-9 was found to be rather late event in apoptotic process. These results suggested that other caspases might be critically implicated. Indeed, pan-specific caspase inhibitor, Z-VAD-FMK, completely prevented DNA cleavage and apoptotic bodies formation. However, Z-VAD-FMK failed to prevent cell death and it was incapable to fully counteract the main apoptotic hallmark-chromatin condensation. Finally, our data indicate that cellular decision between apoptosis and necrosis is made upon the availability of both caspase proteases and intracellular ATP. |
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Keywords: | caspase‐3 caspase‐9 Ac‐LEHD‐CMK Z‐DEVD‐FMK Z‐VAD‐FMK cell death N6‐benzylaaminopurine riboside nuclear apotosis |
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